Index

Topic name Page number

1 A chemistry for Biologists: 1–31

1. Chemistry of life
2. Carbohydrates1
3. Carbohydrates 2
4. Lipids
5. Proteins
1 B Mammalian transport system: 32- 64
1. The principle of circulation
2. The role of Blood
3. Circulation in blood vessels
4. The mammalian heart
5. Atheroscelerosis
1 C cardiovascular health and risk: 65-85
1. Risk, correlation and cause
2. Investigating the cause of CVDs
3. Risk factors for cardiovascular disease.
4. Diet and cardiovascular health
5. Dietary antioxidants &cardiovascular disease.
6. Using evidence
7. Benefits and risks of treatment .
2 A Membrane, and transport : 86-118
1. Cell membrane
2. Cell transport and diffusion.
3. Osmosis
4. Active transport
5. Mammalian gas exchange system .
2 B proteins and DNA : 119-148
1. Enzymes
2. How enzymes work
3. The structure of DNA and RNA
4. How DNA works
5. The genetic code.
6. DNA and protein synthesis.
2 C Gene expression: 149-168
1. Gene mutation
2. Patterns of inheritance
3. Sex linkage
4. Cystic fibrosis
5. Genetic screening
Topic 2

Introduction to
Biological
molecules.

r
ab
Learning outcomes
lG
Description of how large
biological molecules are made
iha
from smaller molecules.
.N

Description of structure and

function of carbohydrates,
lipids and proteins.
Dr

Carrying out biochemical tests

to identify carbohydrates,
lipids and proteins.

Explaining of how some key

properties of water make life
possible.

001
 First: structure and function of carbohydrates, lipids
and Fats:
Macromolecules means giant molecules. There are 3 types of macromolecules in living organisms:
1. Polysaccharides
2. Protein(polypeptides)
3. Nucleic acids.
Polymer means they are made from many repeating subunits( monomers) that are similar or identical
to each other.
Lipid are not polymers yet made of simpler biochemicals.

Organic Amino Fatty acids

Monosaccharides
bases acids and glycerol

r
Monomer

ab
Polymer
Nucleotides
lG
Nucleic
Polysaccharides Proteins Lipids
iha
acids

A: Carbohydrates
.N
Dr

All carbohydrates contain the elements carbon, hydrogen and oxygen.

Hydrates=Hydrogen and oxygen which are present in a ratio 2:1 ( 2H to 1O) as in water.
General formula: Cx(H2O)y.
They are divided into three main groups :
Monosaccharides.
Disaccharides.
Polysaccharides.
The word saccharide refers to sugar or sweet substance.

002
 Monosaccharides Disaccharides Polysaccharides
Molecular (CH2O)n C12H22O11 (C6H10O5)n
formula

Definition Molecule consisting of a A sugar molecule consisting of Is a polymer whose

single sugar unit. two monosaccharides joined subunits are
together by a glycosidic bond. monosaccharides
joined together by
glycosidic bonds.
Examples [Link] when n= 3/(3C) Sucrose( glucose+ fructose) Starch
C3H6O3 Lactose( glucose+ galactose) Glycogen
Maltose ( glucose+ glucose) Cellulose
2. Pentoses when =5 (5C) Chitin
C5H10O5
Components of DNA (deoxyribose
sugar)&
RNA and ATP ( ribose sugar)

r
3. Hexoses when n=6/(6C)
C6H12O6

ab
As fructose, galactose, glucose
which are all used in
[Link] and energy lG
release due to the large
number of C-H bonds.
2. Used in formation of di
and poly saccharides.
iha
Reducing / All are reducing sugars with Lactose and Maltose are All non reducing
non reducing reducing ends reducing sugars sugars, with no
While sucrose is non reducing reducing ends.
sugars, with no reducing end.
.N

Water All water soluble All water soluble but less All water insoluble.
solubility readily soluble than
monosaccharides.
Dr

Taste Sweet Sweet Non sweet

Number of One Two rings More than 2 rings
rings

Powder Crystalline Not crystalline

Glycosidic
Absent✖ Present✔ Present✔
ring

Notice

003
 1- Monosaccharides(1A. )

Glucose
• Has 6 carbons, 6 oxygen and 12 hydrogen atoms ( C6H12O6), C:H:O is 1:2:1
• Has 5 hydroxyl groups(-OH) .
• Found in straight structure: when glucose is found as dry powder.
• Found in ring structure ( 6 membered ring) :When glucose dissolves in water it gives two ring
forms ( in which carbon 1 joins to oxygen on carbon 5)
isomers, i.e 2 forms of same chemical)
1. α-glucose: where -OH group on carbon 1 pointing downwards.
2. β-glucose: where -OH group on carbon 1 pointing upwards.
• Importance of Ring structure: more stable in solution, and occupy less space, and can easily

r
ab
add more rings to increase the stored energy and stability of polymers as glycogen and starch.

Free functional
group
lG
iha

α-glucose
.N
Dr

Structural formula of glucose

( straight chain)

β-glucose

Free functional
Fructose group

β-fructose
004
 2- Disaccharide(1A. )

• Has 12 carbons, 11 oxygen and 22 hydrogen atoms ( C12H22O11)

• A sugar molecule consisting of two monosaccharides joined together by a glycosidic bond.
• Formation of glycosidic bond (covalent bond):
Occurs as a result of condensation reaction catalysed by specific enzymes, involving the
removal of water molecule.

• Breakage of glycosidic bond (covalent bond):

Occurs as a result of hydrolysis reaction catalysed by specific enzymes, involving the addition of
water molecule.

• From 2 α-glucose

r
Example: Maltose
formation • Forming 1,4 α-glycosidic bond, with one free functional group.

ab
• Malt sugar, found in germinating seed such as barley.
Free functional
lG group(reducing
end)
iha
.N

Example: sucrose
• From α-glucose, and β- fructose.
Dr

formation • Forming 1-2 glycosidic bond where both functional groups are
occupied.
• Stored in plants as sugar cane.
No free functional
group

• From glucose, and galactose.

Example: lactose
formation • Milk sugar , main carbohydrate found in milk.

005
 Notice ;
[Link] of different functional groups:

Notice

[Link] for reducing sugar:

By adding Benedict’s reagent to the tested solution and heat in a water bath.
If colour changes from blue to brick red ppt.( Gradually from blue to green to yellow
to orange to brick red, so reducing sugars are present.
2+ +
Reducing sugar + Cu Oxidised sugar+ Cu

Its a quantitative test where

[Link] faster the change in colour to brick red the higher the concentration of reducing sugars

r
2. OR the higher the intensity of the red colour , the higher the conc. of reducing sugars

ab
measured using colorimeter.

All monosaccharides and disaccharides including maltose and lactose are reducing
sugars, why?
lG
Due to presence of free functional group ( aldehyde group or ketone groups).

Why sucrose is non reducing?

Due to presence of 1-2 glycosidic bond between glucose and fructose where both functional
iha
groups are occupied.
.N

3. Testing for sucrose as a non reducing sugar:

Dr

[Link] heating the tested solution with dilute hydrochloric acid (few drops) then allow
it cool, then add potassium hydroxide/ sodium hydrogen carbonate to neutralise
the acid, this is done for hydrolysis of glycosidic bond and release free
monosaccharides with free functional groups.
• OR using hydrolytic enzymes in presence of water to break the glycosidic bond.
II. and then add Benedict’s reagent and heat to 95C.
III. If colour changes from blue to brick red so sucrose (non reducing sugar) was present.

006
 3- polysaccharides(1A. )

• General formula (C6H10O5)n.

• Is a polymer whose subunits are monosaccharides joined together by glycosidic bonds, 11 or more
monosaccharides
• Formed by condensation of monosaccharides added by glycosidic bonds, with final molecule may
reach to thousand monosaccharides.
• Role of polysaccharides:
1. Starch and glycogen are Energy storage materials( having metabolic function) in plants and animals
as they are compact, inert (unreactive) , and insoluble molecules so don’t interfere with water potential
of cell. Also glucose can be made available again quickly by enzyme catalysed reaction.
2. Cellulose has a structural function, where it builds up the cell wall due to its high tensile
strength( capable of stretching).

r
ab
1-Starch
Starch is a mixture of 2 substances- amylose and amylopectin.
lG
Amylopectin: release glucose for cellular respiration rapidly when needed.
Amylose: releases glucose more slowly over time , keeping you going longer.

A- Amylose:
iha
1. It is a polysaccharide made by condensation of α- glucose .
2. That are linked by 1-4, α-glycosidic bond.
3. Non branching chain.
.N

4. Chains are coiled forming helical (spiral) structure ( making the final molecule more compact so it
takes up less space so doesn’t get into the way of organelles or substances moving around
Dr

cell. ).

1-4 glycosidic
bond
Arrangement of α- glucose units in amylose, the 1,4 linkage
causes the chain to turn and coil. The glycosidic bonds are
shown in red and hydroxyl groups are omitted.

007
 B- Amylopectin ( not helical):

{
1. It is a polysaccharide made by condensation of α-glucose.
2. They are linked by 1-4,α-glycosidic and 1-6,α-glycosidic bonds.
3. Branching chain formed by 1,6 α-glycosidic bonds, but chains are shorter than amylose.
4. Mixture of amylose and amylopectin molecules build up into large starch grains found in
chloroplast and in storage organs such as potato # tubers and seeds(starch grains can be
easily seen by light microscope).

Glycosidic bond between C atoms 1 and 6

of neighboring glucose units(1,6 link)

Removal of water
(condensation)

r
ab
Overall branching structure of an
amylopectin or glycogen molecule.
Branching structure of amylopectin or
glycogen.
lG
Showing formation of a 1,6 link, a branched
point

This structure cause amylopectin to be insoluble, compact with high density, and rapidly
iha
hydrolysed and so these make starch have a metabolic function by being a convenient energy
storage molecule.
Explain why glycogen is a good storage molecule ?
1. Insoluble: so it won’t lower the water potential nor osmotic pressure inside cells, so no effect on
.N

chemical reactions inside cells( ).

2. Many terminals(ends) for easily attachment and removal of glucose (branched)
Dr

3. Glucose can be stored quickly.

4. Rapidly hydrolysed by specific enzymes giving glucose easily and quickly when required for
respiration and energy release.
5. Makes it more compact taking less space ( allow storage of large quantities of glucose in a small
space)

3. Testing for starch using iodine solution

Iodine doesn’t dissolve in water so its iodine in potassium iodide solution:
[Link] drops of iodine solution to solid or liquid substance to be tested .
[Link] starch is present colour will change from orange brown to blue-black colour.
III. Explaination: starch molecules tend to curl up into long spirals. The holes that run
down the middle of this spiral is just the right size for iodine molecules to fit forming
starch iodine complex.

008
 2-Glycogen
1. Type of glucose: α- glucose
2. Branched
3. Types of bond: 1-4 and 1-6 glycosidic bonds
4. Role: energy storage.
5. Glycogen is very similar in structure to amylopectin , but glycogen is greatly more branching than
[Link]?
• Same as above answer (advantage of having highly branched molecule for storage)
6. The glycogen molecules tend to clump together to form granules, which are visible in liver cells
and muscle cells, where they form an energy reserve.

3-Cellulose
1. Type of glucose: β- glucose ( it is a polysaccharide of β-glucose)

r
2. Types of bond: 1-4 ,β-glycosidic bonds.

ab
3. β- glucose units are linked at 180 to each other( alternately oriented).
4. Unbranched polymer (linear/ straight chain) allowing molecules to lie parallel to each other.
lG
OH groups lined up to form
1-4, β-glycosidic bond.

Two β- glucose molecules

iha
lined up to form a 1,4 link.
One glucose molecule must
be rotated 180 relative to the
other, thus making cellulose
molecule looks like a flat
.N

ribbon.
Dr

{
5. With many -OH( hydroxyl) groups projecting out in different directions, this allows:
I. Many Hydrogen bonds between cellulose molecules to give parallel chains.
II. To form bundles called microfibrils.
III. Many microfibrils held together by more H bonds to form cellulose fibres.
IV. Where fibres are found at angles( criss cross over each other ).

6. These make the cellulose fibres have a very high tensile strength ((i.e slightly elastic but
unstretchable) to prevent cell bursting and allow it to withstand turgor pressure.
7. Cellulose cell wall is freely permeable with many gaps in walls allowing passage of water and
substances.
8. Insoluble.

009
 Hydrogen
bond

r
ab
8. Role of cellulose in living organism:
cellulose has a structural function , as it enters in cell wall formation due to its high tensile strength.
9. Role of cell wall( 7μm) lG
I. Made of cellulose with high tensile strength to allow cell withstand high turgor pressure due to
osmosis.
II. Fully permeable due to presence of gaps in wall.
iha

Notice
[Link]: means unequal distribution of charges.
It occurs in many different molecules, wherever there is an -OH, -CO or -NH group.
.N

Notice
Dr

[Link] bond: where the negatively charged oxygen/ nitrogen/ fluorine in one molecule is attracted to
a positively charged hydrogen of another molecule .

Hydrogen
bond

[Link] which have groups with dipoles are polar Attracted to water( because
water molecules also have dipoles) Such molecules are hydrophilic ( water soluble).
4. Molecules with no dipoles. Non polar. Not attracted to water. Hydrophobic(water
hating).

010
 B: Lipids (1A.4)

• They are all organic molecules which are insoluble in water, why?
Lipids contain the elements carbon, hydrogen and oxygen, with much reduced
proportion of oxygen to carbon and hydrogen than in carbohydrates, which
decreases the number of polar -OH groups , making lipid non polar , so they are
insoluble in water(hydrophobic), being unable to make Hydrogen bonds with water.
• fats are less dense than water and so float.
• Lipids are esters formed by fatty acids combining with an alcohol.

• They are divided into :

r
Triglycerides.
Phospholipid.

ab
Steroids and cholesterol (discussed later)

1- Triglycerides(fats& oils)
lG
1. Glyceride is an ester formed of fatty acid combining with the alcohol glycerol.
2. Triglyceride molecule formed from 3 fatty acids tails combining with one glycerol, with three
ester bonds..
iha
3. The triglycerides differ from each other according to the length of the tail of fatty acids which
vary according to the number of -CH2, and can be saturated or unsaturated.
Long hydrocarbon tail ( often of 15 or 17 carbons) attached to the acid
.N

A-Fatty acids head( carboxyl group -COOH)

Carboxyl group
Dr

Of 15 or 17 carbon
atoms long

Carbon carbon
double bond.

Saturated fatty acid

Unsaturated fatty acid

011
 Saturated fatty acids Unsaturated fatty acids

Tail of fatty acids has no carbon carbon double Tail of fatty acid has carbon carbon double bonds
bond between neighbouring carbons. between neighbouring carbons (-C=C-)
Chain is straight. Chain have kinks.

Saturated because they contain the maximum They are called unsaturated because they don’t
amount of hydrogen, hydrogen to carbon ration is contain the maximum possible amount of hydrogen,
larger. hydrogen to carbon ratio is smaller.

Animal lipids are often saturated and occur as fats. Plant lipids are often unsaturated and occur as oil
(ex; olive and sunflower oil)

Fats with saturated fatty acids are solid at room Fats with unsaturated fatty acids are liquid at room
temperature. temperature.

Number of hydrogen atoms in hydrocarbon tail= Number of hydrogen atoms in hydrocarbon tail=

r
9 C X 2= 18 +1 = 19 hydrogen atoms 19- ( 2) =17 hydrogen atoms

ab
Organic molecules with hydroxyl (-OH )groups , attached to carbon
B-Alcohols(glycerol) atom.
Glycerol is an alcohol with 3 -OH groups.
lG
Reaction between acid and alcohol produces an ester with
ester bond (-COO-).
iha
.N

So Triglycerides:
Dr

They are non polar due to

the presence of
Esterification hydrophobic head and three
hydrophobic tails.

012
 Role of Triglycerides Structural adaptation of Triglycerides
1- Energy storage Richer in carbon- hydrogen bonds( C-H bonds) more than carbohydrates ( i.e
more reduced ),
So release more than twice the energy released by same mass of
carbohydrates. ( 1gm releases 39KJ)
2- Thermal insulator, Being non polar ,where it is stored just below the dermis of skin reducing heat
loss.
3- Electrical insulation, in Being non polar , where it forms part of the myelin sheath around neurones
nerve cells
3- Protection of vital organs Being hydrophobic
where its stored around the
kidneys
4-Metabolic source of water When oxidized in respiration , they are converted into carbon dioxide and water,
in some mammals like desert which is very important in dry habitats.
kangaroo rat.

Notice: fatty acids have different melting point ?

The greater the number of double bonds, the lower the melting points

r
Notice
Because the fatty acid chain is more bent, so fatty acids don’t pack closely together.

ab
Weak intermolecular forces, so less energy needed to separate fatty acid chain
molecules.
lG
2- Phospholipids
iha
1. Phospholipid molecule formed of 2 fatty acids attached to one glycerol(head) with phosphate
group attached to 3rd carbon of glycerol.
It has a hydrophilic head made of glycerol with attached phosphate group, and a hydrophobic tail
made of 2 fatty acids.
.N
Dr
Hydrophilic head
2 hydrophobic tails

One of the 3 fatty acids is replaced by

phosphate group, which is
polar( hydrophilic) so can dissolve in
water.

013
2. The phospholipid molecules form a membrane around a cell, where the hydrophilic heads lie
facing the watery solutions on the outside of the membrane( facing cytoplasm and tissue fluid),
and the hydrophobic tails form a layer that is impermeable to hydrophilic substances.

The phospholipids molecules arrange themselves tail to tail to form a phospholipid bilayer
that forms the basic structure of the cell membrane .

r
Cytoplasm

ab
lG Tissue fluid
iha
Point of comaparison Triglycerides/fat/lipid Phospholipids
Elements C, H, and oxygen C, H, and oxygen
Presence of glycerol molecule ✔ ✔
.N

Presence of fatty acids ✔ ( 3 fatty acids) ✔ (2fatty acids)

Dr

Presence of double bond( C=O) ✔ ✔

Presence of ester bond ✔ ( 3 ester bonds) ✔ ( 2 ester bonds)

Phosphate group ✖ ✔

3. Testing for fats using emulsion test :

[Link] substance thought to contain lipids is shaken vigorously with
absolute ethanol to dissolve lipids.
[Link] ethanol is poured into a tube containing water.
III. If lipid is present , a cloudy white suspension is formed.

014
 C: Proteins(1A.5)
Proteins are an extremely important macromolecules forming than 50% of dry mass of most cells.
Having many functions:
1. Making some hormones as insulin and glucagon.
2. All enzymes are proteins.
3. Essential component of cell membrane (
4. Make antibodies that protect body from [Link] protein, signaling proteins)
5. Oxygen carrying pigment haemoglobin and myoglobin are proteins.
6. Making Collagen in arteries which help them withstand high pressure, prevent over stretching,
and prevent bursting.
7. Keratin which is protein found in hair, nails and the surface layers of skin.
8. Actin and myosin are proteins responsible for muscle contraction.
9. Proteins may be storage products-ex; casein in milk, ovalbumin in egg white.
• Basic monomer is amino acid.

r
• Elements: carbon, Hydrogen, oxygen and Nitrogen.

ab
[Link] acids: 1. There are 20 different amino acids which occur in the
protein of living organisms, all with different R groups
α- carbon
lG 2. Function of R groups:
I. Variable group, different in different amino acids.
II. It determines the three dimensional shape of protein.
III. It determines wether the protein is water soluble or water
iha
insoluble.
Example:
Variable side chain
Amino acid with non polar R group (hydrophobic side chain)
.N

as -CH3 as collagen , is water insoluble.

Amino group Carboxyl group
Amino acid with polar R group _CH2OH are water soluble by
being able to form hydrogen bonds between chains.
Dr

20 Different R groups determine the 20 different amino acids, examples ( no need to memorise)

R group Amino acid Side chain Water solubility

-H glycine non-polar Water insoluble
- CH3 alanine non-polar Water insoluble
- CH2OH serine polar Water soluble
being able to form
- CH2SH cysteine polar hydrogen bonds
between chains.
- CH2COOH aspartic acid acidic
- CH2CH2CH2CH2NH2 lysine basic

015
 3. Function of amine and carboxyl groups :
They cause amino acids to act as buffer in cells, this means they resist changes in pH when an
acid or alkali is added to an amino acid in solution.
When an acid is added, the _NH2 group combines with H+ ions from the acid to form NH3+
When an alkali is added, the _COOH group combines with OH ions from the alkali by loss of H+ to
form _COO-, so in both cases, the conc. Of H+ ions in solution doesn’t change greatly so pH
remains about the same.
So the carboxyl group will give H ion if the pH increase and become anion(-ve charged) and amine
group takes H ion if the pH decreases and become cation ( + ve charged)

r
ab
2. Types of protein bonding:

A-peptide bond:
lG
A molecule made up of many amino acids linked together by peptide
bonds is called polypeptide
iha
.N

1. Condensation reaction ( loss of water molecule)

Dr

2. OH/ O- from carboxyl group of one amino acid , and Peptide bond is a
H+ from amine group of another amino acid . strong covalent bond , not affected by
3. Peptide bond links C- N. pH and temperature changes.

B-Hydrogen bond:

Hydrogen bond
formed between strongly polar
group, easily broken by changes
in temperature& pH.

The hydrogen bonding occurs between the the oxygen of -CO- group of one amino acid and the
Hydrogen of the -NH- group of the amino acid four places a head of it.

016
 Polypeptide chain
C-Ionic bond:

Ionic bond formed between ionised amine (NH3 ) group of R

+ )
group of one amino acid and ionised carboxylic acid (COO +
-
group of another R group of neighboring amino acid, they can
be broken by pH -& temperature changes.

D-Disulfide bond:
Strongest bond

Disulfide bond is a strong covalent

bond form between two cysteine
molecules which contain sulfur
atoms.

r
-2H ( oxidation)
Where cysteine amino acid group is

ab
the only amino acid capable of
+2H ( reduction) forming disulfide bonds.
They can be broken by reducing
agents such as Cu2SO4 and
PbNO3.
lG
iha
E-Weak hydrophobic interaction:

Hydrophobic interaction formed between two non polar

R group, they are weak interactions, but still these groups
tend to stay together because they are repelled by the
.N

watery environment around them.

It maintains the three dimensional shape of protein.
Dr

So bonds that stabilise the structure of protein are

disulfide(strongest bond), hydrogen bond, ionic bond and
hydrophobic interactions.

Summary

017
 3. Protein structure:

A-Primary structure
Peptide
bond
1. It is the linear sequence
of amino acids in a
polypeptide or protein
with peptide bonds
between them , which is
the last bond to break at
high temperature.

B-Secondary structure

r
Hydrogen bond without

ab
including R gps.

1. It is the regular folding or coiling of the polypeptide α- helix

chain held in shape due to hydrogen bonding
lG
between the the oxygen of -CO- group of one
amino acid and the Hydrogen of the -NH- group of
another amino acid, (Hydrogen bond between polar
iha
groups - NH- and -CO-)
2. Types of folding :
A. α- helix type :the polypeptide chain is coiled into
spiral shape, in which the hydrogen bonds
.N

between amino acids in the same polypeptide

chain stabilize the α-helix structure, with the
Dr

peptide bonds forming backbone and R groups

protruding in all directions.
B. β-pleated sheet( much looser straighter shape
than α-helix) in which the polypeptide chain are
held into regular/parallel pleats/flat sheets held
together by hydrogen bonds between the amino
and carboxyl ends of amino acids .

β-pleated sheet

018
 C-Tertiary structure
Hydrogen + ionic + disulfide bonds
and hydrophobic interaction.

1. It is overall folding and coiling of the

polypeptide chain in a specific way forming
a precise 3 dimensional shape.
2. It is maintained by:
Interaction between R groups side chains.
I. H- bonds between polar groups(NH- and
CO-)
II. Ionic bond between ionised amine and
carboxylic acid group
III. Disulfide bonds between cysteine (S-H)
groups.
IV. Hydrophobic interaction between non polar

r
side chains.

ab
• Most enzymes have tertiary structure, only few
have quaternary structure.
Secondary and tertiary structure of lysozyme .

α-helices
lG
iha
Random coils

Disulfide bond
.N
Dr

β-pleated sheet

D-Quaternary structure Primary structure: linear sequence

of amino acids in a peptide .
1. It is the three dimensional
arrangement of two or more Secondary structure: repeating
pattern in structure of polypeptide
polypeptides. chain, held together by hydrogen
bonds, such as α helix or β pleated
2. They are held together by the sheets.
same four types of bonds as in
tertiary structure. Tertiary structure:.the three
dimensional overall folding of
3. Examples; haemoglobin formed secondary structure
of 4 polypeptide chains( 2α-and
2β-globins) , while collagen is Quaternary structure:.the three
made of 3 polypeptides. dimensional arrangement of more than
one polypeptide

019
 4. Types of proteins:

A-Globular protein
1. Spherical ,they are water soluble.
2. This is because the amino acids with hydrophilic polar A section through a part of globular protein
R groups are facing outwards ( so hydrogen bonds can
form with water) while amino acids with hydrophobic R
groups pointing to the inside towards the center of
molecule.
3. The molecule curl up into a spherical / ball shape
( globular shape) and have tertiary structure with
specific 3D shape making them metabolically active .
4. I.e Many have metabolic functions.
• Examples: haemoglobin, myoglobin, insulin, antibodies,

r
Enzymes

ab
Enzymes structure and function
lG
Explain how primary structure of an enzyme determines its three
dimensional structure:
iha
1. Primary structure is the sequence of amino acids in polypeptide chain. Notice

2. Which determines the folding of protein(secondary structure).

3. And determines the position and type of bonds between R groups of amino
acids.
.N

4. Such as disulfide bond ( describe ), hydrogen bonds( describe),.....

5. amino acids with hydrophilic polar R groups are facing outwards ,while amino
acids with hydrophobic R groups pointing to the inside.
Dr

6. Enzymes are globular proteins, having tertiary structure.

7. Forming specific shape of active site.

020
 B-Fibrous protein

1. Have simpler structure ( no tertiary structure), with polypeptides lying parallel to

each other so more stable to changes in temperature and pH.
2. They don’t curl up but form long strands (poly peptide chains) with many cross
links ( cross linked chains)
3. Water insoluble.
4. With large number of repeating amino acid sequences
5. Have structural function ( being very tough thus giving strength).
6. Examples:
I. keratin forming hairs, nails, and the outer layer of skin making these structures
waterproof.
II. Collagen (structural protein provides strength to artery wall)
Fibrous protein Globular protein

r
Shape Long and narrow fiber like structure. Round/ spherical
Has no tertiary structure( no Has tertiary structure( complex folding)

ab
complex folding) And sometimes Quaternary structure.
Purpose Structural function Metabolic Function( ex catalytic,
transport, ...)
Amino acids
lG
Large number of repeating amino Irregular amino acid sequence..
sequence acid sequences
iha
Durability Less sensitive to changes in pH and More sensitive to changes in pH and
temperature temperature.
Solubility (generally)Insoluble in water Genrelly soluble in water
.N

Examples Collagen in tendons, keratin, myosin Enzymes, haemoglobin, insulin and

in muscles. immunoglobulin
Dr

Notice : though carboxyl and amino ends give

them ionic properties, yet they dont dissolve in
water:
Because molecules molecules are so big that
they form colloid ( a suspension of molecules
that are not fully dissolved).
They don’t settle and can’t be easily separated.
021
 Collagen structural adaptation
1. An insoluble fibrous protein.
2. Found in tendons, cartilage, bones, teeth , walls of blood vessels.
3. Made of three polypeptide chains(quaternary structure) ,each in a shape of helix but not α- helix as it
is not tightly wound.
• 300nm long polypeptide, each polypeptide chain is of 1000 amino acids.
4. Glycine ( smallest amino acid) is repeated every third position In each polypeptide
5. The 3 helical polypeptides are wound around each other forming triple helix( helical structure).
6. Which are held by many H- bonds between the polypeptides.

7. Also they are held by covalent bonds( cross links) between collagen molecules lying parallel to
each other (between the R groups of amino acids lying next to each other) to form fibrils.
8. The ends of the parallel molecules are staggered( arranged not in a line) to avoid any weak spot along

r
the length of fibril.

ab
9. Many fibrils lie along each other forming strong bundles called fibres.
• This give the collagen high tensile strength, i.e can withstand large pulling forces without stretching or
lG
breaking.

A C
B
iha
.N
Dr

Many of these triple helices lie side by side ,

The polypeptides which make up a Three helices wind together to linked together by covalent cross links
collagen molecule in a form of a form collagen molecule. between side chains of amino acids near the
stretched out helix. The three strands are held end of poly peptides to form collagen fibril.
With every third amino acid is glycine. together by many hydrogen bonds each fibril made of many triple helices lying
and some covalent bonds. parallel with one another .

Collagen fibres ( each fibre made of many fibrils lying side

by side.
Can be seen by light microscope.

022
 C-conjugated protein

Some protein molecules are joined with ( conjugated to) another molecules called a prosthetic group
( i,e not made from amino acids).
This includes :

1. Haemoglobin structure and function

1. They are globular shape( where the polypeptide chains fold

giving globular structure)
2. Water soluble as it has amino acids with hydrophilic R
groups facing cytosol forming Hydrogen bond with water.
3. It is made of 4 polypeptide chains ( 2α- and 2β-of globins )
so has quaternary structure.

r
4. Each polypeptide chain has a haem group( prosthetic group,

ab
i.e not made of amino acids) made of iron (Fe+2) ion
attached to a porphyrin ring to bind with oxygen forming
oxyhaemoglobin, so
lG
5. 4 polypeptides ( haems) carry 4 oxygen molecules (4O2)
I.e one haemoglobin carry 4 oxygen molecules
iha
-Hb + 4O2 HbO8

2. Lipoproteins
.N

Proteins are conjugated with lipids .

Dr

Where lipoproteins are very important in the transport of cholesterol in blood.

As Triglycerides are insoluble, so they are conjugated with proteins forming lipoproteins
( either LDL or HDL) formed into vesicles.
HDL contains more protein than LDLs, which is partially why they are denser,as proteins are
more compact molecules than lipids.

3. Glycoprotein

Proteins with carbohydrates prosthetic group, with the carbohydrate part of molecule helps them to
hold a lot of water and also make it harder for protein digesting enzymes( proteases ) to break them
down.
Example: mucus and viscous which reduces friction.
Also explains why mucus produced in stomach protects the protein walls from digestion.

023
 Notice:
[Link] boiling collagen in bones/teeth , the helices of collagen
Notice
molecules (appearing in diagram b ) un wind.
[Link] found in walls of arteries to withstand pressure, prevent over
stretching, and prevent bursting and rapture.
[Link] should be able to compare between collagen and haemoglobin .

4. Testing for proteins using biuret test ( Cu2SO4 + dilute KOH / NaOH)
All proteins have peptide bonds , which form purple complex with copper(II)ions
[Link] biuret reagent is added to the solution to be tested.
II. If colour changes from blue to purple this indicates the presence of proteins.
III. Notice that colour develops slowly over several minutes.

r
ab
Second: Some key properties of water making
life possible(1A.1)
lG
1. Water is dipolar , where each water molecule has oxygen atom which is slightly negatively
charged( -δ) and hydrogen , is slightly positively charged ( +δ) .
iha
2. This polarity of water molecules causes them to be attracted to each other forming
hydrogen bond( weak attraction between water molecules),
3. Hydrogen bond plays an important role in protein structure and structure and functioning of
.N

DNA.
-δ
-δ
Dr

-δ
+δ +δ +δ +δ

+δ +δ

024
 Distribution of water molecules
Properties of water: around ions in a solution.

A-water as a solvent:

1. Water is an excellent solvent for

ions and polar molecules, this is
because its dipolar.
• ions are charged and So water
molecules can collect around charged
ions , with oxygen-δ facing +δ ion,
thus separating them from each other
and allowing them to move freely and

r
react with other chemicals.

ab
So the importance of this property:
lG
1. To allow metabolic reactions in living cells to help dissolve reactants and allow their free
moving to be able to interact with one another.
iha
2. Help maintain the stability of cell membrane.
3. It is a transport medium due to its dipole nature in:
I. Animals: in blood, in the lymphatic, excretory and digestive systems of animals by being able
.N

to dissolve and transport digested food, hormones, antibodies, wastes.

II. Plants: salts are transported in xylem vessels while sucrose and amino acids are
Dr

translocated in phloem.

B-Water has high specific heat capacity:

1. It is the amount of heat energy

required (in joules) to raise the
temperature of 1kg of water by 1C.
2. Water has high heat capacity due to
the presence of many hydrogen
bonds between water molecules
making them stick to each other.

025
 So the importance of this property:

Water is resistant to change in temperature so:

1. It provides a relatively stabilised temperature of lakes and oceans by allowing slow change
in temperature of water in lakes as environmental temperature changes, thus stable
environment for aquatic organisms.
2. cause temperature in the cell and bodies of living organisms to be more constant( since
water makes70 yo 80% of body) , so biochemical reactions can take place at constant
rates and for providing optimum temperature for maximum enzymatic activity.

C-water has high latent heat of vapourisation:

r
1. It is the amount of heat energy needed to break hydrogen bonds between water molecules

ab
and change water from liquid to gas(vapour)/amount of heat released during a change of
state. lG
So the importance of this property:

1. Water has a high latent heat of vapourisation, due to its high heat capacity, which is a
iha
consequence of having many hydrogen bonds that tend
to stick them together, so water needs this high amount
of energy to break these H-bonds.
.N

So it plays a role in decreasing body temperature, by

evaporation of sweat using the excess latent heat , while
Dr

reducing risk of dehydration because large amount of heat

can be lost for relatively loss of water.
2. It also plays a role in cooling down plants by transpiration.
3. Also protects aquatic animals from freezing , as for water to change from liquid to solid ,
water molecules have to lose a relatively large amount of energy, making it less likely that water
will freeze, same for aquatic organisms.

026
 D-Water density and freezing point :

0
1. When temperature falls below 4 C , the density of water decreases.

So the importance of this property:

1. Ice therefore floats on liquid water and insulates the water under it, thus reducing the
tendency of aquatic living organisms to freeze
completely so increasing their chance of survival in
cold conditions.
2. Also changes in density of water with change in
temperature causes currents ,which help maintain the
circulation of nutrients in oceans.

r
ab
E-water having high surface tension and cohesion :
lG
1. Cohesion: is the force by which water molecules stick together by hydrogen bonds.

So the importance of this property: is allow water to move in long unbroken columns
through the vascular tissues in plants
iha

2. Surface tension: the tension of the surface film of water caused by the attraction of the
water molecules( cohesion force) in the surface layer by the
.N

bulk of the water, which tends to minimize surface area.. don’t

study definition just understand.
Dr

So the importance of this property: allow certain small organisms

as pond skaters to exploit the surface of water as a habitat,
allowing them to settle on or skate over its surface.

F-water as a reagent:

1. Used as a reagent in some chemical reactions inside cells, as during photosynthesis.

2. Also essential in all hydrolysis reactions ( mechanism by which large molecules are broken
into smaller ones) as in digestion.

027
 1. Water has high melting and boiling points
Because it takes a lot of energy to break all hydrogen bonds that hold the
Notice molecules together.

[Link] has high surface tension :

Because the attraction between water molecules ( including hydrogen bonds) is
greater than the attraction between water molecules and air, Thus the water molecules hold
together forming a thin skin of surface tension.

3. How water is involved in transport of molecules in living organisms:

Water is a solvent
Water is polar/ dipoles.

r
Polar molecules / ions dissolve in water

ab
Example: oxygen, carbondioxide, amino acids transported in water.

lG
iha
.N
Dr

028
Topic 1B

Introduction to
Mammalian
transport system

r
ab
Learning outcomes
The principles of circulation
lg
iha
The roles of the blood
.N

Description and explanation of

the function of blood, including
oxygen transport
Dr

Relate structure of veins,

arteries and capillaries to their
functions.

Description of cardiac cycle

and its control

Describing and understanding

the course of events that lead
to atherosclerosis.

[Link] Gabr 032

 First: The principles of Circulation
A : importance of transport system in animals:
Large organisms have small surface area to volume ratio,
so simple diffusion isn’t sufficient due to limitations....
[Link] metabolic rate ( high energy requirements)
[Link] S.A to volume ratio, so long distance of diffusion.
[Link] gradient.

1. They have small surface area to volume ratio. Longer distances for nutrients to
reach cells. So diffusion alone would be too slow and insufficient .
2. So Heart needed to pump blood
3. where substances such as nutrients and oxygen are transported in the flow of a fluid
( blood) around the body ( down pressure gradient ensuring mass flow).
4. Circulatory systems allow efficient supply to cells of glucose, amino acids , hormones to

r
all parts of the animal.

ab
5. As they have high metabolic rate (high energy demand) , with a need to regulate a
constant body temperature , where cells use much oxygen and nutrients and produce
much carbon dioxide (which is needed to be removed from cells quickly) .
lg
B: Transport system in small organisms:
iha
The needed oxygen and nutrients in single celled organisms can
diffuse directly into the cells from the environment and waste
products can diffuse out because,
.N

1. The diffusion distance from outside to the inner most areas of the cells are very small.
2. Large surface area to volume ratio .
Dr

3. The metabolic demand is low , with no need to regulate their own temperature and the
cells don’t use much oxygen and nutrients or produce much carbon dioxide.
4. So diffusion alone would be sufficient to supply their needs

C: Features of mass transport systems:

Mass transport system: an arrangement of structures by which substances are
transported in the flow of a fluid with a mechanism for moving it around the body.

1. Respiratory system:
• As diffusion over surface is not enough
• Respiratory system has a large surface area (lungs/gills) to allow exchange of gases
in and out of transport system.

[Link] Gabr 033

2. Heart:
To generate pressure , ensuring mass flow ( which is the transport of substances from high
pressure to low pressure over a long distance).
• Thus overcoming limitation of diffusion, where they have small surface area to volume ratio,
so Longer distances for nutrients to reach cells, thus diffusion alone would be too slow and
insufficient .

3. System of branching vessels:

• That carry substances , following a very specific route to required body parts.

[Link] transport medium ( blood) : in which oxygen , nutrients, as well as waste products
dissolve.

D: The circulatory system:

Types of circulation

Open Closed Single

r
circulation circulation Double

ab
lg
iha

In the open circulation, the blood is not enclosed in the blood vessels and is pumped
.N

into the cavities of the body. On the contrary, in the closed circulation, the blood is
pumped through the vessels separate from the interstitial fluid of the body
Dr

1. Mammals & birds have a closed,

double circulatory system.
First circuit to
• Closed circulation means that blood is lungs

transported in closed vessels inside the

living organism.
Second circuit
• Double circulation means systemic and around the rest
of the body
pulmonary circulation , where for each
complete circuit round the body, the blood
passes through heart twice. Blood
transported from heart to lungs and back,
then to rest of body and back

[Link] Gabr 034

 Notice
A. Explain advantages of having
double circulatory system:
One side of the heart pump blood to lungs, and the
other to rest of body.
1. Separation of oxygen rich blood (oxygenated
blood) and oxygen depleted blood (deoxygenated
blood) so Maintaining a steep gas concentration
gradient of oxygen in lungs, tissues. I.e steep
concentration gradient for gas exchange, thus
tissues receive as much oxygen as possible.
As multicellular organisms (name them) have high

r
metabolic rate.

ab
2. Allow pumping of blood under 2 different pressure:
lg
Relatively higher pressure in systemic circulation to body ensuring that glucose and oxygen reach
all body tissues over long distance, also blood can reach to brain as blood is being pumped
iha
against gravity...(allowing effective mass flow).
Lower pressure in pulmonary side protects delicate pulmonary capillary network from being
damaged by higher pressure. Exam tip:
.N

If asked how double

circulation helps mammals to
carry out effective gas
exchange:
Dr

Same answer without

4. Transport system in fish: . mentioning higher pressure to
body....
• Single circulation in which the blood
flows through the heart once for each
complete circuit of the body
Disadvantages
Both oxygenated and deoxygenated
blood are mixed reducing
concentration gradient.
Rapid fall in velocity and pressure as
blood leaves the gills.
So slower delivery of oxygen for
respiration in tissues
pressure of blood too low for efficient
kidney function in mammals.

[Link] Gabr 035

 Second: The roles of the blood:
You have about 5dm3 of blood in your body,
with a mass of about 5kg.
Inside blood plasma , there are red blood cells,
white blood cells and platelets ( small cell
fragments with no nucleus).

[Link] blood cells(erythrocytes)

Function:
Transport oxygen from lungs to respiring tissues.
Also transport of carbon dioxide.
2. Veins
Structure:
• Relatively small in size about 7µm to squeeze through

r
capillaries, this helps slow down movement of red

ab
blood cells allowing effecient gas exchange and make
them very close to the surface so shorter diffusion
distance.
lg
• Small size also makes haemoglobin nearer to the
surface, so short distance for diffusion.
• No nucleus, no mitochondria, no endoplasmic
iha
reticulum so more room for haemoglobin So more
oxygen transported( more oxygen carrying capacity)
• Biconcave shape to have larger surface area to volume
ratio so oxygen can diffuse into and out of them
.N

rapidly.
• Flexible to squeeze through capillaries.
• Full of haemoglobin which react with oxygen forming oxyhaemoglobin to transport oxygen to
Dr

body cells.

Notice:
Red blood cells are very flexible, this is possible because the cells have a
Notice
specialised cytoskeleton, made up of a mesh-like network of protein fibres
that allows them to be squashed into different shapes, but then springs back
to produce the normal biconcave shape.

In separate documents named circulation 2

[Link] Gabr 036

 2. White blood cells(leucocytes)

Function:
They are much larger than erythrocytes but can also squeeze through tiny blood vessels
because they change their shape, they are many different kinds of white blood cells , with wide
variety of functions, all are concerned with defending the body against infection.
They all contain a nucleus and have colorless cytoplasm.

2. Veins
3. Platelets ( thrombocytes)

Function:
They are tiny fragments, found in bone marrow .
There are about 150,000 to 400,000 platelets per mm of blood .
Involved in blood clotting , which is needed to prevent blood loss and prevent entry of pathogens.
Notice :

r
Megakaryoctes are large cells that are found in the bone marrow and produce platelets.

ab
Formation of a clot :
Plasma, blood cells and platelets flow from a cut vessel, where the contact
between the platelets and the cut tissue( collagen fibres in skin) cause
platelets to break open in large numbers.
substances :
lg Releasing several

Serotonin: cause smooth muscles of blood vessels to contract.

iha
Narrowing(constricting)blood vessels. Thus cutting off the blood flow
to the damaged area.
.N

Thromboplastin: which is an enzyme that starts a sequence of chemical

change that clot the blood
Plasma, blood. V
Dr

Process of blood clotting :

1. Plasma at the damaged tissue release thromboplastin. Which catalyses the conversion of
large soluble protein prothrombin (biologically inactive) into another soluble protein called thrombin
enzyme ( biologically active).
In presence of calcium ions at right concentration which aids in conversion of prothrombin into
thrombin.
2. Thrombin converts soluble fibrinogen ( plasma protein) into insoluble fibrin Fibrin forms a
mesh of fibres which traps blood cells, platelets to form a clot.
3. Special proteins in the structure of platelets contract , making the clot tighter and tougher to form a
scab that protects the skin and vessels underneath as they heal, also preventing entry of bacteria

Exam tip:
Narrow blood capillaries
prevent excessive bleeding by
allowing less blood flow near
skin surface so blood clots
[Link] Gabr 037
 Platelets at a damaged
tissue

Thromboplastin
Calcium ions
Prothrombin( precursor of
thrombin)

Catalyses

Thrombin

Catalyses
Fibrinogen( precursor of Forms
Fibrin Clot
fibrin)
Protease breaks peptide

r
bonds in fibrinogen to
produce fibrin, which is

ab
hydrophobic, causing fibrin
to stick together.

4. Blood plasma
lg
iha
Blood plasma is the fluid part of your mass transport system.
Water forms 90% of blood plasma
Where the properties of water make it ideal being the largest
.N

component of plasma:
1. Water is a good solvent. So can transport many substances
- Where polar compounds such as glucose, amino acids can
Dr

dissolve in water.
- Ions dissociate in water.
- Globular proteins such as antibodies can dissolve in water.
2. Cohesion between water molecules. Allow continuous
blood flow.
3. High specific heat capacity which helps stabilise body temperature.
4. High latent heat of vaporisation So ,that in body temperatures,
plasma stays liquid and doesn’t evaporate.
5. Low compressibility.
6. Allows efficient circulation of blood.
7. PH neutral, allowing stability of proteins ( preventing their denaturation).

[Link] Gabr 038

Function of plasma :
It carries all your blood cells and everything that needs transporting around your body Including ;
1. Digested food particles ( glucose and amino acids) from the small intestine to the liver and then to
all the parts of the body where they are needed for immediate use or storage.
2. Nutrient molecules from storage areas to the cells that need them.
3. Excretory products ( such as carbon dioxide and urea ) from cells to the organs such as the lungs
or kidneys to be excreted.
4. Hormones from where they are made to where they cause changes in the body.
Also plasma helps to maintain a steady body temperature:
By transferring heat from internal organs( as gut) or very active tissue( leg muscles in someone
running) to the skin , where it can be lost to the surrounding.
Also act a s a buffer to regulate pH changes
It carries all , blood. V

r
ab
lg
iha
.N
Dr

[Link] Gabr 039

Transport of oxygen:

A. Haemoglobin

Haemoglobin plays a role in the transport of both oxygen and carbon dioxide:

1. First role of haemoglobin in transport of oxygen

1. Each haemoglobin molecule can combine reversibly with four oxygen molecules (eight oxygen
atoms). Forming oxyhaemoglobin in lungs.

[Link] remains bound until blood in area of low pO2 ( i.e, high pCO2)
Notice: partial pressure is pressure exerted by a gas.

r
2. Second role of haemoglobin in transport of carbondioxide

ab
1. Carbon dioxide combines with -NH2 group(amino group) of haemoglobin forming
carbaminohaemoglobin. lg
2. Carbon dioxide remains bound until area of low
pCO2( i.e high pO2)
iha
B. Haemoglobin dissociation curve
.N

The shape of the haemoglobin dissociation curve reflects the way that oxygen atoms combine with
haemoglobin molecules.
Its aim is to find out how haemoglobin behaves at different concentrations( partial pressures) of
Dr

oxygen.

The curve shows that at low partial

High partial pressure of
oxygen (in lungs) pressures of oxygen ( in respiring
cells), the percentage saturation of
haemoglobin is very low that is, the
haemoglobin is combined with only
a very little oxygen. At high partial
Description
of graph pressures of oxygen ( in lungs), the
Low partial pressure
of oxygen (in percentage saturation of
respiring tissue)
haemoglobin is very high; it is
combined with large amounts of
oxygen

[Link] Gabr 040

 Behaviour of haemoglobin to different pO2 at different parts of the body

In lungs In respiring cells

Concentration of oxygen in RBCs is relatively Concentration of oxygen in body tissues is

low , so oxygen diffuse from air in lungs down relatively low while in cytoplasm of RBCs is
concentration gradient into RBCs higher (more oxyhemoglobin dissociation)
haemoglobin picks up oxygen and bind than in surrounding tissue ,as haemoglobin
together (more oxyhaemoglobin)so free oxygen has lower affinity to oxygen, so oxygen
concentration in cytoplasm of red blood cells diffuse out into body cells down
stays low maintaining steep concentration concentration gradient.
gradient between air in lungs and RBCs so more
oxygen diffuse in and joins onto haemoglobin

Haemoglobin in RBCs in Haemoglobin in RBCs in actively

capillary in lungs respiring cells

r
Here in lungs haemoglobin picks up oxygen, . Here in respiring cells, haemoglobin releases

ab
where the partial pressure of oxygen (pO2) is oxygen, where the partial pressure of oxygen
high , pCO2 is low. this haemoglobin ( pO2)is low and high pCO2, the
haemoglobin will be about 20–25% saturated
will be 95–97% saturated with oxygen
l g{ with oxygen.

This means that Hb coming from the lungs carries a lot of oxygen; as it reaches a muscle, it releases
around three-quarters of it. This released oxygen diffuses out of the red blood cell and into the muscle
where it can be used in respiration.
iha
So PO2 decreases as blood flows through arteries and into veins........as arteries takes blood to cells, while
veins takes blood away from cells so O2 diffuse out of capillary into cells because there is a lower PO2 in
cells and CO2 increase in blood by entering blood.
.N

Why the dissociation curve is S-shaped curve?

Dr

As haemoglobin is made of four subunits ( 4 polypeptides) with 4 haem groups

haemoglobin picks up oxygen, it becomes more saturated with oxygen, until fully saturated .
Oxygen molecules combine with the iron atoms in the haem groups of a haemoglobin molecule. You will remember
that each haemoglobin molecule has four haemgroups.

The binding of first oxygen molecule is difficult. Where a first oxygen molecule combines with
an iron atom in a haem group the whole haemoglobin molecule is slightly distorted as many many
molecules will be broken down ( this will cause a conformational change). The distortion makes it
easier for other oxygen molecule to combine with haem groups, As haemoglobin becomes
saturated less oxygen can bind so the curve flattens out.
( allosteric mechanism)
Notice: the same process happens in reverse when oxygen dissociates from haemoglobin where
it gets progressively harder to remove the oxygen.
[Link] Gabr 041
 C. The Bohr shift

Its that the amount of oxygen the haemoglobin

carries is affected by both partial pressure of
oxygen (pO2) and partial pressure of carbon
dioxide (pCO2).
Where if the partial pressures of carbon dioxide
increases ( e.g. in respiring tissues), the
dissociation curve moves to the right, so it gives
up oxygen more easily. This is known as Bohr’s
effect .

r
1. The significance of this ( the importance of the effect of carbon

ab
dioxide on Hb )

lg
Carbon dioxide influences the percentage saturation of Hb with oxygen
1. Where in cells with high rate of aerobic respiration(active cells) , where there is high demand of
oxygen , and High pCO2 So the affinity of haemoglobin for oxygen is reduced So,,
iha
haemoglobin releases more oxygen much more easily (i.e more oxyhaemoglobin dissociates)
than it would be at lower concentration of carbon dioxide. So more oxygen for respiring
cells readily available to meet the demand for increase in respiration, in other words provide
.N

sufficient oxygen for respiration.

2. In lung capillaries,where carbon-dioxide levels are relatively low , making it easier for oxygen to
Dr

bind to the haemoglobin ( increase in affinity of haemoglobin to oxygen).

D. The fetal haemoglobin

fetus depends on its mother to supply it with oxygen.

If blood of fetus had same affinity for oxygen as the blood
of mother, very little oxygen would be transferred.
[Link] haemoglobin: has higher affinity for oxygen than
adult haemoglobin So can remove oxygen from
maternal blood even at low PO2.
[Link] addition, that maternal and fetal blood run in opposite
directions thus maintaining a steep concentration gradient
between mother’s blood and that of fetus.

[Link] Gabr 042

 2. Describe how carbon dioxide play a role in the unloading of oxygen from haemoglobin ;

r
ab
lg
Blood is carried in the blood in three different ways;
• 5% as un dissociated carbon dioxide ( CO2) in solution in plasma .
iha
• 85% as Hydrogen carbonate ions( HCO3 ) in solution in the plasma .
• 10% Combined with -NH2 groups of haemoglobin forming carbamino-haemoglobin.

1. Carbon dioxide diffuses down steep concentration gradient from tissue into capillaries and some
.N

dissolve in the plasma (5% CO2).

2. Some of the carbondioxide diffuses into the red blood cells .
Dr

A. Carbonic anhydrase which catalyses the reaction between carbon dioxide and water in cytoplasm
of RBC to form carbonic acid , so very fast reaction, thus maintaining steep concentration gradient for
diffusion of carbon dioxide from tissue to blood.
- Where Carbonic acid then dissociates into hydrogen ions ( H ) and hydrogen carbonate ions (HCO3).

- HCO3 Will diffuse out of the red blood cells into plasma, Where 80-90% of CO2 is transported as
hydrogen carbonate ions in the plasma Where the reaction maintains the concentration gradient
for carbon dioxide from tissue to blood, also if carbon dioxide is transported as CO2 ( which is acidic)
the pH will decrease, but HCO3 ions are alkaline acting as a buffer.
[Link] Gabr 043
- H : Haemoglobin has higher affinity to Hydrogen ions than oxygen. Hydrogen ions react with
haemoglobin forming haemoglobinic acid, ( HHb ), i.e Hydrogen ions promotes the
oxyhaemoglobin dissociation by Causing a change in tertiary structure in oxyhaemoglobin
causing release of oxygen. Increasing supply of oxygen to respiring tissues.
• So this shows that the higher partial pressure of carbon dioxide, causes the haemoglobin to release
more oxygen ( Bohr shift) .

B. Formation of carbaminohaemoglobin:
Where haemoglobin has higher affinity for carbon dioxide than oxygen, so in high pCO2 , some carbon
dioxide in RBCs combines with terminal amine groups (-NH2) of some of haemoglobin molecules ,
forming carbamino- haemoglobin. So stimulating haemoglobin to release more oxygen in areas of
low pO2. 10% is of carbon dioxide is carried in this way.

r
ab
lg
Carbon dioxide passes into the plasma and RBCs
by diffusion. It combines with water to form
iha
carbonic acid, catalysed by the enzyme carbonic
anhydrase.

Carbonic acid dissociates to give

.N

hydrogen ions and hydrogen

carbonate ions.
Dr

Hydrogen carbonate ions pass out of the red

blood cells by diffusion, and chloride ions move
in. This is called the chloride shift( which is an
Haemoglobin acts as a buffer, exchange of ions that takes place in our RBCs to
accepting the hydrogen ions to form ensure no build up electric charges takes place
haemoglobinic acid to avoid changing during gas exchange.
the pH of blood.

Another figure showing the transport of carbon dioxide from tissues to lungs .

Important notice:
That as carbon dioxide builds up, it affects the pH and this
has an effect on the protein structure, so haemoglobin does
not work as well (i.e it has a lower affinity for oxygen)

[Link] Gabr 044

3. What happens when blood reaches the lungs;

When blood reaches the lung , the whole reaction go into reverse .
The alveoli has low pCO2, and high pO2. So carbon dioxide will diffuse out of the blood into the
air in the alveoli/lungs.
This stimulates :
1. The carbon dioxide in the carbamino-haemoglobin to leave the red blood cell
2. And hydrogen carbonate and hydrogen ions to recombine forming carbondioxide molecules
once more ( where carbonic anhydrase catalyse the reverse reaction in lungs, and hydrogen
carbonate ions act as buffer in plasma)
This leaves the haemoglobin molecules free to combine with oxygen, ready to begin another
circuit of the body.

r
ab
lg
iha
.N

Actively respiring cells At lungs

Dr

Low pO2 High pO2

High pCO2 Low pCO2

Lower pH Higher pH

Higher temperature Lower temperature

More oxygen released More oxygen combining

Exam tip:
When asked to explain the difference between the dissociation curve?
1. Dissociation curve of ....x...is shifted to (right/left) in respect to ...y...dissociation curve.
2. Haemoglobin affinity in ....x.... (lowered/ increased)
3. At low PO2 , the percentage saturation of haemoglobin is lower/ higher
in ...x.....than..y....
4. (Name Organism) needs more oxygen , for more respiration for more activity and
higher metabolic rate.

[Link] Gabr 045

 E. Problems with oxygen transport

A. At high altitude:

How people become adapted to low pO2 at high altitudes:

Notice : haematocrite ( proportion of the blood composed of Red blood cells).
Description:
1. At high altitudes , partial pressure of oxygen is lower than that at sea level, so less oxygen in
inhaled air.
2. Haemoglobin is less well saturated with oxygen ( about 70%) and person may suffer from
altitude sickness, where less oxygen. Less respiration. So altitude sickness.
3. So
A. they produce more red blood cells.

r
- So compensating for smaller volume of oxygen absorbed (lower saturation of Hb).

ab
B. Increase in breathing rate , heart rate.
C. Increase in capillary density and number of mitochondria.
- So tissues can receive sufficient oxygen .
lg
How hypoxia( where body tissues don’t receive an adequate oxygen supply) occurs when
a person ascends from sea level to a high altitude
Lower partial pressure of oxygen at high altitude.
iha
So less oxygen in inhaled air.
Decrease diffusion ( pressure gradient) between alveoli and blood.
Less oxygen enters pulmonary capillaries.
So percentage saturation of haemoglobin is lower, as as haemoglobin has lower affinity for
.N

oxygen at high altitude than at sea level.

Plus the person has insufficient red blood cells to compensate.
Dr

[Link] Gabr 046

 Third: 1B.3 structure of veins, arteries and capillaries &
their functions. :
There are three main types pf blood vessels: arteries, veins and capillaries.

General structure of each artery and vein consists mainly of three layers:
1. Tunica Intima: endothelium (lining tissue)made of α single layer of flat (thin)
cells (squamous epithelium) , forming a very smooth layer facing the lumen ,
which minimises the friction with the moving blood.
2. Tunica Media ( middle layer): made of smooth muscles, collagen and
elastic fibres.
3. Tunica Externa (external layer) consists mainly of elastic fibres & collagen
fibres ( which gives general strength & flexibility to both arteries & veins)

1. Arteries

r
ab
Carry blood, under relatively high pressure, away from the heart to all body cells.
All arteries carry oxygenated blood except for pulmonary and umbilical arteries ( during pregnancy carry
deoxygenated blood from fetus to placenta)
lg
The external layer
of tough The middle layers of
tissue(collagen). artery wall contain elastic
fibres&smooth muscles;
iha
arteries nearest to the
heart have more elastic
fibres, those further from
the heart have a greater
proportions of muscle
.N

tissue.
Dr

Lumen is small when artery The endothelium forms a

unstretched(recoil) by flow of smooth lining which allows the
blood from heart easiest possible flow of blood.

Overall shape:
Thicker tunica media (thick wall) than external layer.
A thick layer of smooth muscle and elastic tissue.
Appears in cross sectional area as well defined oval shape , with narrow lumen in relation to the
thickness of wall.
Folded endothelium (tunica intima).

Adaptation of arteries:
1. Tunica Intima(endothelium):
- Single layer of flat thin cells with smooth surface facing the lumen to maintain smooth flow with least
possible frictional resistance to blood flow.
- It is folded to increase the diameter of lumen (allow expansion/stretching) of artery during
ventricular systole to avoid damage of endothelium.

[Link] Gabr 047

2. Tunica media (middle layer):
- Thicker with more Smooth muscle and elastic tissue to maintain blood pressure and maintain
blood flow.
- Smooth muscles to contract and relax changing volume of blood delivered by changing diameter
of artery .
- Thick tunica media ( with thick elastic tissue, muscles) with lots of collagen fibres to withstand
high pressure without rupture.
- Elastic tissue allow stretching and recoiling of arteries to smooth out flow of blood,
maintain blood pressure .
Notice
1. Artery stretch (becomes wider) when high blood pressure surges into them during Notice
ventricular systole so widening the lumen of artery, reducing pressure a little , and
accommodate the greater volume of blood without being damaged (so
doesn’t rupture with the help of presence of collagen in walls to increase the
strength).
2. Artery recoil (unstretch) inwards ( becomes narrower) as the low pressure blood surges into
them during ventricular diastole , thus helping to maintain high pressure and rapid blood flow.

r
3. The blood pressure in all arteries is relatively high, but it falls in arteries further away from the

ab
heart. These are known as peripheral arteries.
Arteries further from the heart have fewer elastic fibres in tunica media, but more proportion of
smooth muscle.
Also arterioles ( smaller branches of arteries) have larger proportions of smooth muscle As
muscles can contract.
reducing blood flow..
lg
Narrowing diameter of arteriole to increase resistance
thus helping in controlling the volume of blood flowing into tissues and
So

different times( vasodilation and vasoconstriction)

iha
3. Tunica externa(external layer)
Contains elastic fibres and collagen fibres to withstand high pressure of blood and prevent bursting
as collagen gives strength.
.N

4. Narrow lumen: to keep blood flowing under high pressure where the further the artery from the
heart , the narrower the lumen Which help resist the flow of blood at arteries away from heart. Thus
Dr

keeping blood pressure in arteries high.

Exam tip:
If asked about adaptation of
aorta
Write same as any artery in
addition to
• It branches to supply blood to
different parts of body
• Has semilunar valve to prevent
back flow during diastole.
[Link] Gabr 048
 2. Veins

Return blood from body organs to the heart.

All veins carry deoxygenated blood except for pulmonary and umbilical veins.

Smooth inner surface Relatively thin layer of

smooth muscle with
elastic fibres

Relatively large
Outer tough layer
lumen
consisting mainly of collagen
fibres

Overall shape:

r
Thinner tunica media/ thinner walls with less smooth muscle as blood is flowing under low pressure and
less elastic tissues as it doesn’t need to stretch and recoil.

ab
A thin layer of smooth muscle and elastic tissue
Appears in cross sectional area with irregular oval/ flattened shape , with wide lumen in relation to the
thickness of wall. lg
Smooth endothelium (tunica intima).
Relatively thin tunica extrna

Adaptation of veins:
iha
1. Tunica Intima (endothelium):
- There are semilunar valves formed from the endothelium , where these valves allow blood to flow
towards the heart in one direction , preventing its back flow.
.N

2. Tunica media:
- With less elastic fibres and smooth muscles as blood is flowing under low pressure in veins so blood
vessels don’t need to stretch .
Dr

3. Thin wall as blood pressure is low and to be easily affected by the contraction of the surrounding
skeletal muscles allowing blood in veins to flow.
Also with less collagen in walls because blood pressure is low.
4. Wide lumen:
- To reduce the resistance to blood flow .

Explain how blood flow in vein?.

Veins are surrounded by skeletal muscles.
Veins have thin wall to be easily affected by the contraction of the
surrounding muscles.
Contraction of muscles causing semilunar valve opens, and squeeze
blood up along the veins through valves.
So valves allow blood to flow in one direction (towards the heart)and
its closure prevents its back flow.
Also the negative intrathoracic pressure during inspiration also helps ensure returning of blood to heart.
[Link] Gabr 049
 A back flow of blood will close the valve ,
Blood moving in the direction of the heart forces
ensuring that blood can’t flow away from the
the valve open, allowing the blood to flow through.
heart.

3. Capillaries

Their function is to take blood as close as possible to all cells, allowing rapid transfer of substances
between cells and blood.

r
The capillary network links the arterioles and the venules.

ab
Capillaries form a network(capillary beds) throughout every tissue in the body except in cornea and
cartilage.
lg
iha
.N

Overall shape:
Made of single layer of endothelial cells. One cell thick.
Have many endothelial pores .
Dr

Small diameter ( ~7μm) about same diameter as red blood cell.

Large surface area to volume ratio.
Adaptation of capillaries:
1. Endothelium layer (i.e wall is made of endothelial cells , which is one cell thick)
- For shorter distance of diffusion of molecules So higher / faster rate of diffusion.
-
2. Endothelial pores:
- To allow small molecules as water and low molecular mass solutes as glucose and ions to leave the
blood into tissue fluid, and prevent large molecules such as plasma proteins from leaving blood.

3. Narrow lumen(small diameter) about 7μm.

Almost same diameter as red blood cells. Thus slowing down flow of red blood cells for sufficient
oxygen to diffuse out to cells.
Allow red blood cells to be close to body cells for efficient diffusion.
Also allow blood containing nutrients such as glucose to be in close contact with many body cells.
Also the small size , with very thin walls of capillaries allows them to be extending into small spaces
fitting between individual cells to reach and contact with many cells, allowing rapid diffusion of
substances between blood and cells.
[Link] Gabr 050
4. Large capillary network so :
Large surface area to be able to reach all cells
Large surface area to volume ratio. to slow down the flow of blood For more exchange of
substances.

Blood pressure, velcocity in different regions of the human circulatory

system.:

r
ab
From A to B
Decrease in blood pressure in aorta
Heart is in diastole
No blood entering aorta. lg
Blood is leaving the aorta.

Distance from left ventricle

iha
Change in
pressure Change in velocity vs total
cross sectional area.
.N
Dr

Causes of blood
pressure reduction Y
in capillaries: Z
Leakage of tissue
fluid
Large surface area.
Long distance from
heart.

X total cross-sectional
area.
Y velocity of blood
flow
Changes over all Z pressure of blood.

[Link] Gabr 051

 r
ab
lg
iha
.N
Dr

Explain why blood samples are normally taken from veins rather than arteries?.
Arteries have blood flowing under higher pressure which wouldn’t allow drip. Notice

Besides artery are deeper to reach to insert a needle for drip.

Also there would be a greater blood loss associated with intra arterially .

[Link] Gabr 052

Point of comparison Artery Vein Capillary

Tunica intima 1. endothelium ; single Same as artery Present ( as artery)

layer of flat thin cells
with smooth surface.

r
Tunica media Thick Thin Absent

ab
Tunica extrna Contains both collagen Mostly collagen fibres Absent
fibres and elastic fibres.

Lumen Narrow Wide Narrow abou7μm about same size

lg as RBC.

Valves Absent Present as semilunar Absent

valves ensuring one way
flow of blood.
iha
Blood pressure High Low (lowest) Falling/ decreasing

Blood flow(velocity) Rapid Slow (but faster than Slow

capillaries)
.N

Pulsation Pulsates Doen’t pulsate Doesn’t pulsate.

Linking structure to Thick walls to withstand Valves to prevent back Porous wall to facilitate exchange of
Dr

high pressure flow of blood. substances.

function
Narrow lumen to maintain Thin wall to be easily Wall is made of endothelial cells,
blood pressure. affected by the which is one cell thick for shorter
No valves due to high contraction of the diffusion distance of molecules.
pressure. surrounding muscles.
Wide lumen to reduce
resistance to blood flow.

[Link] Gabr 053

 Fourth: 1B.4 The mammalian heart :
[Link] structure: Walls of the heart are made from cardiac muscle.

1. Made of 4 chambers:
- 2 upper thin walled atria
- 2 lowered thicker walled ventricles.

The right side of the heart receives blood from systemic circulation and pumps it to the lungs.
The left side of the heart receives blood from lungs and pumps it around the rest of the body.

Why atria have thinner muscular walls than ventricles?

- It receives blood at low pressure from vena cava .
- Also, Atria pump blood for shorter distance into ventricles , while ventricles pump blood a long
distance.
- So Ventricles need to overcome greater resistance in blood vessels.
- So atria needs to generate lower pressure than ventricles.

r
ab
Why wall of left ventricle is thicker ( with more muscles) than that of right ventricle?
- To generate higher blood pressure during systole
- So can over come higher resistance to flow of blood to arteries due to their narrow lumen ( also
lg
overcome the elastic recoil of arteries).
- So it can transports blood to a greater distance which is all body organs except lungs.
- While right ventricle generates low pressure to avoid damaging of capillaries in the lungs.
iha
Carotid arteries to
neck and head
Aorta
Right pulmonary
artery ( to right Left
.N

lung) pulmonary artery

(to left lung)
Dr

Left pulmonary vein

Superior vena cava receiving
( from left lung)
blood from the head, neck ,
arms&chest.
Right pulmonary Left atrium
vein( from right lung)
Semilunar valve Semilunar valve
Bicuspid valve
Right atrium
Tendinous cords
Tricuspid valve

Thicker cardiac
Inferior vena cava
muscle of left
collecting blood
ventricle
from lower part of Aorta
the body. Thinner cardiac muscle
Apex of the heart
of right ventricle

[Link] Gabr 054

2. Valves:
- 2 atrioventricular valves( bicuspid with 2 flaps and tricuspid with three flaps)
- 2 semilunar valves

Function of valves?
- Valves open to allow blood to flow in one direction( from... to ...) , and close to preventing its back
flow, thus maintaining pressure and steep concentration gradient for oxygen and carbon dioxide.
- Function of semilunar valves
Located between ventricles and their respective arteries preventing back flow of blood from aorta to
left ventricle and from pulmonary artery to right ventricle.

How atrioventricular valves are adapted?

- Where the cusps of valve are attached to the inner heart
walls (papillary muscle) by tendinous cords, which when
contracts pull on tendons allow the valve to close& hold
the cusps of valve in place, thus preventing the valve

r
from opening inside -out ( i.e opening in opposite

ab
direction).

3. Coronary arteries:
lg
- Blood vessels which supply the heart muscle with
iha
a constant supply of nutrients and oxygen to be
used in aerobic respiration to release energy need
for contraction.
- Branching directly from aorta as it is much fast to
.N

reach muscles
- Also aorta is closest blood vessel carrying
Dr

oxygenated blood so supplies coronary artery with

highest level of oxygen.

4. Septum:
- Divide human heart into left and right side .
- Keeping oxygenated and deoxygenated blood separate .
- Allowing sufficient oxygen being carried to the body tissues.
- Also allow blood to be pumped under two different pressures, lower pressure to lungs and
higher pressure to all body parts.
5. Myoglobin:
A respiratory pigment which has a stronger affinity for oxygen than haemoglobin , thus
myoglobin stores oxygen for respiration needed to keep the heart contracting regularly.

[Link] Gabr 055

 2. How your heart works:

How can you hear your

heart beats?

You can use a stethoscope where

you will hear a lub- dub sound.
As the sound of the heart beat is the sound of heart valves. Each complete lub- dub represents
one heart beat.
The rate of heart beat shows how frequent your heart is contracting

r
ab
The Lub is caused when ventricles The dub is when ventricles relax and a
contract and the blood is forced against back flow of blood hits the semilunar
atrioventricular valves causing the
lg valves in the pulmonary artery and aorta
closing of the atrioventricular valves( causing the closing of the semilunar
valves leading to the ventricles) valves( valves leading out of the heart)
iha
.N
Dr

[Link] Gabr 056

 3. The cardiac cycle:
The cardiac cycle is the sequence of events which make up one heart beat.
It involves ( Atrial systole, ventricular systole and Diastole)

1. Atrial systole (0.1 seconds):

- When atria are full ,Both contract and volume
of atria decrease.
- Blood pressure in atria increases.
- Blood pressure in atria is higher than in the
ventricles.
- Atrioventricular valves open.
- More Blood flow into the the ventricles.
- Semilunar valves are closed.
2. Ventricular systole ( 0.3 seconds):

r
- Waves of excitation , passes down walls of

ab
ventricles .
- Both ventricles contract together from the lg
base and upwards , so ventricular volume decreases.
- Blood pressure in ventricles increases.
- So pressure in ventricles is greater than atria which pushes up against the
iha
cusps of AV valves. So AV valves close.
• Notice : the contraction of papillary muscles , attached to valves by tough
tendinous cords, prevent AV valves from being turned inside-out by
.N

pressure exerted when ventricles contract.

- Blood pressure in ventricles greater than in artery.
Dr

- Semilunar valves open

- Blood flow s into arteries to..(lungs/and rest of body).
3. Diastole( 0.4 seconds):
- Atria and ventricles relax.
- Pressure in ventricles decreases ( pressure of blood in arteries is higher than than in ventricles) , causing a
slight back flow of blood Where blood fills the semilunar valve cusps ( causing pressure of blood to
push into the cusps of semilunar valves) . Causing them to close.
- Blood flows from the veins through the atria where pressure builds up and opens the AV valves and
ventricles starts to fill with blood too.
- Notice: inferior vena cava collects deoxygenated blood from lower parts of body , while superior vena cava
receives deoxygenated blood from head, neck , arms and chest . Deoxygenated blood delivered to to the
right atrium.
[Link] Gabr 057
 Notice

The pressure changes in the left side of the heart during the cardiac cycle.

Aortic valve

Aortic valve

r
Bicuspid valve
Bicuspid valve

ab
0s
lg
0.1s 0.4s 0.8s
iha
Atrial Atrial
systole Atrial Diastole systole
.N

Ventricular Ventricular systole Ventricular Diastole

Diastole
Dr

Point of comparison Diastole 0.4s Atrial systole 0.1s Ventricular systole

0.3s

Chambers Atria and ventricles Atria contract Ventricles contract

relax Ventricles relax Atria relax

Pressure Slightly higher in atria Higher in atria Higher in ventricles

Valves Semilunar valve close Semilunar valve close Semilunar valve open
Atrioventricular valve Atrioventricular valve Atrioventricular valve
open open close

Blood flow Cardiac filling From atria to ventricles From ventricles into
Ventricular filling major arteries.
Ventricular evacuation.

Volume of ventricles 0% to 70% 70% to 100% 100% to 0%

[Link] Gabr 058

 4. The initiation and control of heart beat :
Cardiac muscle differs from the muscle in all other areas
of the body in that it is myogenic. This means that it
naturally/ automatically contracts and relaxes; it does not need to receive impulses from a nerve to make it
contract, as it initiates its own rhythm via SAN.
If cardiac muscle cells are cultured in a warm, oxygenated solution
containing nutrients, they contract and relax rhythmically, all by themselves.
Also strongest muscle in the body as it beats through out life time.

Notice

r
ab
Atrial systole Atrial diastole

Ventricular
diastole
Ventricular systole
lg Ventricular diastole

0 0.1 0.2 0.3 0.4 0.5 0.6 0.7 0.8

iha
Seconds

How to calculate the heart rate: Table shows change in volume of blood in the left
.N

Example: ventricle during one second.

One beat
Dr

1-0.2 = 0.8s Find two identical consecutive points

So heart rate= 60 /8= 75bpm (0.2s - 1 s) then this represents 1 beat
1.0 - 0.2= 0.8s
1 beat =0.8s
X beats=60s
So 60/0.8= 75 bpm

[Link] Gabr 059

 Fifth: 1B.5 atherosclerosis :

1. Cardiovascular diseases:
- Disease of heart , and blood vessels, example narrowing of lumen, high blood pressure,
thrombus, reduced blood supply .
- In other words ,diseases of the heart and circulatory system many of which are linked to
atherosclerosis.

2. Atherosclerosis: Artery walls

- A condition in which yellow fatty deposits build up
on the lining of the arteries(plaque), causing
Smooth normal
narrowing of arterial lumen, thickening and endothelium

r
hardening of arterial walls which result in many
health problems.

ab
Slight damage to the endothelial cells lining the
artery leads to an inflammatory response, followed
How atherosclerosis develop : by a build up of cholesterol

1. Endothelial lining of arteries is damaged ( caused

lg
by high blood pressure, and substances in
tobacco smoke, stress, free radicals).
2. Body’s inflammatory response takes place, where
White blood cells arrive at the site of damage .
iha
Fatty deposits grow to form an atheroma.
3. These cells cause the accumulation( building up)
of chemicals from blood such as cholesterol.
4. This leads to formation of atheroma (plaque) on
the endothelial lining of the artery.
5. Also fibrous tissue and calcium salts build up
.N

around the atheroma, turning it into hardened

plaque. Fibrous tissue and calcium salts build up around the
6. Narrowing in diameter (lumen) and loss of atheroma forming a hardened plaque which narrows
Dr

elasticity of arteries. the artery and makes the walls rigid.

7. This cause an increase in blood pressure which

cause more damage in other areas of endothelial
lining and more plaque will form.
8. This cause the increase in risk of formation of
blood clots,
9. So reduced supply of oxygen , glucose and
nutrients to tissue.
10. Leading to myocardial infarction (heart attack), or
angina .

Why atherosclerosis is more likely to occur in arteries than in vein :

1. Blood in arteries flow under relatively high pressure , which put more strain on endothelial
lining of vessels and can cause small areas of damage.
2. While in vein pressure is lower so damage to the endothelium is much less likely.

[Link] Gabr 060

3. Effect of atherosclerosis on health:
Consequences of
atherosclerosis

Weakening of blood vessel Incomplete blockage Complete blockage

Reduced blood supply Brain

Increased Angina Heart
Aneurysm blood pectoris Myocardial Stroke
pressure infarction

1. Aneurysm :
• Where if an artery is narrowed by plaque, blood tends to collect behind the blockage.
• The artery bulges (swell) and the wall is put under more pressure than
usual , so it becomes weakened (aneurysm).
• The weakened artery wall may split open, leading to massive internal

r
bleeding Leading to massive blood loss. And drop in blood

ab
pressure.
• This happens in the blood vessels supplying the brain or in the aorta.
• If early diagnosis takes place to aneurysm , it can be treated by surgery before they burst.
lg
2. Raised blood pressure:
Narrowed arteries due to plaque on walls cause raised blood pressure.
iha
Which damages the tiny blood vessels
Effect on kidney:
If those vessels are feeding kidney tubules, high blood pressure may force protein molecules
.N

out their walls( doctors can test for protein in urine as a sign of kidney damage).
Effect on retina:
Tiny blood vessels supplying retina are easily damaged, thus if become blocked or leak, their
Dr

will be deficiency in oxygen supply to retinal cells, which would die and cause blindness.
Effect on brain
Stroke, Caused by bleeding from damaged capillaries in the brain, or blockage cutting blood
supply to brain .

3. Heart disease (CHD):

Angina and myocardial infarction (heart attack) are the
two most common heart diseases.

[Link] Gabr 061

1. Angina:
1. Plaques builds up slowly in coronary arteries. Resulting in a decrease in diameter of
coronary arteries Reducing blood flow to the parts of heart muscle beyond(after) the
plaque. So heart muscle receives less oxygen
and glucose. So heart muscle resorts to
anaerobic respiration leading to build up of lactic
acid and death of some muscles.

2. Symptoms:
usually first noticed during exercise, as cardiac
muscle is working harder and needs more oxygen .
The anaerobic respiration in cardiac muscle cause

r
gripping pain in chest that extend to particularly left

ab
arm, jaw and cause breathlessness.
These symptoms subside( become less intense)
once exercise stops. lg
3. It can be managed by :
• taking regular exercise
iha
• losing weight
• Stop smoking
• Reducing fat intake.
.N

4. Treatment:
Symptoms treated by resting and drugs that cause rapid dilation of coronary arteries so
Dr

supplying cardiac muscle with oxygen needed.

If it gets worse, other drugs used to dilate blood vessels and reduce heart rate.
In sever cases, they use a stent to be inserted in the narrowed arteries to hold them open, or
use by pass surgery .

[Link] Gabr 062

 2. Heart attack:
1. Caused mainly by blood clots( thrombosis) resulting from atherosclerosis where:
1. Plaques builds up slowly in coronary arteries. damage the walls of arteries.
Followed by formation of blood clot by:
• where platelets touch the damaged surface of the plaque triggering the clotting process.
• The plaque itself may rupture and break open, and the released cholesterol will cause the
platelets to trigger the blood clotting process.

2. Or platelets touch the damaged endothelial

lining( caused by high blood pressure or smoking)
triggering the clotting process.

r
Clot formed in coronary arteries known as coronary

ab
thrombosis Blocking the coronary artery. So part of
heart muscle is permanently starved of oxygen. Muscles
resort to anaerobic respiration. Lactate produce and
lg
accumulate in the cells. Lowering pH so enzymes denature
and cells die. Leading to heart attack .
iha
2. Symptoms:
Pain in chest at rest that extend to particularly left arm, jaw and cause breathlessness., much
more sever than angina.
.N

It may occur at any time, though exercise may start it and often lasts for several hours.
Death may occur very rapidly with no previous symptoms, or it may happen after several days
of feeling tired and suffering symptoms mistaken for indigestion.
Dr

3. Treatment:
Not relieved by rest and vasodilation alone.
React quickly giving two full strength aspirin tablets to help stop blood clotting and send them
to hospital as fast as possible .

Notice:
1. Coronary arteries are like an inverse tree, in other
words branching downwards with larger branches
splitting into smaller ones .
2. So the extent of damage is based on on how high
the blockage is.

[Link] Gabr 063

4. Stroke:
- Caused by an interruption to the normal blood supply to an area of the brain,
Causes :
1. Bleeding from damaged capillaries
2. Or blockage of cerebral artery due to blood clot , an
atheroma or combination of both cutting off the blood
supply to the brain .
Notice if blockage is in one of the main arteries leading to the
brain causes a very serious stroke that can lead to death, but
if its in one of smaller arterioles leading into brain , the effect
may be less disastrous.

Symptoms:
It varies depending on how much of brain affected .
Dizziness, confusion, slurred speech, blurred vision, or partial loss of vision,and numbness.

r
In more sever strokes, there can be paralysis, usually in one side of body.

ab
lg
iha
.N
Dr

[Link] Gabr 064

Topic 1C

Introduction to
cardiovascular
health and risk

r
Understand how people’s perception of risks is

ab
often different from actual risk.
Distinguish between correlation and causation.
lg
Investigating the causes of CVDs.
iha
Evaluate the design of studies used to determine
health risk factors, including sample selection
and sample size used to collect data that are
both valid and reliable.
.N

Knowing how factors such as diet, high blood

pressure, smoking and inactivity increase the risk
Dr

of cardiovascular disease.

Dietary antioxidants and cardiovascular disease.

A. Know how factors such as diet increase the risk of CVD.
B. Analyse data on the possible significance for health of blood cholesterol
levels and levels of HDL and LDL.
C. Know the evidence for a causal relationship between blood cholesterol level
( total cholesterol and LDL) and cardiovascular disease.
D. Understand how people use obesity indicators such as BMI and waist to hip
ratios.

Dietary antioxidants and CVS.

Benefits and risks of treatment.

[Link] Gabr 065
 1C.1 Risk, correlation and cause:
According to whether the disease in transmissible and caused by pathogen or not , it is sub-
classified into;
A. Non- Infectious disease: (non communicable.)
Not caused by pathogens and non transmissible.
long term degenerative disease.
Example:
1. Deficiency diseases as anemia and marasmus.
2. Inherited ( genetic diseases) as sickle cell anemia and cystic fibrosis.
3. Heart disease , or cancer.
B. Infectious disease: ( communicable)
A disease caused by pathogens and transferred from one person to another ( transmissible).
For many diseases
you can increase or
lower the risk of

r
becoming ill based on

ab
factors in your lifestyle.

• Risk:
The probability that an event will take place.
lg
• Probability:
A measure of the chance or like hood that an event will take place, which is
calculated mathematically.
Example :
iha
The probability of getting out the pink ball is :1 in 6 or 0.17 or 17% .
• Risk factors:
Factors which affect the risk of an event happening.
.N

Steps
1. Identify risk factors that may contribute to the cause of disease.
2. Look at people who have same factors (e.g smoking)
Dr

3. Compare their risk of the disease with the average risk for the whole
population.

Multifactorial disease:
A disease which can result from the interactions of many different factors, not from one simple
cause, in other words many factors influencing your chance of having a disease.

Types of risks

Actual Perceived
Probability of an event Perception of people of a certain risk.
occurring at a certain time. Not always as the actual risk.
Example: motorcycles and Affected by
car death risks. [Link]
[Link]
[Link]

[Link] Gabr 066

 Epidemiology:
Study of the spread of disease and the factors that affects it.
The branch of medicine which deals with the incidence, distribution, and possible control of diseases.

Correlation: Causation
A strong tendency for two sets of data to When a factor directly causes a
change together (indirect). specific effect.
A change in one variable is accompanied In other words a causal relation ship
by a change in another variable. involves: change in one variable
Proven by statistical analysis.
directly result in change of another
Example: mortality data from
variable,
atherosclerosis may change in a similar
A change in one variable is caused by a
pattern to a-life style factor such as change in another variable.
smoking or lack of exercise. Proved by lab tests.
However, this still doesn’t prove that one Example: increase in blood cholesterol

r
is the cause of the other, so further
level causes an increase in risk of CVD.

ab
research is always needed to
demonstrate a causal link.

Causation was established by further research and lab

A Spanish study showed that there is a
lg testes including :
Correlation between smoking and incidence of Tobacco smokes contain substances that damage
iha
death from atherosclerotic heart disease. endothelium lining of arteries , increasing plaque
Where smoking increase risk of death from formation , thus narrowing of arteries lumen
atherosclerotic heart disease. Increasing blood pressure increasing risk of
atherosclerosis.
.N

percentage of the population affected

Dr
Percentage of the population affected

50

37.5

25

12.5

0
death from CVD obese overweight diabetes

The figure shows the percentage of deaths in the UAE from cardiovascular disease
each year . It also shows the statistics for obesity and diabetes.
This data suggest a possible correlation between obesity and heart disease.
However: you can’t set a conclusion on a set of data .
[Link] Gabr 067
 Positive correlation: Negative correlation: No correlation:
As one variable ( ex As one variable ( ex There is no connection
increase in age) increase the increase in level of activity) between the two variables.
risk of CVD. decrease the risk of CVD.

1C.2 investigating the causes of CVDs:

r
ab
A. Designing studies:
Its how to evaluate the design of studies to decide if data are meaningful
1. Should be based on very big sample size.
2. Investigating one variable effect while keeping all other variables same (controlled), which is

3.
lg
usually impossible when working on human beings.
Carry the study over a long time( longitudinal studies) at least one year.
Thus tracking the impact of their known life style over time.
iha
4. You can add safety precaution ( like choose people with no risk of CVD/healthy) to make the study
on.
Types of studies
.N

Cohort/ Longitudinal studies Case-control studies

Start with a normal group
Dr

Group with disease Group without disease.

[Link] some to risk factors.
[Link] remain unexposed. Data is collected through questionnaires.
Advantage: easy , quick and large sample size.
Scientific studies which follow the same Disadvantages: some people might forget or
group of individuals for many years don’t say the truth.

” Ideally, the controls are similar to the

cases in every way, except
they do not have the disease or
condition of concern.

[Link] Gabr 068

Cohort / longitudinal study: classified a
group according to exposure.
Vs Case-control study: identifies group of people
with a disease and selects control group without
disease.
Exposure Disease
Exposure Disease
Exposed
? ? Yes (case)
Unexposed
No (control)

Metadata analysis (meta-analysis)

When data from all the available studies in a particular area are analysed.
This is to give more reliable evidence .

[Link] scientific studies:

r
ab
1. Valid
lg
An investigation which is well designed to answer the question being asked.
iha
Refers to proper methodology.
It is the extent to which the instruments that are used in the experiment measure exactly what
you want them to measure.
Measurements are affected by a single independent variable, while all other variables apart from
.N

independent variable have been controlled.

No observer bias.
Dr

2. Reliable
Is about the consistency of a measure.
It is the extent to which the outcomes are consistent when the experiment is repeated
more than once.
Repeated by other scientists and they had similar results, in other words include repetition and
comparing with other scientists who got similar results.

3. Precise:
Measurements with only slight variation/difference between them, in other words taking proper
measurements.
Precision refers to how close measurements of the same item are to each other.
Example: recalibration of tools, using colorimeter.

4. Accuracy
Accuracy refers to how close a measurement is to the true or accepted value.
 r
ab
lg
iha
.N
Dr

Valid, reliable and precise are important in evaluating all practical

work.

4. Biased
when some one is unfairly for or against an idea( e.g when a scientist is paid by someone with
a vested interest in a specific result- they may receive benefit from the outcome)
So its important to know who carried out the research, who funded it, and where it was
published.
5. Evaluate
To access or judge the quality of a study and the significance of the results.

[Link] Gabr 070

 Reliability can be
evaluated using
Error bars

r
ab
Group 1 Group 2 Group 3

Mean value 14.95 15.79 18.51

Standard deviation
lg 3.71 4.27 3.92

Error bars can represent minimum and maximum data in a ranged set of data , so error bar
iha
shows the spread of data around the mean as they connect the highest and lowest values.
The larger the error bar the lower the reliability and vice versa.
.N

Longer values : more

spread out ,data is
Dr

more variable from Shorter values: low

the mean so less spread out, data are
reliable. clumped around the
mean / less variable
from mean so more
reliable.

[Link] Gabr 071

 C. (1C.3)Risk factors for CVDs

r
Factors affecting the probability of something to happen.
Notice that CVDs are multifactorial meaning having multiple

ab
risk factors.

A. Modifiable
Changeable
lg [Link]
modifiable
Non changeable
iha
1. Smoking
.N
Dr

1. Nicotine:
• increasing adrenaline which in turn increase heart rate,and increasing blood pressure.
• Constricts blood vessels, thus increasing blood pressure .
2. Carbon monoxide:
• Binds irreversibly to haemoglobin forming carboxy-haemoglobin, so less oxygen being transported to body
tissues including heart muscles.
3. Smoke particles:
damage endothelium lining of arteries , increasing plaque formation , thus narrowing of arteries lumen
Increasing blood pressure increasing risk of atherosclerosis.

[Link] Gabr 072

 2. Lack of exercise
Negative correlation with CVDs.
As exercise is needed to lower blood cholesterol level, prevent obesity , release stress, lower blood pressure,
balance lipoproteins..........thus lowering risk of atherosclerosis and CVD.

3. Diet and weight HDL

They carry
1. Salts: cholesterol
from body
• High salt intake , leafs to an increase in blood pressure. tissues to liver
to be broken
down.
Increase in HDL
2. Lipids (high intake of saturated fats); Decrease in
cholesterol level in
blood.
HDL can help
remove cholesterol

r
from fatty plaque

ab
on arteries
Decreasing risk of
LDL CVDs by
( bind to cell decreasing risk of
membrane lg atherosclerosis.
before being
taken into cells)
Increase in LDL
So cell membrane
become saturated
iha
Increase in
cholesterol level in
blood.
Increasing risk of
CVDs by
.N

increasing risk of So having high HDL to LDL ratio decreases risk of CVDs
atheroma While having high LDL to HDL increases risk of CVDs
Dr

Explain how increase in fat in diet and less physical activity leads to increase risk of CVDs?
1. High energy intake which is higher than energy output.( energy/fat intake> energy output,i.e
less fat burnt)
2. So excess fat is stored in body causing an increase in weight/obesity.
3. Obesity increases risk of diabetes type 2, increase blood pressure, increases LDL to HDL ratio,
thus increasing cholesterol level in blood.
4. Thus damaging endothelium of arteries.
5. Stimulating an inflammatory response ....formation of atheroma
6. Narrowing of lumen of arteries and they lose their elasticity
7. Thus increasing risk of CVDs
So weight loss programs aim to reduce fat
intake and increase regular exercise
So that energy output> energy input

[Link] Gabr 073

[Link] in fruits and vegetables:
Act as antioxidant which reduces free radicals (donate electrons)/ inhibit the oxidation of
other molecules as free radicals cause cell damage.
Also antioxidants reduce plaque and atheroma formation so preventing endothelial damage .

Investigating the causes of CVDs:

Link between dietary antioxidants and risk of CVD:
Eating five or more portions of fruit or vegetables a day can lower your risk of having a heart
attack. It was based on data from longitudinal study of more than 84000 women and 42000 men
over eight years, looking at their fruit and vegetable intake and cardiac

r
health.

ab
lg
iha
.N

Graph shows the impact of eating increasing amounts of fruits and vegetables on the risk for
coronary heart disease.
Graph shows the relative risk of developing coronary heart disease compared to a person eating
Dr

fewer than three servings of fruit and vegetables per day.

We don’t really know how fruit and vegetables have their effect in reducing risk of CVD .
At one time, it was thought the antioxidants found in fruit and vegetables might be the
answer:
How?
1. As antioxidants reduce free radicals ( donate electrons)/ inhibit the oxidation of other molecules
As free radicals cause cell damage
2. Also antioxidants reduce plaque and atheroma formation.

However, recent studies, including some very large metadata analyses , have shown evidence that
antioxidants being good for your heart is inconclusive( not leading to firm conclusion) .

[Link] Gabr 074

Vitamin C case study:
To investigate effect of vitamin C on CVD:
Vitamin C is important in formation of connective tissue in the body such as bones,
teeth, skin and endothelial lining of blood vessels

So lack of vitamin C increase risk of damage of endothelium lining of artery.

arteries to be more likely to be damaged
So atherosclerosis more likely to develop.
So more likely to be affected by CVDs.

Case study

r
Individual study Metadata study

ab
In Finland

A study at the association of vitamin C

lg In 2016, metadata study was published.
in the blood and risk of heart attack in Conclusions were that there was no
1605 men from eastern Finland. relationship between vitamin C and
The men had no signs of CAD when heart health.
iha
tested between 1984 and 1989 , where The study even showed that taking
their vitamin C was also tested. vitamin C supplements could damge
Between 1984 and 1992 a total of a total heart health.
.N

of 70 of men had a heart attack, where Showing a contradictory evidence,

of the men who showed low vitamin C and that scientists must look at all
levels, 13.2% had heart attacks, of that evidence to avoid coming
Dr

compared with 3.8% of the men who to wrong conclusions.

showed no sign of vitamin C deficiency.

[Link] dietary factors:

Alcohol and caffeine consumption.

4. Stress
Increase adrenaline level thus increasing heart rate and breathing
rate as well as blood pressure.

[Link] Gabr 075

 5. High blood pressure
Force exerted by blood on walls of blood vessels... which increases the risk of atherosclerosis....
so hypertension (consistent high blood pressure 140/90 mmHg) is precursor to other CVDs.
How to take a blood pressure reading?
It is measured by sphygmomanometer.
Normal blood pressure is 120/80 mmHg.
Measured at rest
Factors affecting blood pressure:
1. Age
2. Gene
3. Fitness
4. Stress
5. High salt intake

r
6. Lack of exercise

ab
7. High saturated fat intake.
8. Obesity
lg
iha
[Link] modifiable risk factors
Non changeable
.N

2. Age
1. Gender As we get older blood 3. Genetics
Dr

vessels lose part of its

Below 50 years male > female elasticity and get narrower. Includes:
Where risk is lower in women due This leads to hypertension. 1. Tendency to develop
to presence of oestrogen. hypertension.
However, after menopause risk 2. Cholesterol balance in body.
almost become equal. 3. Arteries easily damaged.

Reducing risk atherosclerosis and CVDs?

1. Eating a balanced diet with plenty of fruits and vegetables help prevents atherosclerosis .
2. Not to smoke to help maintain healthy weight to avoid high blood pressure and diabetes type 2.
3. Reduce stress and get plenty of exercise.
4. Take early actions because there is clear evidence of the early signs of atherosclerosis in
teenagers and even younger children , if known factors are already in place.
[Link] Gabr 076
 1C.4 diet and cardiovascular disease:

1. Energy budget:

A term referring to the ratio of energy input (food intake) to output (mainly exercise).
Input> output Output> input
Weight gain ( may lead to obesity) Weight loss

So weight loss programs aim to reduce fat intake and increase regular
exercise
So that energy output> energy input
Solutions might includes taxes on food, town planning to make walking and
cycling easier, education people to prevent childhood obesity

r
2. Measuring healthy weight

ab
[Link] mass index

BMI=
weight in kilograms
lg
This compares your weight to your height in a simple formula;

(Height in meter)2
iha
For an adult, the following definitions apply:
A BMI of less than 18.5 Kgm-2 means you are underweight.
A BMI of 18.5-25 Kgm-2 is the ideal range.
.N

A BMI over 25 and up to 30 Kgm-2 means you are overweight.

A BMI of 30-40 Kgm-2 is considered obese.
A BMI over 40 Kgm-2 defines you as morbidly obese.
Dr

Problems with body mass index:

1. BMI doesn’t recognise difference
between muscles and fats.
2. BMI values underestimate body fat
in older people who have lost a lot
of their muscle mass.
3. So BMI is not a good predictor of
CVDs on its own but combined with
other factors .

[Link] Gabr 077

 Why some people with high BMI don’t believe that they are at risk of developing CVD?
1. BMI is not reliable indicator of obesity in people with a high muscle mass as in case of
athlete’s ( can’t recognise difference between muscles and fats)
2. Lack of education /awareness that BMI is linked to CVS .
3. People with high BMI don’t feel unwell/ they don’t show any symptoms to CVD.

Exam hint
Why do people under estimate risks?
1. Long time for symptoms to appear.
2. Risk is applied on groups rather than individuals.
3. Own Experience contradicts with research, example if they see people smoking, eating
high fat, high salt diet, never exercising and yet appearing well
4. So people then under estimate the risk factors of CVD associated with smoking, obesity,
lack of exercise or a high salt diet.
5. Mistakes when people asses risk, example sometimes people will continue smoking

r
because they don’t want to gain weight as smoking speed up metabolism and reduces

ab
appetite.
6. 6. Calculating personal risk/benefit situation, so easy to think that the immediate
benefit( pleasure in eating high fat food, smoking, not wanting to make effort to exercise)
lg
is more important than the apparently low risk of heart disease.

2. Waist to hip ratio:

iha
Waist to hip ratio is the best measure of obesity and also best way to predict an increased risk
of CVDs.
Waist size (cm)
=
.N

(Hip size (cm)

Waist size gives a good indication of the amount of fat a person is carrying.
Dr

Gender Waist: hip ratio indicating obesity

Male >0.9

Female >0.85

[Link] Gabr 078

 1C.7 The benefits and risks of treatment:
Treatment

1. Life style 3. Surgery

2. Drugs
[Link] smoking [Link] angiogram
2. Reduce food intake and exercise 2. Coronary bypass
regularly. 3. Heart transplant
3. Reduce alcohol and caffeine intake.
4. Reduce salt in take.
5. More vitamin C
6. Decrease saturated fats intake and

r
increase unsaturated fat intake.

ab
7. Avoid stress.
8. Reduce cholesterol intake.
9. Increase HDL; LDL ratio. lg
iha
1. Controlling Controlling blood Drugs preventing
blood pressure cholesterol level: clotting
Antihypertensives Anti cholesterol
.N

A. Diuretics A. Statins A. Anticoagulants

Dr

B. Beta blockers B. Plant stanols and B. Platelets

sterols inhibitors

C. ACE inhibitors

[Link] Gabr 079

 1. Controlling blood pressure
Antihypertensives

A. Diuretics B. Beta blockers:

Mode of action Mode of action

Eliminates excess salts and fluids in urine Block receptors on surface of heart
by decreasing water reabsorption in the muscle
kidney So heart muscle don’t respond to
This will decrease volume of blood. hormones such as adrenaline.
Thus decreasing blood pressure. So heart rate slows down /slower
So less chance of damage of walls of And contraction becomes less strong
artery. Decreasing blood pressure.
Side effects:

r
Hypotension , kidney problems, dizziness

ab
and headache.

C. Sympathetic nerve lg
inhibitors

Mode of action
iha
Where the sympathetic nerves stimulate arteries to constrict .....increasing blood
pressure
So sympathetic nerve inhibitors , inhibit/ prevent the nerves signaling to arteries
So they stay dilated
.N

So blood pressure lowered.

Examples:
Dr

ACE inhibitors which inhibit the activation of Angiotensin so no no stimulation of

aryeries to constrict.
Mode of action :
When blood pressure falls. Kidney release renin. Cause cutting of
Angiotensinogen into angiotensin I ( inactive). Angiotensin II (active)
Stimulating constriction of artery.

Benefit. Risk.
Prevent constriction of arteries Blood pressure might go too
So stay dilated low( hypotension)
So decrease blood pressure Side effects as nausea , swollen
So decrease risk of atherosclerosis thus ankle, constipation, dizziness.
decreasing risk pf CVD
[Link] Gabr 080
 Controlling blood cholesterol level:
Anti cholesterol

A. Statins B. Plant stanols and

sterols
Mode of action
Mode of action
Inhibit synthesis of cholesterol
Naturally occurring in plants
Thus reducing blood cholesterol level ( decrease LDL).
With similar structure to
By blocking enzyme in liver responsible for making
cholesterol
cholesterol.
So reduce amount of cholesterol
So increase in HDL/ decrease in LDL/ increase in HDL;
absorbed from small intestine
LDL ratio.
into your blood
Potential risk:
So reducing LDL level.

r
Muscle inflammation

ab
Liver damage
Kidney damage
Muscle pain lg
Nausea/ insomnia/ headache
Constipation/ diarrhea
People taking statins will no longer try to lower blood
iha
cholesterol level by following healthy diet
Drugs preventing clotting
.N

A. Anticoagulants B. Platelets
(warfarin) inhibitors
Dr

Mode of action Mode of action

Prevent formation of clot Prevent platelet coagulation.
By interfering with manufacture of prothrombin by
inhibiting some enzymes in the coagulation cascade.
So no thrombin to bind with fibrinogen
So fibrin is not formed
Reducing effectiveness of platelets
So reducing chance of blockage of artery
Maintain oxygen supply to tissue
So less risk to heart attack/ stroke
risk:
Internal bleeding, nausea, dizziness, stomach ulcer,
headache, irritate stomach lining
[Link] Gabr 081
Exam hint
Placebo and their values
1. a substance similar to the drug in every aspect (shape, smell, taste) however, it has no
therapeutic effect (no active ingredient).
2. Its value: they are given to the control group to eliminate psychological factors
Allowing valid results.

Mortality and morbidity:

1. Mortality ; subjection to death
2. Morbidity: subjection to disease.
• Both are calculated per 100,000 to allow valid comparison between different sized
population.

Suggest why different countries have different mortality and morbidity

rates:

r
1. Better health care and awareness
2. New medications.

ab
3. obedience and stick to safety regulations.
4. Less frequent/ sever risk factors.
lg
How can a correlation be further supported?
A. Metadata analysis
B. Statistical tests ( example spearman rank test)
iha
C. Increase in disease incidence is preceded by increase in risk factor.

Why 3 clinical measurements needed for diagnosis?

Three criteria increase diagnostic accuracy
.N
Dr

[Link] Gabr 082

Core practical 2
1C.5 Testing for vitamin C
Objectives
1. To be able to calculate the vitamin C concentration of fruit juices using the
titration method
2. To solve problems set in practical contexts
3. To process and analyse data using appropriate mathematical skills (mean,
median mode, use arithmetic mean)

Safety:
1. Wear eye protection.
2. Avoid skin contact with the DCPIP and test tube solutions.
3. Do not taste the fruit juice.

r
Procedure:

ab
Steps:
1. Extraction of fruit juice by crushing and adding distilled
water to extract vitamin c.
lg
2. Controlled variables: same conc. Of DCPIP, same same
mass of fruit, same volume of extract, same storage DCPIP
iha
conditions.
3. Use DCPIP
4. Titration by adding DCPIP to vitamin c sample drop by
.N

drop where colour change from blue to colourless .

5. Count number of drops /measure the volume of DCPIP Vitamin C
Dr

added for the colorless to change to blue. sample

6. Standardization, repeat using 1% solution of vitamin C so

that the volume of DCPIP decolorised by fruit juice is
compared with volume decolorised by standard vitamin C Keep adding DCPIP
till blue colour of DCPIP
solution. remain.
As DCPIP will be
7. Repeat and take average.
reduced( gain electrons)
Remember : role of vitamin C on CVD Vitamin C will be
oxidised (lose electrons)
Affect the endothelium lining of blood vessels
So low vitamin C. Damage endothelium lining of artery
causing atherosclerosis
As vitamin C act as an antioxidant that reduce plaque and
atheroma formation.
[Link] Gabr 083
 1. What were the independent and dependent variables in this
investigation?
Important
The independent variable was the type of fruit juice used. The dependent questions

variable Was the volume of juice added to decolorise the DCPIP.

2. Why was each titration completed three times to calculate a mean?

Calculating a mean value makes it easier to spot anomalies. Repeated readings also reduce the effect
of errors.

3. Suggest one reason why syringes were used in this investigation rather than burettesOne of:
• Using very small volumes of solution requires a more precise piece of apparatus than a burette.
• Syringes are easier to control, allowing smaller volumes to be added.
• Ease of use
• Relatively low cost

4. Which of the fruit juices tested contained the highest concentration of vitamin C?
Your own answer according to your results.

r
ab
5. The reagent DCPIP tests for the presence of ascorbic acid (vitamin C). It is
blue when oxidized and colorless when reduced. During the reaction between
Important
questions DCPIP and
ascorbic acid, DCPIP becomes reduced and ascorbic acid becomes oxidised.
lg
(a) Describe the direction of movement of electrons during the reaction between
DCPIP and vitamin C. (2marks)
iha
DCPIP gains electrons (1) from the ascorbic acid. (1).

(b) Explain why vitamin C is described as an antioxidant(2 marks)

Vitamin C / ascorbic acid readily loses electrons / becomes oxidised (1) and this prevents other
.N

cellular components / chemicals from becoming oxidised. (1) .

Dr

(c) . Suggest why, when adding ascorbic acid to DCPIP, the tube should be shake gently and not
vigorously with the addition of each drop of DCPIP.(3 marks)
DCPIP becomes colourless when reduced and that is the end point. (1) Shaking
too vigorously would introduce oxygen to the DCPIP / reoxidise it (1) and the Blue colour would return /
would make it difficult to find the true end point. (1)

6. A student tested (assayed), by titration with DCPIP, a solution of blackcurrant juice. The juice
was first decolorised by adding a piece of activated charcoal. The data
obtained are shown in the tables.

[Link] Gabr 084

(a) Explain why the blackcurrant juice was first decolorised (2 marks)
This juice was decolorised to make it easy to spot the endpoint, i.e. the point whenDCPIP just
becomes decolorised. (1) This point would be difficult to judge in
coloured juices. (1)

(b) Calculate the mean values missing from both tables. (2marks)
Note: mean values can be to 1 d.p. more than the raw data values.

(c) . Calculate the ascorbic acid concentration, in mg/100 ml, of the blackcurrant juice. Show your
working. (4 marks)
In 1 ml 1% DCPIP there are 10 mg DCPIP per ml
In 1 ml 1% ascorbic acid solution there are 10 mg ascorbic acid per ml
1 ml (10 mg) DCPIP is decolorised by (1.1 × 10) mg ascorbic acid = 11.0 mg
ascorbic acid (1)
Therefore there are 11.0 mg ascorbic acid in 23.17 ml blackcurrant juice (1)
So in 1 ml blackcurrant juice there are 1/23.17 × 11.0 = 0.47 mg ascorbic acid (1) So in 100 ml
blackcurrant juice there are 0.47 × 100 = 47.0 mg ascorbic acid /

r
vitamin C (1)
Correct answer with no working gets 4 marks

ab
7. Vitamin C is water soluble and cannot be stored within the body. Many mammals,
lg
including dogs, can make vitamin C in certain cells. Humans cannot synthesise vitamin C and
have to obtain it from their diet. However, if they consume more than needed,
the excess is filtered from the blood in the kidneys and passes out in the urine.
iha
Imagine that you are a scientist in a physiology research lab. Outline the design of an
investigation to determine whether taking vitamin C supplements benefits people.
(8 marks)
.N

Any eight from:

Large sample of volunteers (1)
Dr

Matched age / gender / mass / lifestyle / diet (1)

Questionnaire about diet (1)
Collect a day’s urine and test for vitamin C to ascertain base levels – are they already
taking plenty of vitamin C or not enough? (1)
Divide into groups – one group given no vitamin C supplement, one group given small
supplement, one group given larger supplement (1)
Could make it blind / double blind and give first group a placebo (1)
Make sure they stick to normal diet / stay in lab so scientists can control their diet (1)
Collect urine again (one day’s worth) and test for vitamin C content – is the extra being passed
out? (1)
Other valid point (1)

[Link] Gabr 085

Topic 2A.1,2,3,4

Introduction to
cell membrane
and transport.

r
Learning outcomes
ab
lg
Description of the structure of
iha
cell membrane.
.N

Explanation of how
Dr

substances enter and leave

the cells.

The need for gas exchange

surfaces

Understand how the structure of the

mammalian lung is adapted for rapid
gas exchange.

[Link] Gabr 086

 First: structure of cell membrane:
The phospholipids molecules arrange themselves tail to tail to form a phospholipid bilayer that
forms the basic structure of the cell membrane .

Structure of membrane:
• It is extremely thin, about 7nm thick /wide.
• It is a phospholipid bilayer (2 monolayers form
bilayer).
Cytoplasm
• Phospholipids are fluid.
• With the hydrophilic(polar) heads of the two
phospholipid layers facing outwards , which are

r
Tissue fluid
attracted to water by H-bonding.

ab
• While the hydrophobic core ( fatty acid tails)of the
membrane, which is repelled away from water.
lg • All cells membranes , whether they surround the
cell or the organelles, are basically the same.
• With channel and carrier proteins scattered in
iha
membrane.
Fluid mosaic model: • Having also glycolipid , cholesterol, glycoprotein.
.N

a suggestion(hypothesis) for the structure of cell membrane is described as Fluid mosaic model.

• Fluid: where the phospholipid and the protein molecules move about/ diffuse within their
Dr

monolayer, giving the membrane a flexible structure that is constantly changing in shape.
• Mosaic: where there are different protein molecules which are scattered in the cell surface
membrane( phospholipid bilayer), such as pores, channels, and carrier systems in a lipid bilayer.

Fluid mosaic
model

[Link] Gabr 087

 • Explain how the properties of phospholipid contribute to fluid mosiac model of cell membrane?
1. It forms a bilayer with polar head and non polar tail .
2. Proteins are located between the phospholipid. This is due to the interaction between R groups of
proteins and phospholipids.
3. Phospholipids are free to move which makes the membrane fluid.

• What affect the fluidity of membrane are:

1. The percentage of unsaturated fats ( number of C=C), where as it increases the fluidity increase,
this is because the unsaturated fatty acid tails are bent ( i.e with kinks)so fit together more loosely.
2. The tail length, where the longer the tail the less fluid the membrane is.
3. Temperature, where as temperature decrease, the membrane becomes less fluid, and vice versa
4. Cholesterol (-ve correlation) as cholesterol holds fatty acid tails by hydrophobic interaction.

r
• What are the different types of proteins present in membrane:

ab
Intrinsic protein(integral Extrinsic protein(peripheral
proteins) proteins)

1. They are embedded in the membrane, being exposed to

lg 1. They are not embedded in the
aqueous environment on both sides of the membrane. membrane, found on the inner or
2. They are transmembrane proteins (transport molecules outer surface of the membrane.
across membrane) with hydrophilic heads and hydrophobic
iha
2. Many are bound to intrinsic
middles that is exposed to the phospholipid of membrane. proteins.
3. transmembrane proteins (globular proteins) interact with 3. May act to give mechanical
phospholipid to stay in the membrane. How? support to the membrane or may
.N

• The polypeptides (transport proteins) interact with have other functions such as,
phospholipids where: enzymes that have a role in cell
- Region with Hydrophilic/ polar R groups of amino acids signaling.
Dr

interact with phosphate/ hydrophilic head of phospholipid.

- Region with Hydrophobic non polar R groups of amino acids
interact with fatty acid/ hydrophobic tail of phospholipid.
4. Example: (transport protein such as carrier protein or
channel proteins)

Transport protein.

[Link] Gabr 088

 Second: Roles of the components of cell membranes:
• The membrane contain several types of molecules including
• Phospholipid, cholesterol and glycolipid ( branching
A. three types of lipids carbohydrate attached to a lipid).

• Protein( channel / carrier) and glycoprotein (branching

[Link] types of proteins carbohydrate attached to a protein).

r
ab
lg Phosphate head carries a negative
1. Phospholipids: charge and is soluble in water.
iha
Fatty acid chain neutral and
insoluble in water.
.N

Explain how phospholipid molecules form bilayer?

• Phospholipid molecule forms part of bilayer.
Dr

• Fatty acid( hydrophobic) tails may be saturated or unsaturated.

• Each phospholipid molecule has the following function:
1. The hydrophilic (phosphate) head which are polar (facing the water media in the cytoplasm
and the tissue fluid) form H-bonds with water ,so stabilise the membrane.
2. The hydrophobic tail (fatty acid chain)which are non polar (pointing inwards )
- repelled away from water so the arrangement of phospholipid tails to tails held together by
hydrophobic interaction, forming a hydrophobic barrier to most hydrophilic /polar
substances or ions, as glucose, amino acids and proteins, but permeable to lipid soluble
molecules such as alcohol and glycerol, and non polar molecules such as oxygen and
carbon dioxide (also so small so can pass freely in and out of membrane)..
- Also the unsaturated fatty acids contribute to fluidity where as percentage of unsaturated
fatty acids(C=C) increases, the fluidity increase.
3. The two monolayers form a bilayer.

[Link] Gabr 089

 2. Cholesterol:

• Small molecules, with hydrophilic heads and hydrophobic

tails, so, they fit between phospholipid molecules with their
heads at the membrane surface.
• Cell surface membrane in animals contains almost as much
cholesterol as phospholipid.
• While plant cell membranes contain less cholesterol, and
absent from prokaryotes.
• Function:
1. Stabilise membrane and make it stronger as cholesterol is a more rigid molecule than
many of the phospholipids, as without it , membranes quickly break and cells burst
open.

r
2. Cholesterol affects fluidity:(-ve correlation) cholesterol combine with fatty acid tails.

ab
Holding fatty acids chain together by hydrophobic interaction. Thus reducing
movement of fatty acid tails/phospholipid.
3. Prevent passage of polar molecules or ions through membrane due to the presence of
lg
hydrophobic region of cholesterol( i.e contributes to impermeability to ions)

3. Transport Proteins
iha
• They are glycoproteins Including channel/ pores and carrier proteins.
• Function:
.N

1. Provide permeability to ions , water, polar molecules through membrane.

2. Each transport protein is specific for particular kind of ion or molecule to control the type of
Dr

substances that can enter or leave the cell.

A. Channel proteins

1. They are water filled pores and have fixed shape.

2. Function:
Channels allow ion, water and other polar molecules to pass through
membrane by facilitated diffusion. Why?
- Ions , polar molecules are hydrophilic.
- Unable to pass through hydrophobic tail of phospholipid bilayer.
- Where channel proteins are lined with amino acids with hydrophilic
(polar) R groups ,... so they are hydrophilic channels

[Link] Gabr 090

 Types pf channel proteins

A. Not gated (always open) A. gated (open and close)

• Stays open all the time.

• These proteins allow ions & water to flow through
the cell membrane, which is normally hydrophobic
and would resist the passage of these molecules. A gated channel protein remains
closed, until it receives a special

r
• A non-gated channel protein is needed whenever
chemical or electrical signal.

ab
the balance of water and ions must be assisted by
the constant passage of water and ions into or
out of the cell.

B. Carrier proteins
lg
iha
1. Specific proteins that bind to specific molecules.
2. They can flip between 2 shapes, as a result the binding site is
alternately open to one side of the membrane, then the other.
3. Function:
.N

allow ions and polar molecules to pass through membrane by

facilitated diffusion or active transport.
Dr

Notice only for understanding:

A carrier is not open simultaneously to both the extracellular and intracellular environments. Either its
inner gate is open, or outer gate is open. In contrast, a channel can be open to both environments at the
same time, allowing the molecules to diffuse without interruption. Carriers have binding sites, but pores
and channels do not.

[Link] Gabr 091

 4. Glycoproteins
1. Protein molecule with short carbohydrate chain attached to it.
Function:
This carbohydrate chain can form hydrogen bond with water molecules outside the membrane so help
stabilise the membrane structure.
Also this carbohydrate chain help glycoprotein to act as receptor molecules which bind with particular
substance at cell surface membrane.
There are three major groups of receptors:
1. Signaling receptors :receptors that recognise messenger molecules as hormones and
neurotransmitters., ex; glucagon receptors in liver cells.
2. Receptors involved in endocytosis.
3. Receptors involved in binding cells to other cells( cell adhesion) in tissues and organs of animals.
Act as cell markers or antigen allowing cell- cell recognition.

r
Some proteins are enzymes,( especially peripheral proteins) as that in walls of small intestine that

ab
hydrolyse disaccharides to monosaccharides before their absorption.
They Function as transport proteins
lg
iha
So over all function of glycoprotein:
1. Receptors( cell signaling)
2. Antigen( cell recognition)
3. Form H-bond with water to stabilse membrane .
4. Enzymes.
.N

5. Transport proteins in cell surface membrane.

Dr

5. Glycolipids: Same function as

glycoprotein

1. Lipid molecules on the outer surfaces of cell surface membrane with short carbohydrate chain
attached to them.
Function:
form hydrogen bond with water molecules so help stabilise the membrane.
Also this carbohydrate chain help glycoprotein to act as receptor molecules.
1. Signaling receptors
2. cell adhesion.
Act as cell markers or antigen allowing cell- cell recognition.
[Link] Gabr 092
 Third: building a model of the membrane :
A very good example of how technical developments over time enable better scientific
understanding

1. 1. Lipid soluble substances entered more more easily than any others, so
concluded that a large party of the membrane structure must be lipid.
2.
3. 2. The idea of fluidity came from observing the behaviour of the cell surface
membrane when cells join, together with the way in which membranes seal
themselves if they are punctured within a fine needle.
4.
3. Irving langmuir, developed a piece of equipment for collecting lipid monolayers called
Langmuir-Blodgett trough.

4. Then two scientists , Evert Gorter and François Grendle, decided to measure the total
size of the monolayer film formed by lipids extracted from human RBCs.

r
+ estimating total surface area of a red blood cell Found that their

ab
measured area of monolayer was about twice the estimated surface area of cell.
Conclusion cell membrane is a lipid bilayer .
+ Yet results were wrong in two ways
lg
Miscalculating the surface area as
iha
Did’t extract all the they thought that red blood cells
lipid were flat rather than biconcave

Yet conclusion was correct, by

.N

coincidence as the two errors

canceled each other
Dr

5. In 1935, further model of membrane by Hugh Davson and James Danielle.

By staining the membrane So it was seen as by electron microscope as three
layered structure ( 2 distinct line with a gap in middle)
Then upon treatment with acetone ( propane) to
extract lipid , the two lines remained intact suggesting
that they are protein layers.

7. More recent techniques using X-ray diffraction and new electron microscopy methods
gave more details of layers, pores( nuclear pores), carrier molecules.

This is a good example of how technical development over time

enable better scientific understanding.

[Link] Gabr 093

Notice

Over all function of cell membrane:

[Link] between cytoplasm and external environment.
[Link] and select substances that enter or leave the cell.
3. Have receptors for Cell signaling substances such as hormones and neurotransmitters.
4. Allow cell recognition by acting as cell surface antigen thus avoiding cell destruction.
5. Glycoprotein and glycolipid form hydrogen bonds with water for stability.
6. Changing shape of cell( flexibility) e.g in phagocytosis.
7. Location for enzymes.
8. Many chemical processes take place on membrane surfaces, ex; some of respiration
reactions take place on inner mitochondrial membrane.

r
Describe effect of high temperature on cell membrane:

ab
1. It will damage the membrane , due to denature of proteins where:
loss of tertiary structure.
Loss of globular shape. lg
Breakage of ionic, hydrogen , hydrophobic interactions.
And so:
- loss of function of membrane proteins , being unable to receive cell signals, unable to
iha
transport polar molecules .
- Membrane become leaky with loss of its partially permeable nature.
- So membrane can’t regulate the entry and exit of substances.
- Also this will disrupt the interaction between protein and phospholipid bilayer.
.N

Value of phospholipid:
Dr

1. Foundation of cell membrane.

2. Selectively permeable allowing diffusion of small polar molecules (water), non polar lipid
soluble molecules, and gases.
3. Responsible for fluidity.

[Link] Gabr 094

 Fourth: How substances enter and leave the cell:

There are five basic mechanisms by which exchange of substance occur between the cell and its
environment.
1. Simple Diffusion
2. Facilitated diffusion
3. Osmosis
} Passive transport

4. Active transport
5. Bulk transport( endo and exocytosis) } Active transport

1. Simple diffusion

A. Passive transport
} 2. Osmosis

r
ab
3. Facilitated diffusion

1. Diffusion:

Definition:
lg
Net movement of molecules or ions from a region of higher concentration to a region of lower
concentration down gradient, as a result of the random movement of particles.
iha
It is a passive process that depends on the kinetic energy of molecules or ions .
As a result of diffusion, molecules or ions tend to reach an equilibrium situation.

[Link] Diffusion:
.N

The net movement of (liquid or gas) non polar molecules as carbon dioxide , oxygen, and non
polar lipid soluble molecules as alcohol , glycerol and steroid hormones and urea as well from
Dr

region of higher concentration to a region of lower concentration down their concentration

gradient through phospholipid bilayer (hydrophobic core).
It requires no metabolic energy from ATP, but it depends on the kinetic energy of
molecules.

Remember that
increase in fluidity
Increase rate of
diffusion.

[Link] Gabr 095

 Factors affecting rate of diffusion:
1. The steepness of the concentration gradient.
The increase in the concentration gradient increases rate of diffusion.
2. Temperature.
The increase in the temperature, increase the kinetic energy of molecules so faster binding to their
specific protein and cell membrane becomes more fluid and more permeable, thus increasing rate
of diffusion.
3. size of molecules and polarity
larger molecules requires more energy to get them moving so larger molecules decreases rate of
diffusion.
[Link] surface area
The increase in the surface area, increase number of protein transporters so increases rate of
diffusion.
The larger the cell the smaller its surface area in relation to its volume.

r
ab
Surface area(length x width x
number of sides)

Volume (length x width x height)

Surface area : volume ratio

lg
2. Facilitated diffusion :
iha
Passive process that doesn’t need ATP.
It is the movement of polar molecules , ions or larger molecules (example glucose and amino acids) ,
through transporter proteins( channel or carrier) in cell membrane due to the hydrophilic amino acids
.N

lining channels.
Channel proteins: Each channel protein allows one Polar
particular type of molecule to pass through, depending on molecules or
Dr

ions.
molecule shape and charge.
Gated channels are protein channels that open only if
specific molecule is present , or if there is an electrical
charge across the membrane, such as during passage of
nerve impulses along neurones.
Transport proteins with specific
Carrier protein: where polar molecules or ions have a shape.

complementary shape to the binding site on protein carriers

in the cell membrane .
They fit and bind with these protein transporters , changing the shape of the protein allowing the specific
molecule or ion to diffuse , where the movement through membrane takes place because the carrier
changes shape once it is carrying something. Example : RBCs have a carrier to help glucose move into
the cell rapidly.
from region of their higher concentration to a region of their lower concentration down their
concentration gradient).
[Link] Gabr 096
 3. Osmosis:
Passive process that doesn’t need energy from ATP.
It is the net movement of water molecules , from the region of higher water potential ( less negative)
to region of lower water potential ( more negative) down water potential gradient through a partially
permeable membrane.
Due to their random motion (diffusion).
Water molecules are dipolar yet some can pass through phospholipid bilayer(hydrophobic core) by
osmosis as water molecules are very small and have a high kinetic energy, and most of the water
passes through channel proteins called aquaporins.

r
The solute molecules are too large to pass through the pores in the membrane ,but water molecules are

ab
small enough.
This is due to the fact that cell membrane is partially permeable means solutes (dissolved substances ) can
be accumulated either side of the membrane and this result in the movement of water by osmosis across
lg the membrane .
Net movement has been from A to B .
The osmotic concentration: is a measure of the concentration of solutes (only dissolved
iha
substances) in a solution that have an osmotic effect.
This is especially important in living things because many of the large molecules found in the cytoplasm
of a cell don’t affect the movement of water into or out of the cell and so we ignore them when
calculating osmotic concentration.
.N

Osmotic pressure: It is the measure of the tendency of a solution to take in pure solvent by osmosis.
Dr

Types of solutions

Hypertonic
Hypotonic solution Isotonic solution
solution

•Dilute solution •Where the osmotic

•Concentrated solution
• Where the osmotic concentration of solutes in
• Where the osmotic
concentration of solutes in the solution is the same as
concentration of solutes in
the solution is the lower than that in the cytoplasm of
the solution is the higher
that in the cytoplasm of cells.
than that in the cytoplasm of
cells. • So its a solution with same cells.
• So its a solution with lower osmotic pressure relative to
• So its a solution with higher
osmotic pressure relative to another solution.
osmotic pressure relative to
another solution.
another solution.

[Link] Gabr 097

 Tendency of water to move out of a solution depends on:
1. How much water the solution contains in relation to solutes (concentration of solution/ osmotic
concentration)
2. How much pressure is being applied (pressure on a liquid increases water potential) this is called
pressure potential.
Ψ= ψs+ ψp
Pressure potential
Water potential
Inward pressure exerted by cell wall that
Solute limits further uptake of water
potential

Distilled water has zero water potential ( ψ=0, ψρ=0, ψs=0)

In concentrated solution : ψ=ψs+ ψp where ψp= 0

-4= -4+0. So, ψ=ψs
In diluted solution : ψ=ψs+ ψp

r
0= -4+4. So, ψs=ψp

ab
lg
iha
.N
Dr

• The solution in plant • The cell becomes

cell is considered turgid so water
concentrated potential becomes
( hypertonic with lower zero and no net
water potential) movement of water.
• So ψ=ψs and ψp=0 • So ψs=ψp and ψ=0

[Link] Gabr 098

 Another
example for
better
understanding

Solution in right side

Solution in left side represent hypertonic
concentrated solution : As we-reach to
represent distilled water :
ψ=ψs+ ψp where ψp= 0 equilibrium
So ψ=0
-1= -1+0. So, ψ=ψs ψ=ψs+ ψp
0= -1+1. So, ψs=ψp

r
ab
B
lg
Cell represent As we-reach to
Solution in beaker hypertonic equilibrium
represent distilled
iha
concentrated solution : ψ=ψs+ ψp
water : ψ=ψs+ ψp where ψp= 0 0= -1+1. So, ψs=ψp
So ψ=0 -1= -1+0. So, ψ=ψs
.N
Dr

Effect of osmosis on animal cell:

A. In dilute solution(hypotonic);
• Osmosis occurs where water moves from area of high water
potential(outside the cell) to area of lower water potential ( inside
the cell) , down water potential gradient through a partially
permeable membrane.
• Where the osmotic concentration of solutes in the solution is the
lower than that in the cytoplasm of cells..
• Net movement of water into cell.
• So cell swells and may burst.
[Link] Gabr 099
B. In isotonic solution:
equal where same water potential inside and outside cells.
The osmotic concentration of the solutes is the same in solution and in cells.
No net movement of water( no water potential gradient).
So no change in the size of cell.
C. In concentrated solution(hypertonic);
Lower water potential outside, as the osmotic concentration of solutes in solution is higher than in
cytoplasm of cell. the cell so water moves out by osmosis, i.e net movement is out of cell.
So cells shrink( become smaller).

Effect of osmosis on plant cell: Osmotic changes in plant cell

A. In dilute solution:
• Cell become fully turgid , were the cytoplasm presses
out against the cell wall generating hydrostatic

r
pressure (which is pressure exerted by fluid in

ab
equilibrium), so no more water enters.
• The inward pressure of cell wall on cytoplasm increases
until it cancels out the tendency for water molecules to
lg
move in. How plasmolysis occur
• When the osmotic force moving water into plant cell is balanced
with pressure potential forcing it out, the plant cell is
iha
rigid , in a state called turgor,
• It doesn’t burst due to presence of cell wall which is so
inelastic.
• For plants, water potential is combination of solute
.N

potential and pressure potential.

• Ψ= Ψs+ Ψp.
Dr

B. In isotonic solution:
• no change in the size of cell.
C. In concentrated solution:
• water leave the cell by osmosis , so protoplast gradually
shrink until its exerting no pressure at all on cell wall.
• So pressure potential is zero, Ψ= Ψs only as Ψp=0
• So we measure incipient plasmolysis using serial
dilutions, looking for the point at which 50% of the cells
are plasmolysed and 50% are not. This the Plasmolysis:
concentration that is equivalent to solute potential in cell sap, so Shrunken vacuole, cytoplasm and
cell membrane pulled away from cell
Ψ= Ψs only as Ψp=0 wall, cell membrane seen and a
--

• so Protoplast continues to shrink , it begins to pull away from space between cell wall and the cell
membrane.
cell wall
• cells become plasmolysed where cell membrane become
detached from cell wall.
[Link] Gabr 100
 Turgor: the state of plant cell when when solute
potential causing water to be moved into the cell
by osmosis, is balanced by the force of cell wall
pressing on protoplasm.
Incipient plasmolysis; the point at which so
much water has moved put of the cell by
osmosis that turgor is lost and the cell
membrane begins to pull away from cell wall
as the protoplasm shrinks.

Summary for passive transport routes through a cell surface membrane

r
ab
lg
iha
Example: oxygen Aquaporins are type of channel
and carbon dioxide proteins that allow water to
enter or leave the cell thus
.N

avoiding the hydrophobic center

Dr

[Link] Gabr 101

 B. Active processes:

1.
T Active transport:

Active process that needs energy from hydrolysis of ATP, where energy is needed for carrier protein to
change its shape.
It is the movement of polar molecules or ions , through carrier proteins in cell membrane due to the
hydrophilic amino acids lining channels.
Where these polar molecules or ions have a complementary shape to the binding site on protein
carriers in the cell membrane .
They fit and bind with these carriers , changing the shape ( conformational change) of the protein using
ATP allowing the specific molecule or ion to pass against their concentration gradient).
An active transport system moves substances in only the direction required by the cell.
In some cases the substance move out again through open channels down the concentration gradient

r
that has just been overcome, but active transport can move substance faster than they can move out
by diffusion.

ab
Then protein carriers
lg return passively to
original shape to
allow more ions/
polar molecules to
enter.
iha
.N

Examples of carrier proteins:

Dr

A. Pass one kind of C. Pass one kind in

molecule B. Pass two kind of and one out
molecule together. example sodium-
potassium (Na -K ) pump:
example glucose-sodium
•
co transporter

Co transporter

[Link] Gabr 102

 Notice
Evidence of active Factors affecting active
transport : transport:
[Link] in living cells only. 1. Oxygen and glucose concentration.
2. High number of mitochondria. 2. Number of protein carriers.
3. respiratory poisons stop it. 3. Number of mitochondria.
4. Presence of respiratory poisons.

ATPase an enzyme that catalyses the hydrolysis of ATP , releasing energy

to move carrier systems and drive metabolic reactions.
Cyanide: a metabolic poison that stops mitochondria working .

r
ab
Active transport Facilitated diffusion
Requires energy from ATPlg Doesn't require energy
Substances move against the concentration Substances move down the concentration
gradient gradient
Uses only carrier proteins Uses both carrier and channel proteins
iha
Can involve cotransport Doesn’t involve cotransport

4. Bulk transport:
.N

It involves transport of large molecules such as proteins or

polysaccharides, parts of cells or even whole cells where this
requires energy do it is a form of active transport:
Dr

Endocytosis Exocytosis
Involves engulfing of material by cell surface membrane to Process by which materials are removed from
form a small sac or endocytotic vacuole, using energy from cells,
ATP.

[Link] Gabr 103

 Endocytosis Exocytosis

It takes three forms: Example :

1. Phagocytosis: cell eating/bulk transport of solids [Link] secretion of digestive enzymes from cells of
the pancreas, mucus secretions.

Steps :
1. Membrane engulfs bacteria.
2. Membrane fusion forming phagosome/vesicle/ vacuole.

r
3. Lysosome containing hydrolytic enzymes fuse with phagosome.
4. Bacteria digested by hydrolytic enzymes.

ab
2. Pinocytosis; cell drinking;in Which bulk uptake of liquids , [Link] plant cells , they use exocytosis to get their
where the vacuoles(vesicles) formed are often extremely cell wall building material to the outside of the cell
small. surface membrane.
Pinocytosis is very common as cell take in the extracellular
lg
fluid as a source of minerals and nutrients. Steps:
The vesicle/ vacuole containing molecules ( like
waste or digested material) move towards the cell
surface membrane.
iha
Then vesicle fuses with membrane ( don’t write
bind or attach).
Facilitated by the fluid nature of phospholipid.
Contents secreted/ released/ excreted outside
the cell.
Its an active process requiring energy by using
.N

ATP

Mass of tiny vesicles along these cell membranes show

pinocytosis
Dr

Process Occurs against a Needs ATP to supply May use carrier protein
concentration gradient energy molecules

Diffusion No No No
Facilitated No No Yes
diffusion
Osmosis No No No

Active Yes Yes Yes

transport
[Link] Gabr 104
Core practical 3
2A.1 investigating membrane properties:

Objectives:
To know how the effect of temperature and alcohol on membranes can be determined.
To be able to recognise quantitative variables that should be controlled in an investigation .

Safety:
1. Wear eye protection.
2. Water baths at temperatures above 50 °C may scald. Take care when removing lids to
allow steam to escape away from the face or body. If you are splashed by hot water, or
scalded by steam, cool under cold running water immediately.
3. Take care with sharp items such as the cork borer and knife. Always cut or push
downwards onto the tile.

r
4. Ethanol is highly flammable so keep away from naked flames and keep the stoppers on

ab
bottles.
5. Do not handle electric plugs, sockets or switches with wet hands.

Procedure:
lg
iha
.N
Dr

A. Effect of temperature:
Procedure:
1. Set six water bathes at a range of temperature (0°C, 10 °C, 20°C, 30°C, 40°C, 50°C).
2. Get 5 test tubes with equal volume of distilled water 10 cm3.
3. Allow equilibration (leaving in each water bath for 5 mins) to reach experimental
temperature.
4. Get 5 beet root pieces all cut to same size, and all should be of same age.
5. Rinse then dry to remove pigments from surface due to cutting.
6. Add beetroot pieces to test tubes.
7. Then use the colorimeter to measure degree of light absorbance.

[Link] Gabr 105

A. Effect of temperature:
Results:
A. At low temperature:
Tonoplast / cell membrane of vacuole remain in tact.
Betalain /pigment molecules are too large to pass through membrane easily.
So high light transmission.

B. At higher temperature:
Kinetic energy of molecules increase
Increasing movement and diffusion of pigment molecules

Phospholipid of membrane becomes more fluid, bond/interaction between fatty acid tails
begin to separate .
Increasing permeability of the membrane .
So pigment molecules can pass more freely through the cell membrane to the liquid outside.

r
So less light can pass through liquid.

ab
C. At very high temperature:
The protein molecules in the membrane become completely denatured (losing their tertiary
structure by disrupting the bonds that hold their tertiary structure in place), (also
lg
phospholipid may melt) and gaps are formed in the membrane through which the pigment
can flood out .
The change in transmission levels out as the concentration of pigments is the same inside
iha
and outside the cells(equilibrium).

rate of diffusion percentage transmission of light

.N

C
18 16 A
Dr

13.5 12 B
B
9 8
C

4.5 A 4

0 0
10 20 30 40 50 60 70 10 20 30 40 50 60 70
Temperature /°C Temperature /°C

[Link] Gabr 106

 B. Effect of alcohol:
Procedure:
1. Take five test tubes and add 10 cm3 of ethanol to each one. Use a different
concentration of ethanol in each tube (distilled water can be used for a 0%
concentration).
2. Use a cork borer to cut five beetroot cylinders. Use a knife, ruler and white
tile to trim them all to the same length (1 cm is sufficient).
Wash the cylinders thoroughly with water until the water runs clear, then gently pat dry
with a paper towel, to remove pigments from surface due to cutting.
3. Add one beetroot cylinder to each of the five tubes and leave for 15 minutes.
4. Shake the tubes once. Then, working quickly and carefully, use forceps to remove the
cylinder from each tube.
Discard the cylinders but keep the supernatant liquid (the clear liquid above the solid). It

r
may be easier to decant this liquid into clean test tubes.

ab
5. Set the colorimeter to a blue/green filter and percentage transmission. Zero the
colorimeter using a blank cuvette filled with distilled water.
6. Transfer liquid from each test tube in turn into a colorimeter cuvette, place in
lg
the colorimeter and take the percentage transmission reading. Record your results in a
suitable table.
iha
A. Effect of alcohol:
Results:
.N

The change in alcohol concentration affects the integrity of the phospholipid bilayer.
Because
Dr

1. phospholipids are soluble in alcohol, where alcohol dissolves the fatty acids in cell
membrane,
2. so the membrane loses the ability to orientate towards and away from water
( altering the hydrophobic interaction)
3. The lose of hydrophobic and hydrophilic interaction disrupt the phospholipid bilayer,
4. As well as at very high concentration ,proteins in cell membrane denature.
5. resulting in holes forming in the membrane which allow the pigment out of the
cells.
6. The increase in pigment outside the cells reduces the ability of light to penetrate
the solution therefore decreasing transmission.

[Link] Gabr 107

1. List the variables that were controlled during the experiment and state
how they were controlled. This could be done using a table. Important
The variables controlled during the experiment are: questions

- the volume of bathing water or ethanol in each tube (10 cm3)

- the surface area and volume of the beetroot cylinders (dependent on size of
cork borer; 1 or 2 cm in length)
- the equilibration time in the temperature experiment (5 minutes)
- the soaking time for the cylinders (15 minutes)
- the volume of coloured liquid in the cuvettes (e.g. 4 cm3)
- the colorimeter filter / wavelength used (blue / green)
- the part of the beetroot the core was taken from (e.g. the centre)
- the age, variety and storage time of the beetroot (the same beetroot or beetroots from the
same batch may have been used).

2. Suggest why the tubes were placed in the water baths for 5 minutes before the cylinders

r
were added.

ab
The temperature must be equilibrated to ensure the tubes contain water at the correct
temperature before the experiment begins. This allows confidence that the effect of The correct
temperature is being assessed.

experiment began?
lg
3. Why were the beetroot cylinders washed with distilled water and dried before the

• The cylinders are washed and dried to remove excess surface pigment from the cut
• cells at the edge. This excess pigment would distort the transmission readings, giving inaccurate
iha
results.

4. Use the trend line of one of your graphs to describe the effect of temperature or alcohol
concentration on the percentage transmission.
The percentage transmission decreases as the temperature rises. Initially there is little increase, but
.N

at around 40–60 °C the percentage transmission decreases sharply. You should use values from
your own graph. At higher temperatures, the rate of decrease
usually levels out.
Dr

The percentage transmission decreases as the alcohol concentration increases. At low

concentrations of alcohol (0%–10%) there may be little noticeable effect but as the
concentration is increased the decrease in transmission should be proportional until
Leveling off between 60%–80%.

[Link] your results in detail in terms of what is happening to the beetroot membrane.
Answer using the effect of temperature and alcohol parts mentioned before☝ .

[Link] Gabr 108

6. Describe how you would investigate the effect of acetic acid on beetroot
cell membranes. (6)
1. Same equipment and protocol but use different concentration of acetic Important
questions
acid. Award
marks for hypothesis, equipment, procedure, IV and DV, control variables, how
to deal with the data. (6)

7. Explain how (a) high temperatures and (b) ethanol damage cell membranes. Make
reference to the fluid mosaic model in your answer. (4 marks)
Any four from:
1. Cell membranes (surface and around organelles, e.g. vacuole) consist of proteins
2. floating in a phospholipid bilayer. (1)
3. High temperatures can denature the proteins by disrupting the bonds that hold their
tertiary structure in place. (1)
4. High temperatures increase the fluidity of the phospholipid bilayer and may melt the
lipids, causing gaps in the bilayer. (1)

r
5. Ethanol at high enough concentrations may denature some proteins by altering
6. hydrophobic interactions. (1)

ab
7. Alcohol disrupts the phospholipid bilayer and this is more severe in plant cell
8. membranes as they lack cholesterol which helps stabilise the membrane. (1)
lg
8. The cellulose cell walls of plant cells are permeable whereas the cell membranes of plant
cells are partially permeable.
Explain the meaning of the terms
iha
(a) permeable and
(b) partially permeable.
(2 marks)
Permeable: allows any type of / size of molecule to pass through (1)
.N

Partially permeable: only allows some molecules (of certain size or type) to passthrough (1)
Dr

9. By what process does water pass across cell surface membranes?(1 mark)m
Osmosis. (1)

10. Complete the table to compare active transport, facilitated diffusion, exocytosis and
endocytosis.

[Link] Gabr 109

 Some key ideas about graphs

If the particles can move through the lipid bilayer by

A simple diffusion, then there is no limit to the number
that can fit through the membrane. The rate of
diffusion increases linearly as we add more particles
to one side of the membrane.

If the particles can only pass through protein channels

by facilitated diffusion, then the rate of diffusion is
determined by the number of channels as well as the
number of particles.
Once the channels operate at their maximal rate, a
further increase in particle numbers no longer
increases the apparent rate of diffusion. At this limited

r
rate we describe the protein channel as being

ab
saturated.

B
lg At Point A :steep increase in concentration of substance
X
Due to highest concentration gradient so highest rate of
C
iha
diffusion.
B
At point B : less steep increase in concentration of
substance X
Due to lower concentration gradient so lower rate of
.N

diffusion
A
At point C: no change in concentration of substance X
Dr

Equilibrium is reached this no diffusion occurred..

[Link] Gabr 110

 Fifth: the need for gas exchange system

Gas exchange in small organisms

Single celled organisms and very small multicellular organisms have a large surface surface area to volume
ratio.
This means they can get oxygen they need for cellular respiration from air or water they live in through their
outer body surface by diffusion, which would be sufficient to supply their needs.

Gas exchange in large organisms

A Why is circulatory system required in gas exchange?

r
•As diffusion of gases over surface is not enough
So larger organisms need to have a mass transport system /circulatory system

ab
1. Heart:
To generate pressure , ensuring mass flow ( which is the transport of substances from high
pressure to low pressure over a long distance).
lg
• Thus overcoming limitation of diffusion, where they have small surface area to volume ratio,
so Longer distances for nutrients to reach cells,and they have high metabolic rate thus
diffusion alone would be too slow and insufficient .
iha
2. System of branching vessels:
• That carry substances , following a very specific route to required body parts.
• Capillaries which ensure large surface area for gas exchange, thin wall for shorter diffusion
distance.
.N

[Link] transport medium ( blood) : in which oxygen , nutrients, as well as waste products
dissolve.
Dr

B Fick’s law of diffusion:

Surface areaχ concentration gradient

Rate of diffusion=
Thickness of exchange membrane or
barriers( diffusion distance)

Properties of gas exchange surfaces/ factors affecting rate of diffusion of gases across a
membrane :
1. The surface area where the larger the surface area , the more particles can be exchanged at
the same time.
2. The concentration gradient of particles diffusing , the maintaining the concentration gradient
( ex by transporting substances away once they have diffused by continuous blood flow,
ventilation) .
3. The thickness of the exchange surfaces, where the shorter the diffusion distance , the faster
the diffusion can take place.
[Link] Gabr 111
 Sixth: The mammalian gas exchange system:

Features of effective gas exchange system:

1. A large surface area to compensate for the relatively small surface area to volume ratio of
the whole organism.
2. Thin layers to minimize the diffusion distance from one side to another.
3. Continuous Blood flow/ supply to the respiratory surfaces as in animals, maintaining steep
concentration gradient.
4. Moist surface because diffusion takes place with the gases in solution.
5. Permeable surfaces that allow free passage of the respiratory gases.

r
ab
How the structure of human lungs is adapted for efficient gas exchange ?
1. Many alveoli. So large surface area.
lg
2. Covered by extensive network of capillaries , which ensures large surface area for gas
exchange.
3. Thin capillary walls as well as alveolus walls as their walls are made from single layer of
iha
flattened cells. So shorter diffusion distance, allowing faster diffusion.
4. Maintaining steep concentration gradient by ventilation and continuous blood flow.

[Link] in RBCs carry

.N

Human gas exchange system

oxygen
2. Warmer air enables faster
Dr

diffusion and movement of gases

3. Where air is warmed beacuse
lungs are inn core of body
-

vol

2
W
[Link] Gabr 112
 Function

1- nasal passage Warm, clean and add moisture to the air

2-pharynx Common pathway for food&air, ( epiglottis closes the trachea during swallowing which is an
involuntary reflex action)

3- epiglottis Stops food getting into lungs when you swallow.

4- larynx( vocal box) Contains the vocal cords, uses flow of air across it to produce sounds.

5- Trachea Tube with incomplete rings of cartilage, which keeps it open & prevents it from collapse and
allow continuous flow of air into lungs.
Trachea carries air to lungs, lined with goblet cells making mucus, and cells with cilia which
move the mucus away from the lungs.
Notice the incomplete rings of cartilage allows the food to be swallowed and moved
down the oesophagus.

Left and right bronchi These tubes lead to the lungs and are similar in structure to trachea but narrower. They divide to
form bronchioles

r
Bronchioles Small tubes that spread through the lungs and end in alveoli . Their main function is still as an
airway , but some gas exchange can take place.

ab
Pleural membrane Surround the lungs and line the chest cavity forming a sterile sealed unit.

Pleural cavity
lg
Space between the pleural membranes, usually filled with a thin layer of lubricating fluid that
allows the membrane to slide easily with breathing movements.

6- Alveoli Site of gas exchange( thin walled, large surface area, moist, rich in blood supply,well ventilated)
iha
7-Diaphragm A muscle sheet separating the chest cavity(thorax) from the abdominal cavity.
Its dome shaped , with a fibrous middle part forming the roof of the dome, and muscular edges
forming walls . It is flat in the contracting state.
.N

8-internal intercostal Pulls ribs down and in when you breath out ( exhale)
muscles
Dr

9- external intercostal Pulls ribs up and out when you breath in( inhale)
muscle

First : structure
1. Cartilage

Found in trachea and bronchi .

Function:
1. Give support to the walls of the trachea and bronchi .
2. Prevents them from collapse as during inhalation the pressure inside the airways falls
and the cartilage stop them collapsing .
3. Keep air way open and air resistance low.

In trachea : it is C-shaped rings .

In bronchi and large bronchioles: irregular blocks of cartilage .
[Link] Gabr 113
 2. Goblet cells

Found in trachea and bronchi seen in the ciliated epithelium lining.

Mucus is contained in secretory vesicles and released by exocytosis.
Function:
1. Secrete mucus on surface of ciliated epithelium, which is sticky to trap particles of dust,
pollen and bacteria.
2. So pathogens don’t reach the cells lining the trachea/bronchi/ alveoli, thus reducing
chance of infection.

In case of infection : increased secretions of mucus .

3. Ciliated epithelium

Found in trachea and bronchi and in larger bronchioles.

r
Function:

ab
1. Beat back and forth
2. Waft (move) mucus that has trapped dust and bacteria towards back of the throat, where
mucus will be swallowed , so any present bacteria will be destroyed by stomach acid.
3. Thus allowing normal air flow while keeping air ways clean , preventing particles and
lg
bacteria from entering lungs So reducing risk of infection.

Second : How gases are exchanged in the lungs(alveolus)

iha
Gas exchange takes place between alveoli and
blood in blood capillaries, where alveolar air has a
higher concentration of oxygen and a lower
.N

concentration of carbon dioxide than blood in

capillaries.
Oxygen therefore: diffuse from the air in the
Dr

alveoli, across the walls of the alveolus and

capillary and enters the blood .
Carbon dioxide diffuses in the opposite direction.
Where the diffusion gradients are maintained
by:
1. Continious Blood flow past the alveolus ,
which brings deoxygenated blood from the
pulmonary artery and takes away the oxygenated blood through the pulmonary vein
( circulating blood supply).
2. Ventilation of the lungs, which replace alveolar air with air from outside the body.

[Link] Gabr 114

 How alveoli are adapted for gaseous exchange:

r
ab
lg
1. Thin alveolar wall( squamous epithelium)
iha
Alveolar type 1 cell; Which is one cell thick( the alveolar wall is 0.1μm thick) Short distance of
diffusion of gases ( gas exchange) between air in alveolus and blood in capillary which speed up
the rate of diffusion of gases.
.N

2. Many alveoli
Dr

Providing larger surface area for diffusion / gas exchange , where larger number of
molecules( carbon dioxide and oxygen) can diffuse at the same time.

3. Surrounded by many capillaries(capillary network)

1. Capillaries are very close to the alveoli: in other words very little distance between alveolar
epithelium and capillary endothelium for faster rate of diffusion.
2. The walls of the capillary ( endothelium) is one cell thick for short distance of diffusion as
well.
3. The continuous flow of blood in blood capillaries maintain concentration gradient.
4. Form a large network which increase surface area to slow down the rate of flow of blood in
capillaries , for more efficient gas exchange.

[Link] Gabr 115

 4. Surfactant secreting cells:

Alveolar type 2 cells; These are special large rounded cells between squamous epithelial cells in
the alveolar walls secreting pulmonary surfactant( complex of phospholipids and proteins)
1. which reduces surface tension inside the alveoli, keeping the alveolar walls from collapsing as
they deflate during exhalation.
2. Help dissolve oxygen to diffuse into blood.

Simple Diagram showing surfactant's function in stopping the collapse

of the alveoli when exhaling

Walls of alveoli
Thin moist lining/ thin liquid

r
layer to dissolve gases.

ab
Surfactant Will be attracted to the
( phospholipids hydrophilic part of
and proteins) lg surfactant
iha
.N
Dr

[Link] Gabr 116

 Why air reaching lungs doesn’t cause infection

1. Sticky mucus produced by goblet cells and mucous glands traps dust and bacteria thus
prevent bacteria from causing infections of gas exchange and prevent them from
reaching blood ( mucus acting as a barrier)
2. Cilia on ciliated epithelial cells beats back and forth moving mucus carrying dust and
bacteria out of lungs.
3. Macrophage that protect lung by preventing the pathogen entering the blood , by
engulfing inhaled particles and bacteria and digesting them by phagocytosis.

r
ab
lg
iha
.N

Breathing (ventilation) is an active process.

Dr

Inhalation Exhalation
1-Inhalation is an active process, where external 1-normal exhalation which is a passive process,
intercostal muscle contract , moving rib cage up and external Intercostal muscle relax, rib cage falls down
out. under gravity.
Forced exhalation, internal intercostal muscles
contract and pull the ribcage down and in.
2- Diaphragm contracts moving down(flattened) 2- Diaphragm relaxes moving up.( dome shaped)
3- Volume of thoracic cavity increases. 3- Volume of thoracic cavity decreases
4- Pressure of air in lungs decreases,with higher 4- Internal pressure in lungs increases
pressure of air outside the lungs
So air is forced inside the lungs. So air is forced out of lungs
Notice: exhalation is helped by the fact that the lungs are
elastic, so that they tend to empty like balloon.

[Link] Gabr 117

 Inhalation Exhalation

r
ab
lgExam hint;
Role of respiratory system in gas exchange:
1. Ventilation involves removal of Carbon dioxide and bringing of Oxygen , thus
maintaining steep concentration gradient.
iha
2. Alveoli which has ......adaptation( including ,any for large surface area, surfactant, thin
wall, rich in blood capillaries)
3. This allows overcoming the limitation of diffusion ( small surface area to volume
ratio, long diffusion distance, high metabolism and concentration gradient)
.N

How concentration gradient maintained through gas exchange surface

Dr

in human lungs
Ventilation
- Removing carbon dioxide and replenishing oxygen
- Blood flow in capillaries.
- Removing oxygenated blood/ oxygen from alveoli and bringing carbon dioxide to the
alveoli.

Breathing /ventilation:
The process in which physical movement of the chest changes the pressure so that air is
moved in or out aided by diaphragm and intercostal muscles

[Link] Gabr 118

 Topic 2B.1, 2

Introduction to
Enzymes

r
ab
Learning outcomes
Description of how enzymes lg
work.
iha
Investigating the rate at which
substrate converted into
product.
.N

Describing and explaining of

the factors that affect enzyme
activity.
Dr

Comparing the affinity of

different enzymes for their
substrates using Vmax

Explaining how reversible

inhibitors affect the rate of
enzyme activity.

Know that there are

intracellular and extracellular
enzymes.

[Link] Gabr 119

 First: Mode of action of Enzymes:

Definition:
Globular proteins that act as a biological catalyst which speed up chemical reaction by lowering the
activation energy ,but remains unchanged at end of reactions.
Enzymes are specific in their functions by having specific active site.
Most enzymes have tertiary structure ( to enable protein to function,i.e act as biological catalyst), very few
are quaternary.

What makes enzymes specific in their function?

Enzymes have specific active site determined by the specific sequence of amino acids in the polypeptide

r
chain and the overall folding and coiling of the polypeptide chain in a specific way forming a precise 3

ab
dimensional shape bringing amino acids together. Which is maintained by:
I. H- bonds between polar groups(NH- and CO-).
II. Ionic bond between ionised amine and carboxylic acid group
lg
III. Disulfide bonds between cysteine (S-H) groups.
IV. Hydrophobic interaction between non polar side chains.
iha
Describe mechanism of action of enzymes in converting substrate
into products:
.N

Enzyme has a specific active site

Substrate has a complementary shape to the active site.
Dr

Substrate fit into its active site and bind by temporary hydrogen bonding.
Forming Enzyme- substrate complex.
Causing strains/stress in substrate.
So Lowers the activation energy( i.e reaction occurs at lower temperature).
The products produced will no longer fit to the enzymes active site, so they will be
released.
And enzyme will not be used up in reaction

The substrate is held in place by

temporary bonds formed between the
substrate and some of the R groups
of the enzyme’s amino acids.

[Link] Gabr 120

Describe how enzyme work by induced fit mechanism:

Products leaving
active site of enzyme.

Substrate entering active Enzyme-substrate Enzyme-product(s)

r
site of enzyme complex. complex

ab
1. The substrate is partially complementary to the active site (i.e substrate shape not exactly
complementary to active site).
2. Active site changes shape slightly when the substrate binds to it..(i.e moulds and fold around the
substrate).
lg
3. So active site and substrate now complementary and better fit( fit more tightly)
iha
4. Allowing formation of enzyme substrate complex.
5. Where the R groups of the amino acids in the active site interact with the substrate, so strong
bonding of substrate to active site.
.N

6. This interaction can cause the break of the substrate apart, or encourage the formation of bonds
between molecules, forming one , two or more products.
Dr

How enzyme lowers the activation energy to speed up chemical reactions:

Activation energy:
The amount of energy needed to start a chemical reaction (energy needed by reactants to reach
the unstable transition state to be converted into products), as without enzymes reactions would
be too slow to happen.

Where most of the chemical reactions in living cells need very high temperature to be at the
required high rate to produce products,
Our body temperature is 37 °C and we can’t tolerate an increase in this temperature so, Enzymes
are needed to lower down the activation energy needed to change reactants into products , how?

[Link] Gabr 121

 A
A Energy of Transition
state( un catalysed Rx)

B Energy of Transition
state( catalysed Rx) B
i.e enzyme/substrate
complex, during
catalysed reaction.

Overall energy
change

Final state (product)

r
ab
How Enzymes lower the activation energy needed to allow reactions to proceed?
By providing an alternative pathway .
lg
Bring reactants close together in active site forming Enzyme substrate complex.
Where the R groups of the amino acids in the active site interact with the reactant(substrate)
Thus putting strain on the reactants .
iha
So making it easier for bonds in reactant(substrate) to broken down or formed to form products.

Second: investigating progress of enzyme catalysed

reaction:
.N

A. Planning the investigation:

Dr

1. Start the experiment with known

concentration of substrate and enzyme.
2. Set controlled variables; constant pH and
temperature.
3. Take samples every 5 mins ( any time
intervals).
4. Plot a graph with the dependent variable
on y-axis against time on x-axis.
5. The measurable variable can be
( measurement of substrate concentration
or product concentration).
6. From the graph determine the rate of disappearance of substrate or rate of appearance of
product.
7. Also from graph you can determine the initial rate.

[Link] Gabr 122

B. Graph description;
As time increase, the volume of oxygen increase. Fig 1.3 showing course of an enzyme catalysed reaction.
Where in the first , a large volume of oxygen is
collected ( increase steeply till 1min)
As the reaction continues after 1 min , the rate at which
oxygen is released gradually slows down.
The rate of the reaction keeps slowly down till it
eventually stops completely(levels off).

C. Explanation:
1. Initially high concentration of substrate ,
• presence of free active sites ,
• so more enzyme substrate complexes formed, so
high rate of reaction.

r
2. Rate slows down as concentration of substrate decreases( because more substrate is converted to

ab
Product), so less substrate to bind with enzymes.
• Occupied active sites.
• less successful number of collisions. lg
• So less enzyme substrate complexes, so slower rate of reaction by time till it stops( level off as
substrate has been used up).
3. ( while explaining use data quotes as evidence).
iha
D. Initial rate calculation:
Fastest rate of reaction is at the beginning.
How to measure?
.N

1. Either by calculating the slope of a tangent to the curve , as

close to time 0 seconds as possible.
Dr

2. By dividing the volume of the products produced/ OR

substrate used at initial rate of reaction( in first 30 seconds
according to above example) by time taken for this volume to be produced.
3 3
Example to figure 1.3: 2.7/ 30 = 0.09 cm/s or 5.4/ 60= 0.09 cm/s.

[Link] Gabr 123

 Third: Factors affecting Enzyme activity:

1. Enzyme concentration:

Molecular activity/ Turnover number:

Is the number of substrate molecules upon which one molecule of enzyme can act and turn into
product per minute.

In this investigation, different concentrations of catalase

enzymes were added to same volume of substrate(hydrogen
peroxide solutions).
Description :
All curves are similar following same trend of initial steep

r
increase followed by gradual slow down till curves level off.

ab
Notice:
To compare the effect of different enzyme concentrations on
lg
rate of these 5 reactions, it is fair to look at the rate right at
the beginning of the reaction, because once reaction is
going , the amount of substrate in each reaction begins to
iha
vary because substrate is converted into product at different
rates, till rate starts to level off because enzymes are no
longer limiting factors, but the concentration of substrate
.N

will be the limiting factor.

Description:
Dr

Fig 1.5 showing rate of reaction in the first 30 seconds

calculated for each enzyme concentration .. The initial rate of reaction increases linearly with increase
in enzyme concentration, i.e initial reaction rate is directly
proportional to the enzyme concentration ( provided that
all other factors remain constant).
Explanation:
The more enzyme present , the more active sites will be
available for substrate to slot into, so more successful
number of collisions, so more Enzyme substrate
complexes, so higher rate of reaction.
This linear increase will continue as long as there is plenty
of substrate available.

[Link] Gabr 124

 2. Substrate concentration:

Vmax
Levels off
Enzyme concentration
Rate of enzyme activity/ au become a limiting factor.
Where all active sites become
Initial increase saturated (occupied)
in rate
Substrate is limiting factor where rate
increase with the increase in substrate
concentration, as more active sites can be
occupied, more collisions, so more ESC.

r
ab
Substrate concentration/mM

Description: lg
The rate of enzyme activity increase reaching to maximum ....arbitrary units at ...mM. (Vmax)
Then plateau/ levels off.
iha
From 0 mM to ...mM there was a steep increase in rate of activity, then increase in rate slows down
from....au to ...au.
Explanation:
.N

At low concentration of substrate:

Substrate is a limiting factor.
Dr

There are few collisions between enzyme and substrate.

Some Active sites are unoccupied( i.e become more occupied by increasing substrate concentration),
so few Enzyme substrate complexes formed.
At higher concentration of substrate:( after reaching Vmax)
Enzyme concentration is a limiting factor as at this point, only the increase in enzyme concentration will
increase rate of reaction.
All active sites occupied.
Maximum number of enzyme substrate complexes formed.
So further increase in substrate concentration doesn’t increase rate.

[Link] Gabr 125

 3. Temperature and enzyme
activity:

Temperature coefficient Q10 Optimum

Rate of reaction at (χ+10)°C H-bond formed temperature
Q10= temporary Enzyme
Rate of reaction at χ°C between enzyme becoming
and substrate. denature.
Is the measure of effect of temperature on rate of reaction
Rate of Rx
increases,

Rate of reaction
doubling with
Description: each 10°C rise in
temperature. Enzyme
As temperature increase till 37C , the rate of reaction
completely
increase gradually, reaching to the maximum rate at denature.
temperature 37C, then above this optimum temperature
the rate of the reaction decrease steeply .
Explanation:

r
Below optimum:

ab
1. The increase in temperature, cause an increase in
the kinetic energy of enzyme and substrate molecules. As temperature decrease below
2. So molecules move faster. optimum, enzyme deactivation occurs
by losing their kinetic energy, so
3. So increase in frequency of collision.
4. So more successful number of collisions.
lg decreasing collision,...
The deactivated enzyme can work
again.
5. So more chances to fit and bind together.
iha
6. So more enzyme substrate complexes .
( notice that each 10°C before optimum doubles the rate of reaction)
At 37°C :
.N

Optimum temperature where the enzyme works best.

Increasing temperature above optimum:
1. Decrease steeply in rate of reaction, as molecules vibrate so energetically that some of the bonds
Dr

holding the enzyme molecule in its precise shape start to break .

2. Mainly hydrogen bonds ( and ionic bonds) .
3. So the enzyme will lose its tertiary structure.
4. The shape of active site and its activity will be lost, as the 3D shape of enzyme is changed.
5. The enzyme is denatured (irreversible)
Notice that the peptide bond will be the last to break as temperature increase.

Learning Tip
Not all enzymes have the same optimum conditions.
Enzymes in human have optimum temperature about 37°C because thats our body temperature.
But other organisms may have different optimum set of condition
Example: thermophilic bacteria living in hot springs at temperature up to 85°C, can work at very
high temperature. They are made of temperature resistant proteins that contain a very high density of
hydrogen bonds and disulfide bonds, which hold them together even at high temperature.

[Link] Gabr 126

 4. pH and enzyme activity:

Different enzymes work in different ranges of pH

Description:
At pH 7 , its the optimum pH for this enzyme, where the
enzyme work fastest.
Above or below optimum there is a steep decrease in rate
of reaction( activity declines).

Explanation:
At optimum pH maximum activity .
Major Change in pH, means change in concentration of

r
hydrogen ions in a solution.

ab
The charges of the R groups of amino acids at active site may be affected(changed).
So hydrogen and ionic bonds between amino acids break.
Where the hydrogen and ionic bonds are important in maintaining shape of tertiary structure ( active site)
lg
So active site is altered, as the 3D shape of enzyme is changed.
Enzyme denatured.
So substrate no longer fits so enzyme substrate complex not formed.
iha

Fourth: Comparing Enzymes affinity for their

.N

substrates:
1. Turnover number:
Dr

Is the number of substrate molecules upon which one molecule of enzyme can act and turn into
product per minute, when the enzyme is the rate limiting factor.
Asymptotic curve
2. Vmax: Maximum speed .
It is the maximum rate of enzyme catalysed

÷
reaction.
• At V max all the enzyme molecules are bound to
substrate molecules ,
• The active sites of enzyme are saturated with the
substrate. B
• Vmax is determined by enzyme concentration.

[Link] Gabr 127

Topic 2B 3. 4. 5. 6.

Introduction to
Nucleic acid and
protein synthesis

r
Learning outcomes
ab
lg
iha
Description of the structure of
nucleotides and nucleic acids.
.N

Description of the semi

conservative replication of DNA.
Dr

Explain how the sequence of

nucleotides in DNA codes for the
sequence of amino acids in a
polypeptide..

Explain the roles of DNA and

RNA in transcription and
translation.

Discuss the effect of gene

mutation.

[Link] Gabr 135

 [Link]: structure of DNA and RNA:
Nucleic acids: are formed from many nucleotides held together by phosphodiester bonds
forming polynucleotides/ They are polymers made from monomers known as nucleotides .
DNA and RNA are therefore polynucleotides.

Nucleotides:
Made up of three smaller components ;
1. Phosphate group ( negatively charged)
2. Pentose sugar ( deoxyribose in DNA and ribose in RNA)
3. Nitrogen-containing base.
• The three units are linked together by condensation reaction, with elimination of two
water molecules, to form a mononucleotide.

1. Nitrogenous bases

r
There are just five types of nitrogen bases in DNA and RNA.

ab
The nitrogen bases of the DNA are adenine, thymine, guanine, and
cytosine.
The nitrogen bases of the RNA are adenine, uracil, guanine
lg and
cytosine.
iha
.N
Dr

2 rings 1 ring

The difference between deoxyribose and

ribose is that deoxyribose has one less
oxygen atom in its molecule.

[Link] Gabr 136

 Notice: ATP ( adenosine triphosphate
molecule):
It is a phosphorylated mono nucleotide , made from
ribose( pentose sugar), adenine( nitrogen base), forming
adenosine and can be combined with one, two or three
phosphate groups to give, in turn, adenosine monophosphate
(AMP), adenosine di phosphate (ADP) or adenosine triphosphate
(ATP).

What is ATP?
A universal energy currency of cells as it is :
1. Small and water soluble so can easily diffuse
between cell organelles.
2. Immediate energy donor as it is easily hydrolysed to into

r
ADP to release energy in presence of water.

ab
Uses of ATP:
1. Cell division.
2. Muscle contraction lg
3. Maintenance of body temperature.
4. Anabolic reactions such as protein synthesis.
5. Nerve impulse transmission.
iha
2. The formation of polynucleotide (in both DNA/RNA)
Formed during interphase , where many nucleotides are
.N

linked together by a condensation reaction forming

phosphodiester bond between phosphates of one
Dr

nucleotide and carbon 3’ in the 3’

sugar(ribose/deoxyribose) of the other
nucleotide. 5’
Thus the phosphodiester bond links the 5-
carbon of one sugar with the 3-carbon of
the next.
Forming a sugar phosphate back bone with
its bases at one side( pointing inwards from the
2 sugar phosphate backbones in case of DNA). 3’

5’

[Link] Gabr 137

 First :the structure of DNA
molecule:

1. 2 polynucleotide strands (each nucleotide =deoxyribose, phosphate & nitrogenous base.

2. Running in opposite direction(anti parallel),i.e strands are 3’to 5’ and 5’ to 3’.
3. Held together by Hydrogen bonds between the nitrogenous bases, between the amino
and carbonyl groups of purine and pyrimidine bases on opposite strands.
4. Where the bases pair together according to a complementary base pairing rule where in
each base pair there is a purine and pyrimidine
Adenine pairs with thymine (A=Τ) and guanine pairs with cytosine (GΞC)
5. Each strand has a sugar phosphate backbone with phosphodiester bonds.
6. The two strands twist forming a double helix(3D shape)
7. Each full turn in a DNA molecule has 10 base pairs , 3.4 nm length.

r
ab
Base pair

lg Sugar phosphate
backbone
iha
.N
Dr

know how to
draw H- bonds
between the bases
Line between O-H,
N-H

[Link] Gabr 138

Explain the importance of the hydrogen bonding between the 2 strands of DNA ?
1. Hold the two polynucleotide strands together.
2. Important in contributing to 3D structure of DNA molecule(where the hydrogen bonds
between bases stabilize the α-helix structure).
3. Many hydrogen bonds give stability.
4. H-bonds more easily broken than covalent bonds.
- So strands can be separated for replication(transcription)
5. H-bonds only formed between specific bases so few mistakes (faithful replication).
6. H- bonds can easily reform without chemical reaction .

Structural feature of DNA making it stable molecule?

1. Complementary base pairing holds the strands together.
2. Because of many hydrogen bonds holding the strands together.

r
3. Sugar phosphate backbone with phosphodiester bonds.

ab
4. Double helix structure protects bases .
5. Coiling protects from enzyme or any chemical attack.
lg
Why DNA should stay stable( not broken by enzymes or any chemical reaction) ,i.e
genetic stability?
iha
1. Sequence won’t be spontaneously changed so decreasing chance of mutation So Protein
produced will always be functional.
2. Maintains all genetic information through out life of cell So same genetic information
passed on to daughter cells(offsprings).
.N

3. Maintain size so still enclosed within the nucleus.

Second :structure of RNA ( at the end

Dr

of the topic)

[Link]: Semi-conservative replication of DNA:

What is semi conservative replication?

Its an increase in number of DNA molecules, where both strands of original DNA are
replicated/ copies. Each old parental strand acts as a template to form a new
complementary strand Producing two genetically identical molecules( where the
new DNA molecule has one old-and one new strand)Occurs during S phase of cell
cycle( late interphase).

[Link] Gabr 139

Steps of DNA replication(semiconservative) Waston and Crick hypothesis:
1. The DNA double helix unwinds.
2. The hydrogen bonds between complementary bases broken by enzyme DNA
helicase( strands separate).
3. The free activated nucleotides line up along both strands.
4. Where Both DNA strands act as templates , where each of the bases of activated DNA
nucleotides pair up with its complementary base on each of the old DNA strand( A=T,
CΞG) and hydrogen bonds formed between bases.
5. DNA polymerase enzyme lines up the new nucleotides along the DNA template strand
step by step Sequentially).
6. DNA ligase is an enzyme that catalyse the formation of phosphodiester bonds between
adjacent mononucleotides.

r
7. Process continues along whole DNA molecule.

ab
8. Producing two genetically identical DNA molecules.
9. Replication is semi conservative where each newly formed DNA molecule contains one
original and one newly synthesised DNA strand.
lg
10. Where each of the two strands , the old and new complementary one will wind together
forming two DNA helices genetically identical to each other and to their mother
iha
1 2
.N
Dr

[Link] Gabr 140

4
Experimental evidence for the semi conservative replication of DNA by
Meselson,and stahl).
In the 1950s, no-one knew exactly how DNA replicated.
Three possibilities were suggested:
conservative replication, in which one completely new double helix would be made from the
old one (Figure a)
semi-conservative replication, in which each new molecule would contain one old strand
and one new one (Figure b)
dispersive replication, in which each new molecule would be made of old bits and new bits
scattered randomly through the molecules (Figure c).

r
ab
lg
1. Bacteria(. E. coli) were grown for many generations in a medium containing ammonium chloride with
the heavy isotopes nitrogen-15 (. 15N).
2. This produces bacteria with heavy nitrogen-15 carried in both strands of the DNA molecule, this DNA
iha
would be heavier than DNA with nitrogen-14.
3. The bacteria with heavy nitrogen-15 strands in its DNA molecule were grown in a medium containing
the normal nitrogen isotope N14 and were left to divide one generation.
4. The off springs showed DNA molecule with both strands N14 N.15
.N

14 14 15 14
5. The second generation had N N and N N
Dr

Sample 1
with only
heavy DNA

Sample 2
first
generation

All of the DNA has one heavy strand

and one light strand Hybrid)
Sample 3
second
generation

Half of the DNA molecules have light

DNA and half are hybrid with one light
and one heavy strand.
Sample 4
third
generation

[Link] Gabr 141

Topic 2C

Introduction to
Gene expression
and genetics

r
ab
Learning outcomes

Understand how errors in DNA

replication give rise to
lg
mutation.
iha
Some mutations will give rise
to cancer or genetic disorders
but many mutations will have
.N

no observable effect.
Dr

Genetic pedigree for

monohybrid inheritance.

Sex linkage on X chromosome

Genetic disease cystic fibrosis.

Genetic screening

[Link] Gabr 149

 First 2C.1 :Gene mutation:
Definition:
Alteration in DNA by Sudden, random change in the base sequence of DNA .

Causes of mutation

Error during DNA Exposure to

replication mutagen

As errors are copied during

replication Chemicals such Physical such as
as mustard gas, x-rays, U.V rays
Where wrong bases are tobacco smoke.
inserted

r
Types of mutation

ab
A. Gene mutation
lg B. Chromosomal
mutation

Point mutation Frame shift

(Substitution)
iha
a change in a single base of the
Insertion
DNA code.
HAITI
Deletion
Point mutation can have one of
three effects. Where the nucleotide
.N

Where the nucleotide

is missed out. in inserted twice
So the entire base instead of once.
Silent So the entire base
Non sense Missense sequence is altered,
Dr

mutation sequence is altered,

where each triplet
the base the base the base after mutation is where each triplet
substitution can substitution can substitution can changed. after mutation is
be silent be nonsense be missense The whole gene is changed.
mutation where mutation where now different and The whole gene is
mutation where
the altered codon will code for an now different and
the altered codon the altered
entirely different will code for an
corresponds to codon corresponds to a
protein. entirely different
the same amino corresponds to a different amino
protein.
acid. stop signal. acid.

[Link] Gabr 150

 Gene mutation

Random change in base sequence of DNA during DNA replication ….thus producing new allele ..leading
to protein of different function / shape .
Where errors are being copied during replication
When wrong base is being inserted
Causes of muatation
Exposure to mutagens : chemicals as tobacco smoke and mustard gas
Physical such U.V rays , x rays

Types of mutation
Shift reading
I. backward one
Shift reading
Point mutation Frame shift place forward one place
( substitution )
Change in one single base of DNA code
Affects only
one triplet
←
f.
Deletion Insertion
→

Has one of three effects code One nucleotide is

One extra nucleotide is
missed out ..so the
Silent mutation Non sense Mis sense entire base sequence is inserted ….so the
The base altered ..coding for an entire base sequence is
The base substitution
The base
substitution can entirely different altered after
&

can be non sense .

substitution is protein …where all
Where the altered be mis sense mutation ..so all amino
silent ..where the codon corresponds to amino acids are
mutation where acids after mutation
altered codon a stop codon , so new different after mutation
the altered are affected ,code for
code for same poly peptide might be …so 3D shape of
shorter codon , code for protein is changed
different protein
amino acid
another amino The to Closer to the start , the greater the effect
 r
ab
lg
iha
.N
Dr

[Link] Gabr 151

 B. Chromosomal
mutation

Whole
Chromosomal
chromosome
mutation
mutations
Change in the position of entire
The loss or duplication of whole chromosome
genes within a chromosome.
during meiosis.
Example: down syndrome which is caused by
a whole chromosome mutation at
chromosome 21

- Gene mutation : Read only

• change in nucleotide( base) sequence of DNA , so a new allele is formed .
• This can happen by deletion , substitution, addition.

r
• This change lead to change in the transcribed mRNA (mRNA with altered codons).

ab
• In case of substitution : a new amino acid with different R group may be
incorporated into the growing chain at the ribosome during translation.
• Causing a change in primary structure of protein( amino acid sequence on polypeptide).
lg
• Change in three dimensional shape of protein.
• So different protein with altered function or totally un functional protein may be produced.
iha
Also mutation can lead to cancer characterised by uncontrolled cell division to form a mass of
cells (functionless) known as a tumor.
.N

1 DNA- 2 mRNA- 3 Polypeptide-

One triplet is One codon is One amino acid is
different different different
Dr

(substitution) 4 Function of protein-

polypeptide forms a
different shape.
Amino acid Phe replaced
by Leu so bind cant be
firmed to form shape of
active site

5 Phenotype-
enzyme can’t function because
shape of active
mm
site is changed. Lack
of enzyme causes a genetic disease.
Individual is not healthy.

[Link] Gabr 152

 Explain why most mutation has no observable effect ?\
Imp
1. Genetic code is degenerate 3. Occur in non coding DNA
2. DNA repair mechanism 4. One allele might be affected Imp
Explanation of how a change in DNA sequence might lead to loss of enzyme activity
1. Mutation takes place where there is a change in base sequence of gene, so a new allele is

=
formed.
2. Resulting in a changed, mRNA codons
4. So different tRNA with different anticodon will be involved, as the tRNA will carry
different(incorrect) amino acid to ribosome.
5. So incorrect amino acid might be incorporated into the growing polypeptide chain, so change in
sequence of amino acids, meaning change in primary structure.
6. Polypeptide will fold differently ,leading to Change in tertiary structure(3D shape)
8. Active site will have a different shape/ charge.

r
9. So substrate no longer binds to active site.

ab
Genetic disorder
lg
Disorder resulting from a defect in gene

Sickle cell anemia as another example: Its an example of substitution mutation.

iha
The gene which codes for the amino acid sequence in the β polypeptides is not the same in
everyone. In most people, the β polypeptides begin with the amino acid sequence:
Val-His-Leu-Thr-Pro-Glu-Glu-Lys-
This is coded from the HbA (normal) allele of the gene. Hydrophilic R group
.N

But in some people, the base sequence GAG is replaced by GTG, and the amino acid sequence
becomes:
Dr

Val -Hi s-Leu-Thr-Pro-Val -Glu-Lys-

This is coded from the HbS (sickle cell) allele of the [Link] R group
This type of mutation is called a substitution. In this case, the small difference in the amino acid
sequence results in the genetic disease sickle cell anaemia in individuals with two copies of the
HbS allele.

[Link] Gabr 153

 Second: 2C.2 :pattern of inheritance:

Gene:

A length of DNA coding for specific protein, determining specific characteristics.

Allele:

Alternative forms of same gene.

May be:

Dominant Recessive

r
Allele expressed in phenotype only

ab
Allele expressed in phenotype
when individual is homozygous for
whether the individual is
homozygous or heterozygous for =
that recessive trait.( both alleles
coding for recessive trait)
that allele.
lg
Homozygote : Heterozygote :
iha
An individual An individual
when both alleles where the 2
coding for a alleles coding for
.N

particular a particular
characteristic are characteristic are
identical different
Dr

Genotype:

Genetic make up of an organism with respect to a particular feature

OR combination of /pair of / two / all alleles present in an organism of a particular
trait.
BE
Phenotype:

All characteristics of an organism

Determined by an interaction between genes(genotype) and environment
(observable features)

[Link] Gabr 154

 True breeding:

A homozygous organism which will always produce the same offspring when crossed
with another true breeding organism for the same characteristic.
which means the parents must be both
mm
dominant or both recessive.
nvm

Monohybrid BBx BB bb x bb
cross

A genetic cross where only one gene for one characteristic is considered.

r
ab
lg
Test cross A test made to find out the genotype of an individual with dominant phenotype
iha
for a particular gene by crossing it with one known to have the homozygous
PBB
=
BI recessive genotype for the same gene.
To reveal the parental genotype ( being homozygous dominant or
heterozygous.
.N
Dr

[Link] Gabr 155

 Codominance:

When pair of alleles are equally dominant , so in heterozygous where both alleles at a gene
locus are fully expressed in the phenotype.
Example blood groups

I A and I B are codominant . This means both alleles are expressed and produce their
proteins (antigens) which act together without mixing.
A B
So person with genotype I I will have both antigens, antigen A and antigen B on the
surface of their erythrocytes and will have blood group AB.

1 2

r
ab
Parental phenotype : mother group A Parental phenotype : mother group B
lg
Father group O Father group A
iha
3 Exam hint:
When asked to explain why a
certain organism is used for
.N

scientific experiments:
1. May have short life cycle.
2. Organism may be cheap
Dr

Parental phenotype : mother group A and easy to keep.

Father group B 3. It may produce many
offsprings

Pair of alleles are equally dominant , so in heterozygous , where both alleles at a gene
locus are fully expressed in the phenotype
So the phenotype is intermediate of both
A id dominant over O IAIAIIAIO O is recessive I°I°
B is dominant over O IBIBIIBIO A and B are exmaple of codominance
IAIB AIN?
→
I
A
[Link] Gabr 156 B
 Sampling error:
Rr rr
The theoretical ratios of phenotypes that areMother
Father
predicted by a genetic cross are usually seen
(approximately) in real genetic experiments , however, the numbers are never precise .
This is may be due to: -
1. Reproduction is a result of chance. Where combination of alleles in each gamete is
rr

/
completely random andRr so is the joining of particular gamete.
Yet the theoretical diagrams we draw doesn’t show this.
Child 1 Chill .

#
2. Some offsprings die before they can be sampled . Example some seeds don’t germinate and
some embryos miscarry.

3. Inefficient sampling techniques, example its very easy to allow few Drosophila to escape.

Solution

r
1. So sampling error must be taken into account specially when you are using smaller sample

ab
2. use fast growing plants , Drosophila, and certain fungi and bacteria are so useful as they all
produce large number of offsprings kn a short time.

Genetic pedigree:

r
lg
Tt Tv
fr
bb☒b=
iha
. .

it .
E- *

AR TT * * *
.N

É et et
Tx A * *
Dr

Recessive
Learning tip:
Always remember
to look for the alleles shows
individuals that
show the recessive low
=
phenotype because
these are the only frequency
Solution
ones where you
can be sure of the
genotype- they are
double recessive.

[Link] Gabr 157

 Genetic pedigree
useful in case of:

Useful incase of genetic diseases, as they help predict which family members may be carriers/
diseased by gene mutation.
Used whenever selective breeding for animals is needed.

=
They can track mutation in rate animals.

Male

Female
A B
Learning tip: Learning tip:
This tree shows a
When 2 normal parents
recessive genetic disorder
(1,2)give rise to abnormal
as two normal
parents(1,2)give rise to
diseased child(3).

r
diseased child (3) Possible conclusion:
Disease is recessive

ab
Parents are heterozygous
Child homozygous recessive
lg and has obtained
iha
Third: 2C.3 :Sex linkage:
The chromosomes
.N

Autosomes found in all body cells

carrying information
Dr

controlling body
characteristics but
don’t determine the
gender/ sex.

An individual who produces gametes that contain

Homogametic: only one type of sex chromosome -in human this is
the female.

An individual who produces two types of gametes

Heterogametic: each containing different types of sex chromosome -in human this is the
male.

[Link] Gabr 158

 recessive -

Genetic disease controlled by faulty allele ( resulting from a mutated

unkind
Sex linked disease; allele), carried on a sex chromosome (x-chromosome) , making it
more common in males than in females and is inherited on X-
chromosome to the next generation from the parent.
B i

got XY
.

BB
XX
-

b
got XY
-
.

Bb
XX
b •

bb
XX
B •

r
ab
lg
*④Recessive sex linked diseases, are more common in males than females, as males have only one X
chromosome and thus can’t be heterozygous carriers, so if they inherit a recessive allele on X
chromosome from the mother they are diseased.
iha
-

Examples:
.N

Red green colour

A
blindness:
Dr

Example 2 : Colour blindness (red-green colour

blindness)
The normal (dominant) allele of the gene causes a protein to
be produced that forms the pigment in the cones of the eye
that detects green light . The mutant (recessive) allele does
not cause this pigment to be formed, b.
A person who is homozygous for this mutant recessive allele
have difficulty seeing the difference between red & green.

[Link] Gabr 159

 b
BB

✗4
•

✗4 ✗ ¥
¥

r
ab
lg
B Hemophilia
iha
Example 2 : Haemophilia.
A condition caused by gene mutation which affects production
of a certain protein that is important in clotting.
.N

The disease is recessive, h.

people with haemophilia tend to bleed internally into joints and
[Link] can lead to chronic pain and arthritis.
Dr

[Link] Gabr 160