Macromolecules

Carbohydrates, Lipids,
Proteins and Nucleic Acids
Essential idea: Compounds of carbon,
hydrogen and oxygen are used to
supply and store energy.
Understandings:
• Monosaccharide monomers are linked together by condensation reactions to
form disaccharides and polysaccharide polymers.
• Fatty acids can be saturated, monounsaturated or polyunsaturated.
• Unsaturated fatty acids can be cis or trans isomers.
• Triglycerides are formed by condensation from three fatty acids and one glycerol.
Applications and skills:
• Application: Structure and function of cellulose and starch in plants and
glycogen in humans.
• Application: Scientific evidence for health risks of trans fats and saturated
fatty acids.
• Application: Lipids are more suitable for long-term energy storage in humans
than carbohydrates.
• Application: Evaluation of evidence and the methods used to obtain the
evidence for health claims made about lipids.
• Skill: Use of molecular visualization software to compare cellulose, starch and
glycogen.
• Skill: Determination of body mass index by calculation or use of a nomogram.
Essential idea: Proteins have a very wide range of functions in
living organisms.

Understandings:
• Amino acids are linked together by condensation to form polypeptides.
• There are 20 different amino acids in polypeptides synthesized on ribosomes.
• Amino acids can be linked together in any sequence giving a huge range of
possible polypeptides.
• The amino acid sequence of polypeptides is coded for by genes.
• A protein may consist of a single polypeptide or more than one polypeptide
linked together.
• The amino acid sequence determines the three-dimensional conformation of
a protein.
• Living organisms synthesize many different proteins with a wide range of
functions.
• Every individual has a unique proteome.
Applications and skills:
• Application: Rubisco, insulin, immunoglobulins, rhodopsin, collagen and
spider silk as examples of the range of protein functions.
• Application: Denaturation of proteins by heat or by deviation of pH from the
optimum.
• Skill: Drawing molecular diagrams to show the formation of a peptide bond.
Essential idea: The structure of DNA allows efficient storage of
genetic information

Understandings:
• The nucleic acids DNA and RNA are polymers of nucleotides.
• DNA differs from RNA in the number of strands present, the base
composition and the type of pentose.
• DNA is a double helix made of two antiparallel strands of nucleotides
linked by hydrogen bonding between complementary base pairs.
Applications and skills:
• Application: Crick and Watson’s elucidation of the structure of DNA using
model making.
• Skill: Drawing simple diagrams of the structure of single nucleotides of
DNA and RNA, using circles, pentagons and rectangles to represent
phosphates, pentoses and bases.
 CARBON
• Tetravalent  4 different bonds
• Forms long chains (polymers) 
macromolecules and ring structures
• Isomerism  structural and optical isomers
 Organic compounds
• Compounds containing carbon found in living
organisms
• Not including carbonates, hydrogen
carbonates, CO2 ,CO, HCO3
• There are four major groups:
– Sugars (Carbohydrates)
– Fatty acids ( Lipids)
– Amino acids ( Proteins)
– Nucleotides (Nucleic acids)
 Functional Groups
Structural
Group Found in
Formula
Functional groups have definite Carbohydrates,
Hydroxyl OH alcohols
chemical properties that they retain
not matter where they occur. C
Carbonyl Formaldehyde
These functional groups determine O
the characteristics and chemical O
reactivity of molecules. For example: Amino acids,
Carboxyl C vinegar
OH
Amino groups make a molecule
more basic. H
Amino N Ammonia
Carboxyl groups make a
H
molecule more acidic.
Proteins,
Sulfhydryl S H rubber

O–
Phospholipids,
Phosphate O P O– nucleic acids,
ATP
O
 Carbohydrates
Carbohydrates are a family of organic molecules made up of
Carbon, Hydrogen, and Oxygen atoms. Some are small, simple
molecules, while others form long polymers.
Carbohydrates have the general formula (CH2O).
Simple carbohydrates are generally
called sugars.The most common Ribose
arrangements found in sugars are:
Pentose, a five C sugar,
e.g. Ribose and Deoxyribose.
6

Hexose, a six C sugar,

e.g. Glucose and Fructose. Glucose 1
A structural formula and 4

symbolic form are shown.

In solution, these naturally form rings rather than straight chain structures.
 Functions of Carbohydrates
• Provide energy source: A fuel source when catabolized
during cellular respiration. Energy is stored in the chemical
bonds within the molecule and released during cellular
respiration. Usually simple sugars.

• Provide energy storage: Plants store energy in a complex

carbohydrate form called Starch (amylose) . Animals store
energy in a complex carbohydrate in their muscle tissue and
liver in the called Glycogen.

• Structural Building Material: Plants build their cell walls of a

complex carbohydrate material called Cellulose. Animals
such as arthropods build their exoskeletons of a complex
carbohydrate called Chitin. Chitin is also found in the cell
walls of Fungi.
 Classification of Carbohydrates

Carbohydrates

Monosaccharides Disaccharides Polysaccharides

- Glucose - Lactose - Starch
- Galactose - Maltose - Glycogen
- Fructose - Sucrose - Cellulose
 Monosaccharides

Monosaccharides are used as a

primary energy source for fueling
cellular metabolism.
Monosaccharides are single-sugar
molecules. They include:
Glucose (grape sugar and
blood sugar).
Galactose Glucose is a monosaccharide sugar.
It occurs in two forms, the L- and D-
Fructose (honey and fruit forms. The D-glucose molecule
juices). (above) can be utilized by cells while
the L-form cannot.
Monosaccharides
Carbohydrate Isomers α-glucose

Compounds with the same chemical

formula can have different arrangement of
atoms are called Isomers.
Structural isomers have the atoms linked in
a different sequence from one another.
β-glucose
α glucose polymers form starch.
β glucose polymers form cellulose.
These molecules have very
different properties.
Optical isomers are identical in every way The α and β glucose molecules, are
but are mirror images of each other. examples of structural isomers.
They contain the same atoms but the
hydroxyl groups are linked to the C1
atom differently.
 Disaccharides
Disaccharides are double-sugar molecules joined with a
glycosidic bond.
Disaccharides provide a convenient way to transport glucose.

The type of disaccharide formed depends on the monomers

(single units)involved and whether they are in their α- or β-
form.
Condensation & Hydrolysis
Carbohydrate Carbohydrate
condensation hydrolysis
(Dehydration
synthesis) • Compound sugars can be
broken down into their
• Monosaccharides are joined constituent
together to form disaccharides monosaccharides.
and polysaccharides.
• A water molecule provides
• Water is released in the the hydrogen and hydroxyl
process. groups required.
• Energy is supplied by a • The reaction is catalyzed by
nucleotide sugar such as ADP- enzymes.
glucose.

hydrolysis

O
condensation
Condensation & Hydrolysis
2 monosaccharides

Condensation Hydrolysis
reaction reaction

H2O

Disaccharide + H2O
O

Glycosidic bond
 Condensation & Hydrolysis
2 α-glucose
molecules

Condensation Hydrolysis

H2O

Maltose
molecule

Glycosidic bond
 Disaccharides
Sucrose
Components: α-glucose + β-
fructose
Source: A simple sugar found in
plant sap.
Maltose
Components: α-glucose + α-
glucose
Source: Maltose is a product
of starch hydrolysis and is
found in germinating grains.
Lactose
Components: β-glucose + β-
galactose
Source: Milk
 Polysaccharides - Cellulose
Cellulose is a glucose polymer. It is an important Glucose monomer
structural material found in plants.
It is made up of many unbranched
chains of β-glucose molecules
held together by 1, 4 glycosidic links. 1,4 glycosidic bonds
create unbranched
Parallel chains are cross-linked by hydrogen chains
bonds to form bundles called microfibrils.
– Cellulose microfibrils are very strong.
– They form a major structural component
of plant cells, e.g. in the cell wall.

Cellulose is repeating chains

of β-glucose molecules.
 Polysaccharides - Starch
Starch is a polymer of glucose, made up of long
1,6 glycosidic
chains of α-glucose molecules.
1 1 bonds create
4 branched
Starch contains a mixture of: 6
chains
–
1
25-30% amylose: long unbranched 4
chains of many hundreds of glucose 6

linked by 1-4 glycosidic bonds. 1

4

– 70-75% amylopectin: branched chains Starch granules

with 1-6 glycosidic bonds every 23-30
glucose units.

Starch is an energy storage molecule in plants.

– It is found concentrated in insoluble
starch granules within plant cells.

Photo: Brian Finerran

Starch can be easily hydrolyzed to glucose when
required.
 Polysaccharides - Glycogen
It is composed of α-glucose
molecules, but there are more
1,6 glycosidic links mixed with 1,6 bonds
the 1,4 glycosidic links.
Glycogen is the energy storage
compound in animal tissues
and in many fungi.
It is more water soluble than
starch and is found mainly in
liver and muscle cells, which
are both centers of high
metabolic activity.
Glycogen is readily hydrolyzed
by enzymes to release glucose.

Glycogen is abundant in metabolically active tissues such as

liver (left) and skeletal muscle (right). The glycogen stains
dark magenta.
 Modified Polysaccharides
Nitrogen containing NHCOCH3 NHCOCH3
6 6
group on each glucose
O O O O
5 3 2 5 3 2

4 1 4 1 4 1 4 1

3 2 5 O 3 2 5
O O

NHCOCH3 6 NHCOCH3 6

Chitin is a tough modified polysaccharide made up

of chains of β-glucose molecules.
It is found in the cell walls of fungi and it is an
essential component of the arthropod
exoskeleton.

The exoskeleton of an
insect is made of
chitin
 Lipids
Lipids are a group of organic compounds with an oily, greasy, or waxy consistency.

Like carbohydrates, lipids contain carbon, hydrogen, and oxygen, but in lipids, the proportion
of oxygen is much smaller.

They are relatively insoluble in water and tend to be hydrophobic (water repellent).

Lipids are soluble in organic solvents such as ethanol and ether.

Typical lipids, e.g. neutral fats, consist of fatty acids and glycerol (below).

H O

H C OH OH C CH2 CH2 CH2 CH2 CH2 CH2 CH2 CH2 CH2 CH2 CH2 CH2 CH2 CH2 CH2 CH2 CH2
O

H C OH OH C CH2 CH2 CH2 CH2 CH2 CH2 CH2 CH2 CH2 CH2 CH2 CH2 CH2 CH2 CH2 CH2 CH2
O
H C OH OH C CH2 CH2 CH2 CH2 CH2 CH2 CH2 CH2 CH2 CH2 CH2 CH2 CH2 CH2 CH2 CH2 CH2

Glycerol Three fatty acids

 Lipids
Lipids have many roles, including as:
– biological fuels
– hormones Plasma membrane

– structural components of
membranes
Phospholipids are the primary structural
Fats provide twice as much energy as component of all cellular membranes, such as
carbohydrates. the plasma membrane (false color TEM
above).
Proteins and carbohydrates can be

Dept. Biological Sciences, University of Delaware

converted into fats stored in adipose
tissue. Fat cell

Capillary

Lipids are often stored in special

adipose tissue, within large fat cells
(above).
 Biological Roles of Lipids
Mitochondri
on (false
color TEM)

Lipids are concentrated

sources of energy and
can be broken down Phospholipids form the
Waxes and oils, when structural framework of
(through fatty acid
secreted on to surfaces cellular membranes,
oxidation in the
provide waterproofing e.g. the plasma
mitochondria) to provide
in plants and animals. membrane (above).
fuel for aerobic
respiration
 Biological Roles of Lipids

The white fat tissue (arrows)

is visible in this ox kidney

Fat absorbs shocks

(Cushioning). Organs
that are prone to
bumps and shocks
(e.g. kidneys) are Lipids are a source of
cushioned with a metabolic water. During
relatively thick layer of respiration, stored lipids Stored lipids provide
fat. are metabolized for energy, insulation in extreme
producing water and environments.
carbon dioxide. Increased body fat
levels in winter reduce
heat losses to the
environment.
 Triglycerides
The most common lipids in living things are the neutral fats.
They make up the fats and oils found in plants and animals.

A triglyceride is composed of an alcohol called glycerol

covalently bonded to three fatty acid molecules by dehydration
synthesis reactions.
Globules of fat or oil are
Water is lost to compact and relatively inert
form an ester
bond
H O
H C OH OH C CH2 CH2 CH2 CH2 CH2 CH2 CH2 CH2 CH2 CH2 CH2 CH2 CH2 CH2 CH2 CH2 CH3

O
H C OH OH C CH2 CH2 CH2 CH2 CH2 CH2 CH2 CH2 CH2 CH2 CH2 CH2 CH2 CH2 CH2 CH2 CH3

O
H C OH OH C CH2 CH2 CH2 CH2 CH2 CH2 CH2 CH2 CH2 CH2 CH2 CH2 CH2 CH2 CH2 CH2 CH3

H
Glycerol Three fatty acids
 Fats and Oils
Oils are liquid at
The difference between fats and room temperature,
while fats are solid
oils is their physical state at 20°C.
• Fats are solid at 20°C.
• Oils are liquid at 20°C

These differences in the physical properties of fats and oils are a

result of the type of fatty acid attached to the glycerol molecule.
•Some are saturated fatty acids, with a maximum number of hydrogen atoms.
•Some are unsaturated, with double bonds and fewer hydrogen atoms.
 Saturated Fatty Acids
Saturated fatty acids contain the maximum number of
hydrogen atoms. They do not contain any double bonds or
other functional groups along the chain.
• Saturated fatty acids form straight chains.
• Lipids containing a high proportion of saturated fatty
acids tend to be solids at room temperature, i.e. fats,
such as butter and lard.

O H H H H H H H H H H H H H H H
HO C C C C C C C C C C C C C C C C H

H H H H H H H H H H H H H H H
 Unsaturated Fatty Acids
Unsaturated fatty acids contain some carbon atoms that are
double-bonded with each other (all of the spaces are not taken
by hydrogen atoms).
Lipids with a high proportion of unsaturated fatty acids are oils
and tend to be liquid at room temperature.
• The unsaturated nature causes kinks in the straight
chains. When aligned in a lipid molecule, the kinked fatty
acids do not pack in closely together; hence the more
fluid structure of oils.

Kink
O H H H H H H H H H H H H H H H H H H
HO C C C C C C C C C C C C C C C C C C C H
H H H H H H H H H H H H H H
 Cis/Trans Fatty Acids

While a saturated fatty acid is a straight molecule on the

average, the double bond in an unsaturated fatty acid
produces a kink in the molecule.

This because a double bond cannot rotate. The bend in the

carbon chain, however, is much more pronounced in the cis
isomer compared to the trans isomer.

For this reason, cis fatty acids (and triacylglycerols made from
them) do not solidify as readily as trans fatty acids. Due to the
larger bend, the cis isomers cannot line up next to one
another in as ordered a fashion as the trans isomers.
Cis/Trans Fatty Acids
 Cis/Trans Fatty Acids

While trans fatty acids are uncommon in natural fatty acids,

they form readily when polyunsaturated fatty acids from
plants are "partially hydrogenated" chemically.

This is done
commercially to make
plant fatty acids more
solid and to improve
self-life.
Epidemiological studies
correlate consumption
of trans fatty acids with
increased risk of heart
disease.
 Phospholipids
If one of the fatty acid groups of a triacylglyerol is replaced by a phosphate
group, the the molecule is known as a phospholipid. A phospholipid consists
of:
– a glycerol molecule
– two fatty acid chains
– a phosphate (PO43-) group (ionised under the conditions in cells)
Nonpolar,
H2C COO hydrocarbon
tails of two
HC COO fatty acids
O– condensed
with glycerol
H2C O P O–
O Fatty acid
Glycero

Fatty acid
l

Phosphate group from

phosphoric acid (HPO4) Symbolic
PO43-
condenses with the third - representation of a
OH of glycerol phospholipid
Phospholipid Structure
 Phospholipids
The phosphate end of the molecule is polar and attracted to water (hydrophilic)
while the fatty acid end is non-polar and is repelled (hydrophobic).

As a result, phospholipids naturally form a bilayer with the hydrophobic ends

orientated inwards.

The phospholipid bilayer forms the main component of cellular membranes.

Glycerol and
phosphate ‘head’: the
hydrophilic part of the
molecule

Hydrocarbon tail:
hydrophobic part
of the molecule.
 Steroids The basic structure of a
steroid(shown symbolically
above) is three six carbon atom
rings, and one five carbon atom
Steroids are classified as lipids, but their structure ring.

is quite different from that of other lipids.

The basic structure of a steroids is:

– three 6 carbon atom rings
– one 5 carbon atom ring.

Steroid sex hormones are

Examples of steroids include: responsible for both primary and
– sex hormones (testosterone and estrogen) secondary sexual characteristics
in males and females.
– hormones such as cortisol and aldosterone
– cholesterol is a sterol lipid and is a
precursor to several steroid hormones.
 Lipid Condensation Water is lost to form
an ester bond

Triacylglycerols (also called H O

triglycerides) form when H C O H OH C CH2 CH2 CH2.............CH3

glycerol bonds with three fatty O

acids. H C O H + OH C CH2 CH2 CH2.............CH3
O
Glycerol is an alcohol
H C H OH CH2 CH2 CH2.............CH3
containing three carbons. O C

H
– Each carbon is bonded to
Glycerol Three fatty acids
a hydroxyl (–OH) group.
H
When glycerol bonds with the O
fatty acid, an ester bond is H C O C CH2 CH2 CH2.............CH3 + H2O
formed and water is released. O
H C O C CH2 CH2 CH2.............CH3
Three separate condensation + H2O
O
reactions are involved in
H C O CH2 CH2 CH2.............CH3 + H2O
producing a triglyceride. C
H
Triacylglycerol (triglyceride) Water
 Proteins
Proteins are macromolecules, consisting of many amino acids
linked together as polypeptide chains.
Each cell contains several hundred to several thousand proteins.
Proteins play a key role in the body. They are involved in:
– Enzyme reactions
– Oxidation-reductions, e.g. respiratory chain
– Structure
– Storage
– Transport
– Cell signaling
– Defense
Human Cytochrome C
Insulin-like growth factor 1 (respiratory chain)
(used in cell signaling)
 Amino Acids
Amino acids are the basic units
from which proteins are made. Plants can manufacture all the
amino acids they require, but
animals must obtain a certain
number of ready-made essential
amino acids from their diet.

All other amino acids can be

constructed from these essential
The order in which the different amino acids.
amino acids are linked together to
form proteins is controlled by genes
on the chromosomes.
Tyr Ser
Glu Iso
Amino acids link Phe
together (right) to Met
Ala
form proteins. Ala Ser
 Amino Acids
There are approximately 20 The “R” group varies in
different amino acids found in chemical make-up with
each type of amino acid
proteins.
All amino acids have a common Carbon
R
structure: atom

The ‘R’ group is variable,

which means that it is
different in each amino NH2 C COOH
acid.
The ‘R’ groups of amino
Amine
acids can have quite group H Carboxyl group
makes the molecule
diverse chemical behave like a weak
properties. acid
Hydrogen
atom
 Amino Acids
This “R” group gives
the amino acid
This “R” group can form alkaline properties.
This “R” group
disulfide bridges with other
gives the amino
cysteines to create cross
acid acidic
linkages in a polypeptide
properties.
chain.
NH2
CH2
CH2
SH CH2 COOH
CH2 CH2 CH2

NH2 C COOH NH2 C COOH NH2 C COOH

H H H

Cysteine Lysine Aspartic acid

Amino Acid Variety
 Polypeptides

A polypeptide chain is formed when amino acids are linked

together via peptide bonds to form long chains.
– The process of joining amino acids is called condensation.
– A polypeptide chain may contain several hundred amino acids.
– A polypeptide chain may be functional by itself, or may need to be
joined to other polypeptide chains to become functional.

Peptide Peptide Peptide Peptide

bond bond bond bond
Condensation & Hydrolysis
Two amino
Condensation acids

– Amino acids are joined

together to form peptide
or polypeptide chains.
– A water molecule is

Condensation

Hydrolysis
released.
Hydrolysis
– Polypeptide chains are H2O
broken down into smaller
peptide chains or simple
amino acids. Peptide
bond
– A water molecule provides
a hydrogen and hydroxyl
group.
Dipeptide + H2O
 Condensation & Hydrolysis
R R
H O H O
Two
amino N C C N C C
acids
H OH H OH
H H

Condensation Hydrolysis

R O H R O
Dipeptide +
H
water N C C N C C + H2O
H
H OH
Peptide Bond
H
 Protein Structure
The conformation (or shape) a protein takes is
dependent upon the protein’s amino acid sequence.
The “R” groups of each amino acid react and
interact with each other. These interactions
determine the final conformation of the Lysozyme is a single
protein. polypeptide strand of 129 amino
acids and a tertiary structure
A protein’s conformation is central to its function.If the which is part α-helix, part β-
sheet and part irregular
shape is altered then the protein may no longer be sections.
able to perform its biological role.
Proteins have up to four levels of structure:
– primary: the linking of amino acids in the
polypeptide chain.
– secondary: the shape of the polypeptide chain
– tertiary: the fold of the polypeptide chain
Hemoglobin has a
– quaternary: the interaction of two or more complex quaternary
polypeptide chains structure with four
 Proteins: Phe
Glu

Primary Structure Tyr

Ser

The primary (1°) protein structure is Iso

the amino acid sequence, type , and
number.
Phe
Hundreds of amino acids link
together to form polypeptide Ala
chains.
The chemical interaction (attraction Glu
and repulsion) of the individual
Met Gly
amino acids helps define the final
protein shape.
Ala
When amino acids are
linked together they Ala
form a polypeptide
chain.
 Proteins:
Primary Structure
- -
+ +
+
+ - - +
- +
+ -
-
+ - + -
polar
+
+ - polar
- polar
+
- +
polar
-
 Example of Modification in Levels
of Protein Structure
Sickle-cell anemia is due to a
change in protein structure
at the primary level. Once
the change is made at the
primary level it has an effect
on all subsequent levels.
Resulting the formation or
irregular hemoglobin protein
that cause the molecule to
take on an irregular form
which in turns affects its
normal function and the
shape of the erythrocytes
(red blood cells).
 Proteins:
Secondary Structure
The secondary (2°) structure is the
shape of the polypeptides chain.
There are two common types of
secondary structure:
– α-helix coil
– β-pleated sheets
Most proteins, e.g. lysozyme,
contain a mixture of the two
secondary structures, but the levels
of each vary.
Secondary structures are a result of
hydrogen bond interaction
between neighboring CO and NH
groups of the polypeptide
backbone.
 Proteins:
Tertiary Structure
The tertiary (3°) structure of a protein is
the way in which it is folded (called its
fold).
The protein folds because of
interactions between the “R” groups, or
side chains on the amino acids. Several
interactions
may be involved:
–Disulfide (the strongest links)
– Weak bonding (ionic and
hydrogen).
– Hydrophobic interactions.
 Proteins:
Quaternary Structure
Some proteins contain more than one polypeptide chain.
– The polypeptide chains, or subunits, aggregate together
to become a functional unit.
– The aggregation of subunits is called the quaternary (4°)
structure of a protein.
Alpha chain Beta chain

The hemoglobin molecule

has four subunits: two alpha
chains and two beta chains.
At the core of each subunit is
an iron containing heme
group, which binds oxygen.

Heme group
 Protein Structure: 1°
Ser

Overview
Tyr Glu

Iso Ala Gly

Glu
Phe
Met
Phe
There are four levels of protein structure: Ala

– Primary structure (1°): The sequence of Ala

amino acids in a polypeptide chain.

2°
– Secondary structure (2°): The shape of
the polypeptide chain (e.g. alpha-helix).
– Tertiary structure (3°): The overall
conformation (shape) of the
polypeptide caused by folding.
– Quaternary structure (4°): The 3°
association of multiple subunits of
polypeptide chains.

4°
 Protein Denaturation

Protein denaturation refers to the loss of a

protein’s three-dimensional structure.
– It occurs because the bonds responsible for
maintaining protein structure are altered.
– It usually results in loss of function.
– It is often irreversible.
• Cooking food denatures protein and makes it Reversible protein
denaturation is
easier to digest.
responsible for the
• Alcohols disinfect by denaturing bacterial and “perm”.
viral proteins. Disulfide linkages are
responsible for keratin’s
• Reversible denaturation is involved in waving tertiary structure. These
hair. The keratin protein in hair is denatured are broken and then reset
using a reducing agent, "glued" back into during the chemical
disulfide bridges by an oxidizing agent (H2O2). process of perming.
 Protein Denaturation
Agents that cause protein denaturation are:
Strong acids and alkalis. Heavy metals.
These disrupt ionic bonds and These may disrupt ionic
result in coagulation of the bonds and form strong bonds with
protein. Long exposure can also the carboxyl groups of the R groups
break down the primary structure and reduce the protein charge. This
of the protein. results in protein precipitation.
Heat and radiation.
These cause disruption of the Detergents and solvents.
bonds in the protein through These form bonds with the non-polar
increased energy provided to groups in the protein, thereby
the atoms. disrupting hydrogen bonding.
 Categorizing Proteins
Proteins can be categorized according
to their tertiary structure:
Fibers form due
Globular proteins to cross links
between
α-chain
Fibrous proteins collagen
molecules

disulfide ϐ-chain
bond Collagen is an example of a fibrous
Bovine insulin is an example of a protein. It consists of three helical
small globular protein. It consists of polypeptide chains wound around each
two chains held together by disulfide other. Hydrogen bonding between glycine
bridges between neighboring residues holds these chains together.
cysteine (Cys) molecules.
 Globular Proteins
Globular proteins are very diverse in their subunit
structure.
subunit
– They can exist as single chains or
comprise several chains, as occurs in
hemoglobin and insulin. subunit

Properties of globular proteins:

subunit
– Easily soluble in water
– Tertiary structure is critical to function
– Polypeptide chains are folded into a
spherical shape Hemoglobin is a globular protein. Its
heme (iron containing) groups bind
Functions of globular proteins: oxygen. The red blood cells which
transport oxygen around the body are
– Catalytic, e.g. enzymes mostly made up of hemoglobin.
– Regulatory, e.g. hormones
– Transport, e.g. hemoglobin
– Protective, e.g. antibodies
 Fibrous Proteins

Fibrous proteins form long shapes,

and are only found in animals.
Properties of fibrous proteins:
– Water insoluble
– Very tough physically; they may be
supple or stretchy
– Parallel polypeptide chains in long
fibers or sheets
Functions of fibrous proteins: Fibrous proteins (such as collagen)
– Structural role in cells and organisms, often form aggregates because of
e.g. collagen in connective tissue, their hydrophobic properties.
bones, tendons Collagen makes up about 25% of total
protein in mammals, making it the
– Contractile, e.g. myosin, actin most abundantly occurring protein.
 Protein Function
Proteins can be classified according to
their functional role in an organism. Hemoglobin
Function Examples

Forming the structural components

Structural Collagen, keratin
of tissues and organs
insulin, glucagon, adrenalin, human
Regulating cellular function
Regulatory growth hormone, follicle stimulating
(hormones, cell signaling)
hormone
Forming the contractile elements in
Contractile myosin, actin
muscle (skeletal, smooth, cardiac)

Functioning to combat invading immunoglobulins such as

Immunological
microbes gammaglobulin

Transport Acting as carrier molecules hemoglobin, myoglobin

Catalyzing metabolic reactions

Catalytic amylase, lipase, lactase, trypsin
(enzymes)
 Your unique Proteome

The specific DNA sequence that is unique to one individual is

called a genome. As DNA is the genetic code for proteins, this
means that each individual has a unique set of proteins that he
or she is capable of synthesizing. Thus each individual is said to
have a unique proteome as well as a unique genome.

Proteome is all the proteins

produced by a cell, a tissue or
organism. Everybody has different
proteomes, and possibly identical
twins can have the same
proteomes, but with age they can
change
 Rubisco

• Full name Ribulose bisphosphate carboxylase

• Enzyme - catalyses the reaction that fixes carbon dioxide
from the atmosphere
• Provides the source of carbon from which all carbon
compounds, required by living organisms, are produced.
• Found in high concentrations in leaves and algal cells
 Insulin

• A hormone – signals many cells (e.g.

liver cells) to absorb glucose and help
reduce the glucose concentration of
the blood.
• Affected cells have receptor (proteins)
on their surface to which insulin can
(reversibly) bind to.
• Secreted by β cells in the pancreas
and transported by the blood.

The pancreas of type I diabetics don’t produce

sufficient insulin therefore they must periodically
inject synthetically produced insulin to correct
their blood sugar concentration.
 Immunoglobulins

• Also known as antibodies.

• Two antigen (a molecule on the pathogen
which provokes an immune response)
binding sites - one on each ‘arm’
• Binding sites vary greatly between
immunoglobulins (hypervariable) to
enable them to respond a huge range of
pathogens.
• Other parts of the immunoglobulin
molecule cause a response, e.g. acting as a
marker to phagocytes (which engulf the
pathogen)
 Rhodopsin

• A pigment that absorbs light

• Membrane protein of rod cells of the
retina (light sensitive region at the
back of the eye)
• Rhodopsin consists of the opsin
polypeptide surrounding a retinal
prosthetic group
• Retinal molecule absorbs a single
photon of light -> changes shape ->
change to the opsin -> the rod cell
sends a nerve impulse to the brain
• Even very low light intensities can be
detected.
 Collagen

• A number of different forms

• All are rope-like proteins made of
three polypeptides wound together.
• About a quarter of all protein in the
human body is collagen
• Forms a mesh of fibres in skin and in
blood vessel walls that resists tearing.
• Gives strength to tendons, ligaments,
skin and blood vessel walls.
• Forms part of teeth and bones, helps
to prevent cracks and fractures to
bones and teeth
 Spider silk

• Different types of silk with

different functions
• Dragline silk is stronger than steel
and tougher than Kevlar
• When first made it contains regions
where the polypeptide forms
parallel arrays
• Some regions seem like a
disordered tangle
• When the stretched the
polypeptide gradually extends,
making the silk extensible and very
resistant to breaking.
 Nucleic Acids
Nucleic acids are biochemical
macromolecules involved with the
transmission of inherited
information.
There are two main types of nucleic
acids involved with inheritance:
– Deoxyribonucleic acid (DNA)
– Ribonucleic acid (RNA)

Nucleic acids are polymers

made up of many units
called nucleotides. DNA is the most commonly
occurring nucleic acid.
 Nucleotides
A nucleotide is the basic unit of a nucleic acid.
A nucleotide has three components:
A phosphate group
A sugar (two types are possible)
A base (four types are possible) Base
Phosphate Base Phosphate

Sugar Sugar

Symbolic form of a nucleotide Chemical structure of a nucleotide

 Nucleotide Bases
Purines
There are five nucleotide bases Adenine
found in nucleic acids. • Double-ringed
structures
The DNA nucleotide bases are:
• Always pair
– Adenine up with
Guanine

– Guanine pyrimidines

– Cytosine Pyrimidines
– Thymine Cytosine
• Single-ringed
In RNA, the thymine nucleotide structures
base is replaced with Uracil. • Always pair
up Thymine
with purines

Base
component of a Uracil
nucleotide
 Formation of a Nucleotide
A nucleotide is formed when phosphoric acid and a base
are chemically bonded to a sugar molecule.
Water is given off when both the phosphate group and
base group are joined.
H2O

H2O

(–H2O)
Condensation
Phosphoric
acid
Hydrolysis
(+ H2O)

Part of a base

Sugar (deoxyribose) Nucleotide of DNA

 Formation of a Dinucleotide

H2O
Dinucleotides are formed when two
nucleotides are covalently linked together
by a condensation reaction.
H2O
Each strand is composed of nucleotide
covalently bonded between their
phosphate groups and the deoxyribose
sugar components in a 5,3 linkage H2O
between the sugars and phosphates
The linkage is termed a phosphodiester
linkage (or bond).
 Nucleic Acids
Deoxyribonucleic acid (DNA) consists of two Bacterial plasmid
polynucleotide chains wrapped around each other in a
spiral to form a double helix. DNA is found in:
– The chromosomes in the nucleus of eukaryotes
– The chromosomes and plasmids of prokaryotes
– Mitochondria
– Chloroplasts of plant cells Nucleus

Ribonucleic acid (RNA) consists of a single strand of

polynucleotide. RNA is found as:
DNA double
– Transfer RNA (tRNA) helix

– Messenger RNA (mRNA)

– Ribosomal RNA (rRNA)
– As the genetic material of some viruses
Chloroplast
 DNA Structure
Phosphates link neighboring nucleotides together to form
one half of a double-stranded DNA molecule:
Purine Pyrimidine
base base
(guanine) (cytosine)

Sugar
(deoxyribose)

Phosphate Hydrogen
bonds
Pyrimidine Purine
base base
(thymine) (adenine)
 The Double
Alpha Helix of
DNA
The
complementary
strands run in
opposite directions
or anti-parallel to
each other.

5
4 1
3 2
 The DNA Molecule

Purines join with pyrimidines

in the DNA molecule by way
of relatively weak hydrogen
bonds with the bases forming
cross-linkages.
This leads to the formation of
a double-stranded molecule
of two opposing chains of
nucleotides: Hydrogen
bonds
The Double Alpha Helix of DNA
Chargaff’s rule
 DNA & RNA Compared
Structural differences between DNA and RNA are summarized below:
DNA RNA

Strands Double Single

Sugar Deoxyribose Ribose

Guanine Guanine

Cytosine Cytosine
Bases
Thymine Uracil

Adenine Adenine

Original
Working copy
information for
for making
Info making
proteins
Double stranded proteins Single stranded
DNA molecule RNA molecule
 • Polar molecule/high solubility
Glucose • No special mode of transport needed/dissolves directly in aqueous
plasma

• Varying polarity but all are reasonably soluble

Amino acids • No special mode of transport needed/dissolve directly in aqueous
plasma

• Largely non-polar/very low solubility

• Transported by blood proteins that have polar amino acids on the
Cholesterol outer portion to give water solubility, and non-polar amino acids
internally to bind the nonpolar cholesterol

• Ionizes/high solubility
• No special mode of transport needed/sodium chloride is an ionic
Sodium chloride compound, it ionizes into separately charged Na+ and Cl– ions in
aqueous plasma

• Travels as diatomic O2/ low solubility

• Relatively low solubility in water is exacerbated by the relatively high
Oxygen temperature of warm-blooded animals (oxygen is less soluble in warm
aqueous solutions)/haemoglobin is used to bind and transport oxygen
molecules reversibly

• Non-polar fatty acid components/very low solubility

• Transported by blood proteins that have polar amino acids on the
Fats outer portion to give water solubility, and non-polar amino acids
internally to bind the nonpolar fatty acid molecules