Chemical bond

Chemistry of Life • Covalent bonds

– Sharing electrons btw 2 atoms
• Ionic bonds
– Bond btw ions with opposite charges
• Hydrogen bonds
– Bond between H and O, N
• van der Waals force
– Hydrophobic interactions
1 2
[Link] Chaicherdsakul

Covalent bond Ionic bond

3 4
 Salt

Water is basis of life

5 6

Water molecule Water status

Hydrogen bond

Weak polar molecule

7 8
 Why ice floats? Water’s Life supporting properties
• Cohesive nature
– Hydrogen bonds give water unusually high surface
tension
– Vital for water transport in plants
• Ability to moderate temperature
– Hydrogen bonds give water strong resistance to
temperature change
– Water absorb and store large amounts of heat while
only changing a few degrees in temperature
• Versatility of water as solvent
9 10

Cohesion of water molecules Temperature moderation

• Cohesion: bond • Earth’s giant supply causes temperatures to stay
between water within limits that permit life
molecules • Evaporation removes heat from the earth and
organisms
• Adhesion: bond
between water
molecules and
surface (xylem)

11 12
 Solvent of life Formula
• Solution is a liquid containing two or more • Chemical formula
substances evenly mixed
– The number and type of atoms that C H O
3 6 3
make up a molecule of material
• Structural formula
– A chemical formula that shows the
number and kinds of atoms in a
molecule and how the atoms and
bonds in the molecule are
arranged
13 14

What is life made of? Chemistry of Life

Atomic# Symbol Element % Body Wt
1. Organic molecules:
1 H Hydrogen 9.5 Carbon-containing molecules except CO, CO2
6 C Carbon 18.5
7 N Nitrogen 3.3 – Carbohydrates
8 O Oxygen 65.0 – Lipids
11 Na Sodium 0.2
– Proteins
12 Mg Magnesium 0.1
15 P Phosphorus 1.0 – Nucleic acids
16 S Sulfur 0.3 2. Inorganic molecules:
17 Cl Chlorine 0.2
19 K Potassium 0.4 Abundant in non-living, less complex
20 Ca Calcium 1.5 Na+, K+, Mg2+, Ca2+, HPO42+, Cl-, HCO3-
26 Fe Iron <0.01 15 16
 Carbon chemistry Carbon chemistry
• Carbon has four electrons in an outer shell that • Carbon can use its bonds to form an endless
holds eight diversity of carbon skeletons
• Carbon can share its electrons with other atoms
to form up to four covalent bonds

17 18

Functional groups Some common functional groups

• The unique properties of an organic

compound depend not only on its carbon
skeleton but also on the atoms attached to
the skeleton
• These atoms are called functional groups
• Atom or a group of atoms that is responsible
for the chemical behavior of a substance

19 20
Most macromolecules are polymers Breaking down of macromolecules
• Polymers are made by stringing together many • Macromolecules will be broken down by a process
smaller molecules called monomers called hydrolysis
• Cells link monomers by a process called • Sucrose  Glucose + Fructose
dehydration synthesis or condensation

21 22

Organic compounds

• Lipids

• Carbohydrates
Lipid

• Proteins

• Nucleic acids

23 24
 Lipid Lipid function

• Slightly dissolve in water o Energy storage

o More cal/g than carbohydrates & proteins
• Dissolve in organic solvents e.g. ether,
o Water insoluble  light weight
chloroform, ethanol
o Cell membrane
1. Simple lipid: Fatty acid, Triglyceride o Heat/cold insulator
2. Complex lipid: Phospholipid o Skin moisture
3. Derivative lipid: Steroids o Hormone e.g. testosterone (male), estradiol
(female), cortisol & aldosterone (adrenal gland)
25 26

Fatty acid Fatty acid

o Long hydrocarbon chain with carboxylic acid 1. Saturated fatty acid: All are single bonds
group (COOH) at the end 2. Unsaturated fatty acid: Contains double bonds
Amphipathic molecule
Hydrophilic (water loving)
Hydrophobic (water fearing)

27 28
 Fatty acid
No. of C: DB Melting point (ºc)
– 12:0 Lauric acid 44.2
Animal oil,
– 14:0 Myristic acid 53.9 Coconut oil
– 16:0 Palmitic acid 63.1
– 18:0 Stearic acid 69.6
Room temp
– 18:1 Oleic acid 13.4
– 18:2 Linoleic acid -5 Plant oil
– 18:3 Linolenic acid -11

29 30
[Link] 17 May 2015

US orders ban on 'unsafe' trans-fats Trans fats

• Trans-fats are unsafe to eat and must be banned from the food
supply within three years, US regulators have said.
• The US Food and Drug Administration said partially hydrogenated
oils (PHOs), the main source of trans-fats, are not "generally
recognised as safe".
• It said a ban would save lives by preventing fatal heart attacks.
• Food suppliers have been required to show trans-fats information on
food labels since 2006 but health experts say Americans still
consume too much.
• "The FDA's action on this major source of artificial trans-fat
demonstrates the agency's commitment to the heart health of all
Americans," said FDA's Acting Commissioner Stephen Ostroff.
• "This action is expected to reduce coronary heart disease and
• solids or semi-solids
prevent thousands of fatal heart attacks every year." • long shelf life
31
• cheap 32
 War on trans-fats Triglyceride
• made by pumping vegetable oils with hydrogen • 1 Glycerol
which makes them solids or semi-solids
• eating trans-fats took off in the 1970s when • 3 fatty acids
margarine became popular
• popular foods that may have trans-fats: French
fries, fried meats, frosting
• cheap to produce with a long shelf life
• World Health Organization calls them 'toxic'
• many companies already working to remove
them from foods
33 Non-polar molecule
34

Phospholipid Phospholipid
Consist of:
Glycerol
2 Fatty acids:
H2O fearing
1 Phosphate group:
H2O loving
Micelle
Amphipathic

35 36
Biological cell
 Steroids Cholesterol
• Steroids are very • Flat shape
different from fats in • Between phospholipids
structure and function
• Increase membrane stability
– The carbon skeleton Cholesterol

is bent to form four

• Too much will decrease
fused rings fluidity & permeability of
• Cholesterol membrane

• Sex hormones • Found in animal cells

Testosterone A type of estrogen

37 38

Synthetic anabolic steroids

They are variants of
testosterone
Some athletes use them
Carbohydrate
to build up their muscles
quickly
They can pose serious
health risks
Figure
393.17 40
 Carbohydrates in daily life Carbohydrates in daily life

• Americans consume an • People who are lactose intolerant do not

average of 140 pounds of produce enough of the enzyme lactase
sugar per person per year
– Their cells cannot break
down and absorb lactose
• Cellulose, found in plant cell • Lactose intolerance can
walls, is the most abundant be managed by
organic compound on Earth
– Eating lactose-free foods
– Ingesting lactase in pill
• Milk is rich in many nutrients but make some
form
people ill. This is called lactose intolerance
41 42

Carbohydrates or glycan Type of Carbohydrates

• [CH2O]n n=3-8 • Monosaccharides
– C= carbo, H2O = hydrate – C3: Glyceraldehye
– Saccharide – C4: Erythrose, Theose
– C5: Ribose, Arabinose, Xylose, Lyxose
• Functions
– C6: Glucose, Fructose, Galactose, Mannose
– Storage: Glycogen, starch
– C7: Sedoheptulose
– Structure: Cellulose, Chitin
• Disaccharides: sucrose, maltose, lactose
– Cell recognition: Blood groups (A, B, AB, O)
• Polysaccharides: starch, glycogen, cellulose
43 44
 Monosaccharides Isomers
• Monosaccharides are simple sugars • Monosaccharides Aldehyde Ketone
• Monosaccharides are the main fuel that cells glucose and
use for cellular work fructose are
isomers
– Glucose, found in
sports drinks – Their atoms are
arranged
– Fructose, found in differently
fruit

• Honey contains
both glucose and
fructose
Glucose Fructose
45 46

Ring structure of glucose

Ring structure of fructose
• In aqueous solution, monosaccharides form rings

47 48
Alpha () Beta ()
 Disaccharide Disaccharide

• Disaccharides are joined by the process of

dehydration synthesis or condensation

Alpha 1 4 Glycosidic bond

49 50

Polysaccharides Polysaccharides
Long chain • Varies depending on types of monosaccharide,
Alpha 1 4
length, linkage, degree of branching
• Glycogen
• Starch
– Amylose
Branching – Amypectin
Alpha 1 6
• Cellulose

51 52
 Starch

amylopectin

53 54

Starch Glycogen
• Amylose: Long (14), Unbranched
• Monosaccharide: Glucose
• Amylopectin: Long (14), Branched (16 )
• Long (14), Branched (16)
• Granules in liver

55 56
Amylose Amylopectin
 Cellulose
• Long (14) Unbranched

Starch & Cellulose

H bond

57 58

Polysaccharides Blood groups

Cellulose Amylopectin Glycogen Blood Antigens Antibodies Can get
group on RBC in serum blood from

A A Anti-B O, A
B B Anti-A O, B
AB A, B None O, A,
B, AB
O None Anti-A O
Anti-B
59 60
 Blood groups

Nucleic acid

61 62

Nucleic acid Bases

Nucleotide: Nitrogenous bases
1. Sugar: Ribose
Pyrimidines
Deoxyribose nucleic acid:DNA
Ribose nucleic acid:RNA
Thymine (T)
2. Phosphate group Cytosine (C)
Thymine (T) Cytosine (C)
3. Base: Purines or Pyrimidines Purine
Adenine (A)
Guanine (G)

63
Adenine (A) Guanine (G) 64
 DNA structure DNA structure

These chains are called polynucleotides, or DNA strands

A sugar-phosphate backbone joins them together 65 Double helix 66

RNA DNA & RNA

Nitrogenous base
(A,G,C, or U)
Ribose nucleic Phosphate
group
acid Deoxyribose Ribose

Its sugar has an Double strand Single strand

OH group at C2 Uracil (U)

TAGC UAGC

It has the base

uracil (U) instead
of thymine (T)
Sugar (ribose) 67 68
 Forming a DNA strand
5’

Protein

3’ 69 70

Proteins Amino acid

Four types of proteins
• Protein is made of
Amino Carboxyl
20 different amino group group

acids
R

(b) Storage proteins

• Amine (amino) + group

COOH (acid) Leucine Serine

(a) Structural proteins
• A side group that is
variable among all
20 amino acid Side
groups

(hydrophobic) (hydrophilic)
(d) Transport proteins 71 72
(c) Contractile proteins
 Amino acid Amino acid

73 74

Peptide bond Peptide bond

• Each amino acids

are linked by a Side
group
Side
group
peptide bond Amino acid Amino acid

Dehydration
synthesis

Side Side
group group

Peptide bond 75 76
 Protein structure Protein structure

Four levels of protein Hydrogen bond

structure
Primary Pleated sheet One polypeptide

Secondary Amino acid

(a) Primary structure

Alpha helix
Hydrogen bond
Beta sheet Four polypeptides

Tertiary: Globular Alpha helix

(b) Secondary (c) Tertiary

Quarterly: More than 1 units structure structure

Primary structure
77 78
(d) Quaternary structure

Protein structure Protein malnutrition

• Proteins are required for

growth & development
• Protein malnutrition in
children
– Maramus, Kwashiorkor
– Normal bone
– Decreased muscle,
Cytochrome C Hemoglobin
immune sys, skin
Tertiary structure Quaternary structure
pigment, hair color
79 80
Intermediate
 Chemical reactions
• Metabolism: Sum of chemical reactions occur in living
body
– Thousands reactions occur in cell
– All reactions are connected
• Anabolism: Synthesis of complicated molecules from
simpler precursors
– Amino acids  Proteins
• Catabolism: Breakdown of complex molecules to form
simpler molecules & to liberate energy
– Glucose  CO2 + H2O + Energy (ATP) 81 82

Chemical reactions Exergonic & Endergonic reactions

Reactant (R) Product (P)

• Gibbs Free Energy (G): Maximum amount of work
obtained at a constant temperature and pressure
– “Available energy”
• Energy level (G) = GP – GR
– G - Exergonic reaction
– G + Endergonic reaction
• Heat level (H) = HP – HR
– H - Exerthermic reaction
– H + Enderthermic reaction 83 84
 Biological reaction Enzyme function
• Spontaneous reaction
– Gibbs Free Energy is minus (G –)
– Sucrose + H2O  Glucose + Fructose
G = -7.0 kcal/mole
– This reaction is VERY slow (centuries & no
noticeable changes)
• Enzyme-catalyzed reaction
– Reduce activation energy (Ea)
– Substrate/reactant will bind at active site of enzyme
85 86

Examples
• Catalase. It catalyzes the decomposition of hydrogen
peroxide into water and oxygen
2H2O2 -> 2H2O + O2
– One molecule of catalase can break 40 million
molecules of hydrogen peroxide each second
• Carbonic anhydrase. It is found in red blood cells
where it catalyzes the reaction
CO2 + H2O ↔ H+ + HCO3−
– It enables red blood cells to transport carbon dioxide
from the tissues to the lungs
– One molecule of carbonic anhydrase can process one
87 million molecules of CO2 each second 88
 Enzyme Factors affecting enzyme activity
• Holoenzyme: A complete functional enzyme
• pH
– Apoenzyme
– Changes in pH result in breaking of bonds
– Prosthetic group
– Denature: altering protein forms & lose activity
• Cofactor: Inorganic molecule e.g. Mg2+,Fe2+,Cu2+
• Coenzyme: Organic molecule & vitamins
• Temperature
– Too high or low temperature can denature
proteins
• Substrate concentration
• Enzyme concentration
89
• Inhibitors 90

Optimal conditions for enzyme Concentrations

• pH

• Temperature

91 92