Topic 3: Macromolecules
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3.1 Formation and Modification of
Biological Molecules
Carbon forms a great variety of chain and
ring structures that are the backbones of all
biological molecules
Collectively, most complex molecules based
on carbon are known as organic
molecules
All other substances are inorganic
molecules (including a few small carbon-
containing molecules that occur in the
environment, such as CO2)
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Hydrocarbons
Carbon has four unpaired outer electrons
The simplest hydrocarbon, CH4 (methane),
consists of a single carbon atom bonded to
four hydrogen atoms
More complex hydrocarbons involve two or
more carbon atoms arranged in a linear
unbranched chain, a linear branched chain,
or a structure with one or more rings
Single and double bonds are found in linear
and ring hydrocarbons; triple bonds only in
two-carbon hydrocarbons
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Functional Groups
Functional groups are small, reactive
groups of atoms which give larger molecules
specific chemical properties
Functional groups that enter most
frequently into biological reactions are the
hydroxyl, carbonyl, carboxyl, amino,
phosphate, and sulfhydryl groups
Functional groups are linked by covalent
bonds to other atoms in biological
molecules, usually carbon atoms –
represented
Phosphate byBrings
group: the collective symbol
energy to a R
molecule,
valence elections, and ATP, and its negative
charge
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Hydroxyl and Carbonyl Groups
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Carboxyl and Amino Groups
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Phosphate and Sulfhydryl Groups
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Isomers
Carbons that are linked to four different
atoms or functional groups are asymmetric
Can take either of two fixed positions with
respect to other carbons in a chain
The two forms (isomers) have the same
chemical formula, but have different
molecular structures
Example: In glyceraldehyde, the —H and —
OH groups can take either of two positions,
left or right of the carbon chain
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Types of Isomers
Isomers that are mirror images of each
other (such as glyceraldehyde) are called
stereoisomers
Typically only one of the two forms (L-form or
D-form) can enter into a reaction
Structural isomers are two molecules with
the same chemical formula but atoms are
arranged in different ways
Example: glucose, an aldehyde and fructose,
a ketone
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Stereoisomers
A
mi
no
aci
d
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LlLife recognizes
Leftsid Rightsi
e de
Amino Carbohydrat
acids es
Protei
ns
Structural Isomers
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Adding and Removing Water
In many reactions involving functional
groups, the components of a water molecule
(—H and —OH) are removed from or added
to the groups as they interact
When water components are removed, the
reaction is called a dehydration synthesis
reaction or condensation reaction
Coming together ; taking out water to
bring things together
When water components are added, the
reaction is calledBreaking bonds; using water to
hydrolysis
break things apart
Breaking down of food i.e the mouth
using saliva
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Dehydration Synthesis
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Hydrolysis
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Macromolecules
Carbohydrates, lipids, proteins, and nucleic
acids are large polymers, assembled from
subunit molecules (monomers) into a chain
by covalent bonds
Polymers are assembled from monomers
(polymerization) by dehydration synthesis
reactions
The breakdown of polymers into monomers
occurs by hydrolysis
Ca
rb
oh
yd
rat © 2017 Cengage Learning. All Rights
Macromolecules (cont'd.)
Each type of polymeric biological molecule
contains one type of monomer
Individual monomers may be identical, or
may have chemical variations, depending on
the molecule
A single polymer molecule with a mass of
1,000 daltons (Da) or more is called a
macromolecule
Includes many carbohydrates, proteins, and
nucleic acids
Lipids are not large enough to be classed as
Lip
macromolecules
ids
do
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3.2 Carbohydrates
Carbohydrates serve many functions
Energy-providing carbohydrates are stored in
plant cells as starch, and in animal cells as
glycogen
Structural carbohydrates include cellulose,
a primary component of plant cell walls
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Carbohydrates (cont'd.)
Carbohydrates contain only carbon,
hydrogen, and oxygen atoms in a ratio of
about 1C:2H:1O (CH2O)
Monosaccharides contain three to seven
carbon atoms
Two monosaccharides polymerize to form a
disaccharide
Carbohydrate polymers with more than 10
linked monosaccharide monomers are
polysaccharides
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Monosaccharides
Carbohydrates occur either as
monosaccharides or as polymers of
monosaccharide units
Monosaccharides (such as glucose, C6H12O6)
are soluble in water and sweet tasting
The most common monosaccharides contain
three carbons (trioses), five carbons
(pentoses), or six carbons (hexoses)
All monosaccharides can occur in linear
form
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Ring Forms
Monosaccharides with five or more carbons
(such as glucose) can fold back on
themselves through a reaction between two
functional groups to assume a ring form
Glucose exists as two different enantiomers
α-glucose, with an —OH group pointing
below the plane of the ring
β-glucose, with an —OH group pointing
above the plane
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C. Simplified ring
A. B. Formation
structure
Glucose of glucose
(linear rings
form)
D. Space-filling
model
Ring form induced when placed in
water
Disaccharides
Disaccharides are assembled from two
monosaccharides covalently joined by a
dehydration synthesis reaction
Example: Maltose is formed by a glycosidic
bond linking two α-glucose molecules with
oxygen as a bridge between the 1 carbon of
the first glucose and the 4 carbon of the
second glucose unit – an α (1→4) linkage
Other common disaccharides include sucrose
(glucose + fructose) and lactose (glucose +
galactose)
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Some Disaccharides
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Polysaccharides
The most common polysaccharides (plant
starches, glycogen, and cellulose) are
polymers of hundreds or thousands of
glucose units
Chitin is assembled from glucose units
modified by the addition of nitrogen-
containing groups
Polysaccharides may be linear, unbranched
molecules, or they may contain one or more
branches in which side chains of sugar units
Gl
ycare attached to a main chain
og
en
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C. Cellulose, the primary fiber in plant
cell walls
β(1
4)
linka
ge
Cellulose
molecule Cellulose
Glucose
microfibrils in
subunit
plant cell wall
Cellulose
microfibril
D. Chitin, a reinforcing fiber in the external skeleton of
arthropods and the cell walls of some fungi
β(1
4)
linka
ge
3.3 Lipids
Lipids are water-insoluble, primarily
nonpolar biological molecules composed
mostly of hydrocarbons
Three common types of lipid molecules:
Neutral lipids are stored and used as an
energy source
Phospholipids form cell membranesAd
de
Steroids serve as hormones that regulate
d
cellular activities ph
os
ph
at
e
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Neutral Lipids
Neutral lipids, found in cells as energy-
storage molecules, have no charged groups
(nonpolar)
There are two types of neutral lipids:
Oils are liquid at biological temperatures
Fats are semisolid
A fatty acid contains a single hydrocarbon
chain with a carboxyl group (—COOH) at
one end
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Glycerol and Triglyceride Formation
Triglycerides form by dehydration synthesis
between three-carbon glycerol (an alcohol)
and three fatty acid side chains
A covalent bond (ester linkage) forms
between the -COOH group of the fatty acid
and the -OH group of the glycerol
The polar groups of glycerol are eliminated,
forming a nonpolar triglyceride
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Triglycerides
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Saturated and Unsaturated Fatty Acids
The most common fatty acids have chains
of 14 to 22 carbons
As chain length increases, fatty acids
become less water-soluble and more oily
A saturated fatty acid binds the maximum
number of hydrogen atoms
Only single bonds exist between carbon
atoms
Fatty acids with one double bond are
monounsaturated; those with more than
on double bond are polyunsaturated
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Saturated and Unsaturated Fatty Acids
(cont'd.)
Unsaturated fatty acids (such as vegetable
oils) bend at a double bond and are more
fluid at biological temperatures
Saturated fatty acids are found in solid
animal fats such as butter
Unsaturated fats are considered healthier
than saturated fats in the human diet
Plant oils are converted commercially to
saturated fats by hydrogenation
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Fatty Acids
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Functions of Triglycerides
Triglycerides serve as energy reserves in
animals
Store more than twice the calories per gram
as carbohydrates
A layer of fatty tissue just under the skin
acts as insulation in mammals and birds
(e.g., penguins)
Triglycerides also help make bird feathers
waterproof
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Focus on Research
Atherosclerosis occurs
from the build up of
plaques in the coronary
arteries
Plaques form from the
buildup of excess
cholesterol
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Waxes
Fatty acids combine with long-chain alcohols
or hydrocarbon structures to form waxes,
which are harder and less greasy than fats
Waxy coatings help animals keep skin, hair,
or feathers protected, lubricated, and pliable
Plants secrete waxes that form a protective
exterior layer, which reduces water loss and
resists infective agents
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Phospholipids
Phosphate-containing phospholipids are
the primary lipids of cell membranes
The most common phospholipid has a
glycerol backbone linked to two fatty acid
chains and a polar phosphate group, which
is linked to another polar group
The end of the molecule containing the fatty
acids is nonpolar and hydrophobic, and the
end with the phosphate group is polar and
hydrophilic
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Phospholipid Bilayer
In watery environments, only the polar ends
of phospholipid molecules are exposed to
water; their nonpolar ends collect together
in a region that excludes water
The phospholipid bilayer – a film of
phospholipids two molecules thick – is the
structural basis of membranes
In a bilayer, the polar groups face the
surrounding water molecules at the surfaces
of the bilayer – the hydrocarbon chains form
a nonpolar, hydrophobic region in the interior
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Phospholipid Structure
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Steroids
Steroids are lipids with structures based on
a framework of four carbon rings
Sterols, the most common steroids, have a
single polar OH group linked to one end of
the ring framework and a complex, nonpolar
hydrocarbon chain at the other end
Cholesterol is an important component of
animal cell membranes
Similar sterols (phytosterols) occur in plant
cell membranes
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Steroids
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Steroid Hormones
Steroid hormones control development,
behavior, and many internal biochemical
processes
Examples: The sex hormones that control
differentiation of the sexes and sexual
behavior
Estradiol (female sex hormone) has an —
OH in the position where testosterone
(male sex hormone) has an =O, and
testosterone has a methyl group (—CH 3)
that is absent from estradiol
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Steroid Sex Hormones
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Other Lipids
Several other lipid types have structures
unrelated to triglycerides, phospholipids, or
steroids
Chlorophylls and carotenoids are pigments
that absorb light and help convert it to
chemical energy in plants
Lipid groups combine with carbohydrates to
form glycolipids, and with proteins to form
lipoproteins, which have important structural
and functional roles in cell membranes
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3.4 Proteins
Proteins perform many vital functions in
living organisms
Structural support; enzymes; movement;
transport; recognition and receptor
molecules; regulation of proteins and DNA;
hormones; antibodies; toxins and venoms
Proteins are macromolecules
Polymers of amino acid monomers, which
contain both an amino and a carboxyl group
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Amino Acids
All organisms use 20 different amino acids
to build proteins
Most have the same structural plan: a
central carbon atom is attached to an amino
group, a carboxyl group, a hydrogen atom,
and a variable R group
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Amino Acids (cont'd.)
One amino acid, proline, differs slightly in
that it has a ring structure that includes the
central carbon atom – the central carbon
bonds to a —COOH group on one side and
to an =NH (imino) group at the other side
All amino acids can act as acids or bases
The amino group can produce a basic
reaction by accepting H+, or the carboxyl
group can produce an acidic reaction by
releasing H+
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Amino Acids (cont'd.)
Some side groups are polar and some are
nonpolar
Among the polar side groups, some carry a
positive or negative charge and some act as
acids or bases
Many side groups contain reactive
functional groups, such as —NH2, —OH, —
COOH, or —SH, which interact with other
atoms in the same protein or outside the
protein
Sulfhydryl groups (in cysteines) can produce
disulfide linkages (—S—S—) that help hold
proteins in their 3-D shape
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Nonpolar Amino Acids
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Uncharged Polar Amino Acids
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Negatively Charged Amino Acids
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Positively Charged Amino Acids
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Rights 3-
A Disulfide Linkage
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Peptide Bonds
Covalent peptide bonds link amino acids
into polypeptide chains – the subunits of
proteins
A peptide bond is formed by a dehydration
synthesis reaction between the —NH 2 group
of one amino acid and the —COOH group of
another amino acid
The growing polypeptide chain has an N-
terminal end and a C-terminal end
New amino acids are linked only to the C-
terminal end
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A Peptide Bond
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Four Levels of Protein Structure
Primary structure is the unique sequence
of amino acids forming a polypeptide
Secondary structure is produced by the
twists and turns of the amino acid chain
Tertiary structure is the folding of the
amino acid chain, with its secondary
structures, into the overall 3-D shape of a
protein
Quaternary structure, when present, is
formed from more than one polypeptide
chain
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Protein Structure
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Primary Structure
Primary structure of a protein is the precise
sequence in which amino acids are linked
Changing even a single amino acid alters
secondary, tertiary, and quaternary
structures – which can alter or destroy the
biological function of a protein
Example: Substitution of a single amino acid
in hemoglobin produces an altered form
responsible for sickle-cell disease
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Secondary Structure
The amino acid chain (primary structure) is
folded into arrangements that form the
protein’s secondary structure
The alpha (α) helix is twisted into a regular
right-hand spiral
The beta (β) strand zigzags in a flat plane,
forming a sheet
Most proteins have segments of both
arrangements
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An α Helix
Amino acid side
groups extend
outward from the
twisted backbone
Stabilized by
regularly spaced
hydrogen bonds
Forms rigid, rod-like
structures
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A β Sheet
The amino acid chain
zigzags in a flat
plane
β strands are aligned
side by side in the
same or opposite
directions
Hydrogen bonds
stabilize the sheet
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The Random Coil
A random coil has an irregularly folded
arrangement
Segments of random coil provide flexible
sites that allow α-helical or β-strand
segments to bend or fold back on
themselves
Segments of random coil act as “hinges”
that allow major parts of proteins to move
with respect to one another
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Tertiary Structure
Tertiary structure gives a protein its overall
three-dimensional shape, or conformation
The positions of secondary structures,
disulfide linkages, and hydrogen bonds play
major roles in folding each protein into its
tertiary structure
Attractions between positively and
negatively charged side groups and polar or
nonpolar associations also contribute to
tertiary structure
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Tertiary Structure of Lysozyme
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Chaperonins
Proteins fold gradually as they are
assembled – as successive amino acids are
linked into the primary structure, the chain
folds into increasingly complex structures
For many proteins, “guide” proteins called
chaperone proteins or chaperonins bind
temporarily with newly synthesized
proteins, directing their conformation
toward the correct tertiary structure and
inhibiting incorrect arrangements
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Role of a Chaperonin
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Tertiary Structure (cont'd.)
Tertiary structure determines a protein’s
function
The distribution and 3-D arrangement of
side groups, in combination with their
chemical properties, determine the overall
chemical activity of the protein
Tertiary structure also determines the
solubility of a protein, depending on the
arrangement of polar (hydrophilic) and
nonpolar (hydrophobic) segments
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Tertiary Structure (cont'd.)
Tertiary structure of most proteins is flexible,
allowing them to undergo limited
conformational changes
Conformational changes are important to the
function of enzymes, and to proteins
involved in cellular movements or transport
of substances across cell membranes
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Quaternary Structure
Some complex proteins, such as hemoglobin
and antibody molecules, have quaternary
structure – the presence and arrangement
of two or more polypeptide chains
Hydrogen bonds, polar and nonpolar
attractions, and disulfide linkages hold the
multiple polypeptide chains together
Chaperonins promote correct association of
the individual amino acid chains and inhibit
incorrect formations
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Functional Domains
In many proteins, folding of the amino acid
chain (or chains) produces large
subdivisions called domains
In proteins with multiple functions,
individual functions are often located in
different domains
Domains with similar functions are found in
different proteins
3-D arrangement of amino acid chains
within and between domains produces
highly specialized regions called motifs
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Two Domains in an Enzyme
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Domain Surfaces
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Protein Combinations
Proteins link with lipids to form lipoproteins,
which form parts of cell membranes
Proteins link with carbohydrates to form
glycoproteins, which function as enzymes,
antibodies, recognition and receptor
molecules, and parts of extracellular
supports
Proteins link with nucleic acids to form
nucleoproteins, which form structures such
as chromosomes
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3.5 Nucleotides and Nucleic Acids
Nucleic acids are macromolecules
assembled from repeating monomers called
nucleotides
DNA (deoxyribonucleic acid) stores
hereditary information responsible for
inherited traits in all eukaryotes and
prokaryotes and in a large group of viruses
RNA (ribonucleic acid) is the hereditary
molecule of another large group of viruses –
three major types of RNA are involved in
protein synthesis
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Nucleotides
A nucleotide, the monomer of nucleic
acids, consists of three parts linked together
by covalent bonds:
A nitrogenous base formed from rings of
carbon and nitrogen atoms
A five-carbon, ring-shaped sugar
One to three phosphate groups
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Nucleotide Structure
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Nucleotide Structure
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Nitrogenous Bases
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Ring-shaped Sugars
Nitrogenous bases link covalently to a five-
carbon sugar:
Deoxyribose in DNA
deoxyribonucleotides
Ribose in RNA ribonucleotides
The two sugars differ only in the chemical
group bound to the 2′ carbon (—H in
deoxyribose, —OH in ribose)
In unlinked nucleotides: 1, 2, or 3 phosphate
groups bond to the ribose or deoxyribose
sugar at the 5′ carbon
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Nucleosides and Nucleotide Phosphates
A structure containing only a nitrogenous
base and a five-carbon sugar is a
nucleoside
A nucleotide is a nucleoside phosphate
Examples:
Adenosine monophosphate (AMP)
Adenosine diphosphate (ADP)
Adenosine triphosphate (ATP)
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DNA and RNA
DNA and RNA consist of polynucleotide
chains, with one nucleotide linked to the
next by a phosphodiester bond
One nucleotide is linked to the next by a
bridging phosphate group between the 5′
carbon of one sugar and the 3′ carbon of the
next sugar
Alternating sugar and phosphate groups
forms the backbone of a nucleic acid chain
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DNA and RNA
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The DNA Double Helix
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DNA Base Pairs
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RNA Molecules
RNA molecules exist mainly as single
polynucleotide chains (single-stranded) –
however, RNA molecules can fold back on
themselves to form double-helical regions
In RNA, the uracil (U) base takes the place of
thymine (T), forming A–U base pairs
“Hybrid” double helices (an RNA chain
paired with a DNA chain) are formed
temporarily when RNA copies DNA
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