Cell Biology &

Biochemistry Series:
Set 1

Version: 1.0
Introduction to Molecules
Organism
Tiger Living things can be organized
into several different levels or
tiers of structure. The most basic
of these is the molecular level.

Cellular level
Heart muscle cells

Organelle level
Mitochondrion

Molecular level
Amino acid -lysine
 Biological Molecules
All objects are made up of millions of
molecules too small to see with the naked eye. Water (H2O)
molecules
For example, a glass of water contains millions
of water molecules.
 Biological Molecules
Water is not always pure, and may contain other molecules.
When one or more substances are added together, a mixture is formed.

Na+

Cl–

Na+ Cl–

Na+

Cl–
Cl–

Na+
This mixture contains salt
(NaCl) and water (H2O).
Types of Biological Molecules
The molecules that make up living things can be grouped into five classes:

Water Proteins Lipids

Nucleic acids Carbohydrates

The Importance
of Biological
Molecules
An understanding of the structure
and function of biological
molecules is necessary in many
branches of biology, especially
biochemistry, physiology, and
molecular genetics.
 Biological Formulae
Biological molecules can be portrayed by:
molecular formula
structural formula

Molecular Formula Structural Formula

The molecular formula The structure of a molecule
expresses the number of can be conveyed by a
atoms in a molecule, but does molecular model.
not convey its structure.

C3H7O2S
This space filling model shows
Molecular formula for the amino
the structural formula for the
acid cysteine
amino acid cysteine
Illustrating the Structure
of Molecules
Sticks Lines Spheres Surface

Mesh Dots Ribbon Cartoon

 Biological Formulae
There are several ways of expressing a molecule’s structural
formula. For example, glucose has the molecular formula C6H12O6.
The structural formulae are:

Space filling model

β-D-glucose
Structural formula
α glucose (ring form)

Structural formula
(straight form)
Ball and stick model
Important Biological
Molecules
Carbon
Biological molecules that contain carbon
are said to be organic compounds.
Most cellular material is organic.
Hydrogen
In addition to carbon, organic molecules
commonly include atoms of oxygen and
hydrogen.
Nitrogen and sulfur are components of Oxygen
organic molecules such as amino acids and
nucleotides.

Compounds that do not contain carbon Nitrogen

are said to be inorganic molecules.

Sulfur
 Chemical Bonds
Atom
Chemical elements are able to
form chemical bonds. These
are linkages made between the
atoms in molecules.
Bonds act as a chemical glue to
hold atoms together.

Chemical bonds are formed when

atoms share or transfer electrons.

Bond
The Structure of an Atom
An understanding of an atom’s structure is required to
understand how chemical bonds form.
An atom comprises a nucleus orbited by negatively charged
electrons.
The nucleus is made up of: Nucleus
positively charged protons.
neutrons, which have no charge.
Neutron

The diagram on the right depicts a

sodium atom.
Its nucleus contains:
• 11 positively charged protons Proton
• 12 neutrons (no charge).
Eleven negatively charged
electrons orbit the nucleus in three
electron shells.
Electron
 Electron Shells
Electron
All atoms have electron shells. valency shell

Each shell contains electrons,

which orbit around the nucleus.
The number of shells and
number of electrons vary with
the type of atom.

The number of electrons in each

shell can be calculated by:
Nucleus
2n2 where n = the shell number

In general, atoms are most stable

when they have eight electrons
in their outermost shell.
A sodium (Na) atom has 11
electrons within three electron shells:
The outer shell is called the
valency shell. 2 in the first shell
8 in the second shell
1 in the third shell
 Chemical Bonds
Atoms tend to lose or gain
electrons until they have a stable
configuration. Na Cl

This can be illustrated by the

formation of sodium chloride.
Sodium and chloride atoms
When sodium reacts with chloride, it
releases the single electron in its
valency shell to chloride.

The sodium atom now has 10

electrons and the chloride atom now
has 18 electrons. Na+ Cl–

Both have eight electrons in their

valency shells.
Ionic bond
The atoms now exists as ions,
because they have each lost or The sodium and chloride atoms have
gained an electron. taken on ionic forms, and have formed
a chemical bond based on electrostatic
attraction. The compound they form
together is sodium chloride (NaCl).
Covalent Bonds
H H
Covalent bonds form when electron
pairs between two atoms are shared.
The number of electrons required to H-H
complete an atom’s valency shell will
determine how many bonds an atom will Two hydrogen atoms (above) each have
form. one electron in their valency shell. They
share an electron so the valency shell
The bonds are directional and has its full complement of two electrons.
determine the strength of the bond. Only one covalent bond is possible
Non-metals tend to form covalent bonds
readily.
A line is used to depict the covalent bond
(e.g. H-H).
O O

Two oxygen atoms (right) form

an oxygen molecule by sharing O=O
two pairs of electrons. A double
covalent bond (=) is formed.
Ionic Bonds
Ionic bonds result from the
electrostatic attraction between two
atoms of opposite charge. Na Cl

When electrons are transferred

between atoms, the atoms become
charged ions. These take two forms:
Cation: an ion with a positive charge
(has lost an electron).
Na+ Cl-
Anion: an ion with a negative charge
(has gained an electron).
Ionic
bon
d

A transfer of electrons leaves the sodium

with a net charge of +1 and the chloride
with a net charge of -1. The ions are
attracted together because of their
opposite charge, and a sodium chloride
(NaCl) crystal is formed (left).
 Hydrogen Bonds
Hydrogen bonds involve at least one hydrogen atom. -
A hydrogen atom covalently linked to
an electronegative atom, is attracted
to another electronegative atom (often
O
oxygen or nitrogen atoms). H H Hydrogen
bond
The formation of a water dimer* is an + +
example of hydrogen bonding.
A water molecule (H2O) has a slight positive -
charge on the hydrogens and a slight negative
charge on the oxygen. O H
Electrical attraction between the negative +
charge of one molecule and the positive charge
H
of another results in formation of a hydrogen bond.
+
A water dimer forms by
Hydrogen bonding is also important in the
hydrogen bonding between the
formation of proteins and nucleic acids (e.g. DNA).
positive and negative charges
of two water molecules.

*Dimer: a molecule composed of two identical subunits linked together

Disulfide Bonds Protein chain

A disulfide bond (or sulfur bridge) H H

is a single covalent bond between
two sulfur containing atoms. C SH HS C

Disulfide bonds are important in H H

the folding and stability of proteins.
Cysteine
Disulfide bonds occur between residues
cysteine, a sulphur containing
amino acid.

H H

C S S C

H H

Disulfide
bond
 Van der Waals Forces
Van der Waals forces are a very weak attraction – –
– – –
of molecules when they are very close. – – – Electrons evenly
They occur between non-polar molecules or atoms. –
– –– spread around
the nucleus
They are the weakest of all intermolecular forces;
much weaker than chemical bonds.
The constant motion of electrons around – –
a molecule causes temporary partial – –––
charge; a temporary dipole moment.
– ––
– –– Temporary dipole
The dipole moment induces a temporary moment
dipole in a neighboring atom by attracting
or repelling its electron cloud.
– –
The electron distribution changes – ––– – – –– –
constantly so the attractions are brief –
–
–– – –––
– – – ––
and very weak.

If many Van der Waals forces act at the same time, they Attraction of
can be significant (e.g. in protein configuration). temporary dipoles
 Functional Groups
Organic compounds usually comprise a carbon skeleton with
reactive or functional groups attached.
Functional groups are often involved in chemical reactions, and
play an important role in the structure and function of the molecule.

Cartoon courtesy of Nick Kim

 Functional Groups
Functional groups have definite Structural
chemical properties that they retain Group Found in
Formula
not matter where they occur. Carbohydrates,
Hydroxyl OH alcohols
These functional groups determine
the characteristics and chemical C
Carbonyl Formaldehyde
reactivity of molecules. For example:
O
Amino groups make a molecule
O
more basic. Amino acids,
Carboxyl C vinegar
Carboxyl groups make a OH
molecule more acidic.
H
Amino N Ammonia
Most chemical reactions that occur
in organisms involve the transfer of H
a functional group as an intact unit Proteins,
Sulfhydryl S H rubber
from one molecule to another.
O–
Common biological functional Phospholipids,
Phosphate O P O– nucleic acids,
groups are shown in the table right:
ATP
O
 Hydroxyl Group -OH
H H
Hydroxyl
The hydroxyl group consists of an group
oxygen atom joined by a single
covalent bond to a hydrogen atom. H C C OH
Organic molecules containing
hydroxyl groups are alcohols. H H
A metal hydroxide is formed when a
hydroxyl group is joined to a metal
(e.g. sodium hydroxide).

Structural formula of ethanol,

shown as a straight chain (top) and
a space filling model (bottom).
Carboxyl Group -COOH
H
O
The carboxyl functional group
consists of a carbon atom joined by
covalent bonds to two oxygen atoms, H C C
one of which in turn is covalently
bonded to a hydrogen atom.
H OH
Organic molecules containing
carboxyl groups are called
carboxylic acids (organic acids).
One valence electron on the carbon
is available for bonding to another
atom so that the carboxyl group can
form part of a larger molecule.

In this acetic acid molecule, the

carboxyl group is highlighted.
 Carbonyl Group -CO
H H
O
The carbonyl group is a
functional group composed of a
Propanal is an
carbon atom joined to an oxygen H C C C example of an
atom by a double bond. aldehyde.

If the carbonyl group occurs at H H H

the end of a carbon molecule it is
called an aldehyde. H O H

H C C C H

H H
If the carbonyl group occurs
within the carbon compound
it is called a ketone. Acetone is an example
of a ketone.
 Amino Group -NH2
H
O H
A amino group consists of one
nitrogen atom attached by covalent Amino
bonds to two atoms of hydrogen. A C C N group
lone valence electron on the
nitrogen is available for bonding to HO H H
another atom.
Glycine (above, and space
Organic molecules containing filling model below) is the
amino groups are called amines. simplest amino acid

Amines are weak bases.

The amino group is common to all
amino acids, which in turn are the
building blocks of proteins.
 Phosphate Group -PO3
A phosphate group composed of H
O
one phosphorous atom bound to OH OH
four oxygen atoms.
Organic molecules containing
H C C C O P O–
phosphate groups are called
organic phosphates.
The phosphate group is one of the H H H O–
three components of nucleotides
and often attached to proteins and
other biological molecules. The phosphate group of this
glycerol phosphate molecule
A free phosphate ion in solution is shown in red.
and is called inorganic phosphate
(denoted Pi) to distinguish it from
phosphates bound in molecules.
 Sulfhydryl Group -SH
H H
A sulfhydryl group consists of a sulfur
atom bonded to a hydrogen atom. OH

Organic molecules containing HS C C C

sulfhydryl groups are called thiols.
H NH2 O
As the functional group of the amino
The sulfhydryl group in the amino acid
acid cysteine, the thiol group plays an cysteine is shown here in red.
important role in biological systems.
Disulfide bonds between adjacent Sulfur
cysteine residues are important for atom
protein folding and structure.
In proteins, disulfide bonds contribute to:

tertiary structure if the cysteines are

part of the same peptide chain

quaternary structure, by forming

covalent bonds between different Cysteine (above) is one of two
peptide chains. amino acids which contain a sulfur
group. The other is methionine.
 Water
Water provides an environment in which
metabolic reactions can take place.
Water participates in, and is a common
product of, many reactions.
 The Water Molecule
The most important feature of the chemical behavior
of water is its dipole nature.
Dipole means having two charges.
There is a small positive charge on each of the two hydrogens.

There is a small negative charge on the oxygen.

– Small negative charge

A water molecule
H H
has the molecular
formula H2O
+ + Small positive charge
 Biologically Important
Properties of Water
Property of Water Significance for life

Ice is less dense than water Ice floats and also insulates the underlying water

High surface tension Water forms droplets on surfaces and runs off

Low viscosity Water flows through very small spaces and capillaries

Liquid at room temperature Liquid medium for aquatic life and inside cells

Colorless with a high transmission of

Light penetrates tissue and aquatic environments
visible light

Strong cohesive properties and high

Water can be lifted and does not pull apart easily
tensile strength

Many substances can dissolve in water Medium for the chemical reactions of life (metabolism).
(it is classified as a universal solvent) Water is the main transport medium in organisms.
Biologically Important
Properties of Water
Property of Water Significance for life

Water has a high latent heat of fusion;

significant amounts of energy are required Cell contents are unlikely to freeze.
before water will change state.

Water has a high latent heat of Heat is lost by evaporation of water.

vaporization; in order to evaporate, water Sweating in animals and transpiration in
must absorb a large amount of energy. plants cause rapid cooling.

Aquatic environments are thermally

Water has a high specific heat capacity;
stable. Organisms can maintain stable
it can absorb a lot of energy for only a
internal temperatures despite fluctuations
small rise in temperature.
in external temperature.
 pH Two water
molecules

Water has a tendency to transfer

electrons to another water molecule.
One water molecule becomes positively
charged because it gains a proton (H+)
to become a hydronium ion (H3O+).

The other becomes negatively charged

because it loses a proton to form a
hydroxide ion (OH–).

H2O + H2O ⇌ H3O+ + OH–

This reaction is often simplified by + –
thinking of the process as a
dissociation where:

H2O ⇌ H+ + OH– A hydronium ion A hydroxide ion

(H3O+) has a positive (OH-) has a negative
charge (+1) charge (-1).
 pH
The levels of hydrogen ions (H+) in solution
can be measured using the pH scale.
pH is the negative logarithm of the
hydrogen ion concentration expressed in
moles per liter.
pH = -log [H+]

Photo: Pasco
A pH meter measures the pH of a solution.
It consists of electrodes which contain a probe.
The probe measures the voltage of the solution
and converts it into pH units.
An electronic meter displays the pH reading.
The pH meter above consists
of a probe attached to a hand
held display unit.
 Acids and Bases
In pure water the concentration of H+ and OH- are equal. One
water molecule yields one H+ ion and one OH- ion.
The solution is said to be neutral.

When other substances are added to water, the balance of H+ and

OH- is altered. The solution can be:
Acidic: has a higher concentration of H+ than OH-.
Basic (alkaline or caustic): has a higher concentration of OH- than H+.
The pH Scale Battery acid 0
Lemon juice

1
The pH scale: 2
measures the concentration of 3
hydrogen ions (H+) in a solution.
4 Tomatoes
is a logarithmic scale of Milk
measurement. 5

has a scale range from 0 to 14. 6

7 Blood
On the pH scale:
8
7 is neutral (H = OH ).
+ -

9
0 - 6.9 is acidic (H > OH ).
+ -

10
7.1 - 14 is basic (H < OH ).
+ -

11

12
Sodium
Ammonia-based 13 hydroxide
cleaning fluids solution
14
 Acids
Other substances may contribute to the
concentration of H+ or OH- in a solution.
An acid is a substance that increases
the H+ concentration by dissolving into
H+ and its anion.
An acid is a proton donor.
The dissolution of an acid substance into a
solution releases H+ which lowers the pH.

Examples of
HCl → H + Cl + -
acidic substances
Lemon juice = pH 2
Tomatoes = pH 4
Black coffee = pH 5
The hydrogen ion The chloride ion is
contributes to the an anion (a negatively
acidity of a solution. charged ion)
 Bases
A base is a substance that reduces
the H+ concentration in solution. NaOH

A base is a proton acceptor.

A base can lower the hydrogen ion
concentration of a solution in two
ways:
Directly: By formation of a hydroxide ion
(OH-), which can bind a H+ ion to form
H2O, as with sodium hydroxide (NaOH).

NaOH → Na+ + OH-

OH- + H+ ⇌ H2O
Indirectly: The base accepts a H+ from Limestone
water. The base is ionized and an OH- is
released, as occurs with ammonia (NH3). Examples of basic substances
1M sodium hydroxide = pH 14
NH3 + H2O ⇌ NH4 + OH - -
Limestone (calcium carbonate) = pH 12
 Biological pH
Most biological fluids have a pH close to
neutral (e.g. blood is 7.4, urine range 6.5 -8.0).
Stomach acid is an exception at pH 1.5. In this
case, mucus secretions protect the stomach lining
from damage.

In biological systems, the pH of biological

fluids is critical for proper function.
Small changes (increasing acidity or alkalinity) can
be damaging to the body and may result in death.

The pH of biological fluids is maintained by the

presence of buffers. Metabolic reactions, e.g. during exercise,
can alter blood chemistry. A drop in blood
Buffers, such as blood proteins, minimize pH pH below 7.0 (acidosis) or a rise above
changes by accepting H+ ions when there is an 7.8 (alkalosis) for more than a few
excess, and donating H+ ions when there is a minutes can be fatal. Blood buffers
normally prevent this, but some
shortage.
physiological problems, such as
starvation, excessive vomiting, or renal
failure, can result in death because of
disturbances to blood pH.
 Inorganic Ions
Inorganic ions are important for the structure and
metabolism of all living organisms.
An ion is an atom (or group of atoms) that has gained or lost
one or more electrons. Many of these ions are water soluble.

Oxygen is
Hydrogen is attracted
attracted to to the Na+
the Cl-

Water surrounding a Water surrounding a

negative chloride ion (Cl-). positive sodium ion (Na+).
 Inorganic Ions
Ion Name Biological role
Ca2+ Calcium Component of bone and teeth Bone

Mg2+ Magnesium Component of chlorophyll

Fe2+ Iron (II) Component of hemoglobin

NO3- Nitrate Component of amino acids Neuron

PO43- Phosphate Component of nucleotides

Involved in the transmission of nerve

Na + Sodium
impulses in neurons

Involved in controlling plant water

K + Potassium
balance

Involved in the removal of water from

Cl - Chloride
urine
Hemoglobin showing
iron containing heme
group in green
 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)x.
Simple carbohydrates are generally
called sugars.The most common Deoxyribose
arrangements found in sugars are:
Pentose, a five sided sugar,
e.g. ribose and deoxyribose.
6

Hexose, a six sided sugar,

e.g. glucose and fructose.
A structural formula and Glucose 1
4
symbolic form are shown.

In solution, these naturally form rings rather than straight chain structures.
 Carbohydrates
Carbohydrates are important as both energy storage
molecules and as the structural elements in cells and tissues.
The structure of carbohydrates is closely related to their
functional properties.
Sugars (mono-, di-, and trisaccharides)
play a central role in energy storage.
Carbohydrates are the major component
of most plants (60-90% of dry weight).
Weaving cloth

Carbohydrates are used by

humans as a cheap food source...

Collecting thatch for roofing

Carrying wood ...housing and clothing. Cotton,

linen, and coir are all made up of
...and as a source of fuel,... cellulose, a carbohydrate polymer.
 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).
fructose (honey and fruit juices).

Monosaccharides generally contain

between three and seven carbon
atoms in their carbon chains.
The 6C hexose sugars occur
most frequently.
Glucose is a monosaccharide sugar. It
occurs in two forms, the L- and D- forms.
All monosaccharides are reducing The D-glucose molecule (above) can be
sugars, meaning they can utilized by cells while the L-form cannot.
participate in reduction reactions.
 Disaccharides
Disaccharides are double-sugar molecules joined with a glycosidic bond.

They are used as energy sources and as building blocks for larger molecules.

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.

Only a few disaccharides (e.g. lactose) are classified as reducing sugars.

Carbohydrate α-glucose

Isomers
Compounds with the same chemical formula
can have different arrangement of atoms.
These molecules are called isomers.

Structural isomers have the atoms linked in a

different sequence from one another.
β-glucose
Despite the relatively small differences,
structural isomerism can have important
consequences for the polymers that result.
For example:
α glucose polymers form starch.

β glucose polymers form cellulose.

The α and β glucose molecules,
These molecules have very different
(above), are examples of structural
properties.
isomers. They contain the same
Optical isomers are identical in every way but atoms but the hydroxyl groups are
linked to the C1 atom differently.
are mirror images of each other.
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 Juniper
of starch hydrolysis and is sap
found in germinating grains.

Lactose
Components: β-glucose + β-galactose
A sucrose molecule (above)
Source: Milk depicted as a stick molecule.

Cellobiose
Components: β-glucose + β-glucose
Milk (right) contains the
Source: Partial hydrolysis of cellulose. disaccharide, lactose.
Polysaccharides - Cellulose
Symbolic form of cellulose
Cellulose is a glucose polymer. It is an
Glucose monomer
important structural material found in plants.
It is made up of many unbranched 4
1

chains of β-glucose molecules

held together by 1, 4 glycosidic links. 1,4 glycosidic
bonds create
Parallel chains are cross-linked by hydrogen unbranched 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.

The cellulose structure is shown

(right) as a ball and stick model.
Cellulose is repeating chains of
β-glucose molecules.
Polysaccharides - Starch
Symbolic form of amylopectin
Starch is a polymer of glucose, made up
of long chains of α-glucose molecules. 1,6 glycosidic
1
1
bonds create
4
Starch contains a mixture of: 6 branched chains
1
25-30% amylose: long unbranched 4
chains of many hundreds of glucose 6

linked by 1-4 glycosidic bonds.

4

70-75% amylopectin: branched

Starch granules
chains 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
Glycogen is chemically similar to
amylopectin, but is more
extensively branched. 1,6 bonds

It is composed of α-glucose
molecules, but there are more Symbolic form of glycogen
1,6 glycosidic links mixed with
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.

Structurally, it is almost the same as cellulose

except that the -OH group at carbon atom 2 is
replaced by a nitrogen-containing group
(NH.CO.CH3).

Chitin forms bundles of long parallel chains.

The exoskeleton of an
It is found in the cell walls of fungi and it is an insect is made of chitin
essential component of the arthropod exoskeleton.
Condensation & Hydrolysis
Carbohydrate Carbohydrate
condensation hydrolysis

Monosaccharides are joined Compound sugars can be

together to form broken down into their
disaccharides and constituent
polysaccharides. monosaccharides.

Water is released in the A water molecule provides

process. the hydrogen and hydroxyl
groups required.
Energy is supplied by a
nucleotide sugar such as The reaction is catalyzed by
ADP-glucose. enzymes.

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
 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 can be classified as:
simple lipids: fats, oils, and waxes.
phospholipids and related molecules. Plasma membrane

steroids

Lipids have many roles, including as:

Phospholipids are the primary structural
biological fuels component of all cellular membranes, such as
the plasma membrane (false color TEM above).
hormones

Dept. Biological Sciences, University of Delaware

structural components of membranes

Fats provide twice as much energy as

Fat cell
carbohydrates.
Capillary
Fats and oils are not macromolecules but,
because of their hydrophobic properties, they
aggregate into globules.

Proteins and carbohydrates can be converted Lipids are often stored in special adipose
into fats stored in adipose tissue. tissue, within large fat cells (above).
Biological Roles of Lipids
Mitochondrion
(false color TEM)

Lipids are concentrated

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

The white fat tissue (arrows)

is visible in this ox kidney

Fat absorbs shocks.

Organs that are prone to
bumps and shocks (e.g.
kidneys) are cushioned with
a relatively thick layer of fat. Lipids are a source of metabolic
water. During respiration, stored
lipids are metabolized for energy,
producing water and carbon dioxide.

Stored lipids provide

insulation in extreme
environments. Increased body
fat levels in winter reduce heat
losses to the environment.
 Fats and Oils
The most common lipids in living things are the neutral fats.
They make up the fats and oils found in plants and animals.

Fats and oils are formed by condensation reactions between

fatty acids and glycerol to form ester links (–COO–).
One fatty acid = monoglyceride
Two fatty acids = diglyceride
Three fatty acids = triglyceride or triacylglycerol. Globules of fat or oil are
compact and relatively inert
Triacylglycerols are the most common of these.
Water is lost to 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 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

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

The fatty acids making up triacylglycerols

are long unbranched hydrocarbon chains
(CH3(CH2)n –), ending with a carboxylic acid
(–COOH). Palmitic acid: a saturated fatty acid

Some are saturated fatty acids, with a

maximum number of hydrogen atoms.

Some are unsaturated, with double

bonds and fewer hydrogen atoms.
Linoleic acid: a saturated fatty acid
 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

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

Palmitic acid is a saturated fatty acid.

All of the spaces on the carbon bonds
are filled by hydrogens, which results
in a straight chain molecule, as shown
in the space filling model (right).
 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.

O H H H H H H H H H H H H H H H H H H

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

Linoleic acid is an unsaturated fatty acid.

The double bonds between the carbon
atoms prevent bonds to hydrogen. The
double bonds produce a kink in the chain
as shown on the space filling model (right).
Kink
 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)

H2C Nonpolar,
COO hydrocarbon tails
of two fatty acids
condensed with
HC COO glycerol
O–
H2C O P O–
O Fatty acid

Glycerol Fatty acid

Phosphate group from phosphoric

acid (HPO4) condenses with the Symbolic representation
third -OH of glycerol PO43- of a phospholipid
 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
Steroids are classified as lipids, but their one five carbon atom ring.
structure 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.

Examples of steroids include:

sex hormones (testosterone and estrogen)

hormones such as cortisol and aldosterone

cholesterol is a sterol lipid and is a precursor to

several steroid hormones.
Steroid sex hormones are responsible
for both primary and secondary sexual
characteristics in males and females.
 Lipid Condensation Water is lost to
form an ester bond

Triacylglycerols (also called H O

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

bonds with three fatty acids. O

Glycerol is an alcohol H C O H + OH C CH2 CH2 CH2.............CH3

O
containing three carbons.
H C O H OH C CH2 CH2 CH2.............CH3
Each carbon is bonded to a
hydroxyl (–OH) group. H

Glycerol Three fatty acids

When glycerol bonds with the
fatty acid, an ester bond is H O
formed and water is released. H C O C CH2 CH2 CH2.............CH3 + H2O
Three separate condensation O

reactions are involved in H C O C CH2 CH2 CH2.............CH3

+ H2O
producing a triglyceride. O
H C O C CH2 CH2 CH2.............CH3 + H2O
H

Triacylglycerol (triglyceride) Water

 Introduction to
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 (space filling model

right) 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
There are five nucleotide bases
found in nucleic acids. Purines
Adenine
The DNA nucleotide bases are: • Double-ringed
structures
Adenine
Guanine • Always pair up Guanine
with pyrimidines
Cytosine
Thymine
Pyrimidines
In RNA, the thymine nucleotide Cytosine
base is replaced with uracil. • Single-ringed
The other three nucleotides structures
remain unchanged.
• Always pair up
Thymine
with purines

Base component Uracil

of a nucleotide
 Molecular Structure of
Nucleotides
base (adenine)
Sugar

Guanine nucleotide
DNA and RNA
Adenine nucleotide
DNA and RNA
phosphate

Uracil nucleotide
RNA only

Thymine nucleotide
Cytosine nucleotide DNA only
DNA and RNA
 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.
Because water is given off, both reactions are condensation reactions.

H2 O

H 2O

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

Part of a base

Sugar (deoxyribose) Nucleotide of DNA

Formation of a Dinucleotide
Dinucleotides are formed when two
nucleotides are covalently linked
together by a condensation reaction.
The linkage occurs between the H2O
phosphate group of one nucleotide
and the sugar of another.
The linkage is termed a
phosphodiester linkage (or bond).

O P OH

Phosphodiester bond
 Nucleic Acids
When a large number of nucleotides link together a
nucleic acid (or polynucleotide) is formed.
Bacterial plasmid
Deoxyribonucleic acid (DNA) consists of two
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 & 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

Double stranded Single stranded

DNA molecule RNA molecule
 The DNA Molecule
Symbolic Space-filling
Purines join with pyrimidines in the representation model
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:

The symbolic diagram shows

DNA as a flat structure.

The space-filling model shows

how, in reality, the DNA molecule
twists into a double helix.
Hydrogen
bonds
 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)
 Amino Acids
Amino acids (such as proline
below) 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 amino acids.

The order in which the different 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 different
amino acids acids found in proteins.
The “R” group varies in
All amino acids have a common chemical make-up with
each type of amino acid
structure:
The ‘R’ group is variable, which
means that it is different in each R Carbon
amino acid. atom

NH2 C COOH

Amine
group H Carboxyl group makes
the molecule behave
like a weak acid

Hydrogen
atom
 Amino Acids
The ‘R’ groups of amino acids can have
quite diverse chemical properties.

This “R” group gives

the amino acid
alkaline properties.
This “R” group can form
This “R” group gives
disulfide bridges with other
the amino acid acidic
cysteines to create cross
properties.
linkages in a polypeptide 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 Acids
Not all amino acids can be manufactured by our body.

Ten must be obtained from our diet. These are called essential amino acids.
The essential amino acids are marked by ◆

Amino acids occurring in proteins

Alanine Glycine Proline

Arginine ◆Histidine Serine

Asparagine ◆Isoleucine ◆Threonine

Aspartic acid ◆Leucine ◆Tryptophan

Cysteine ◆Lysine ◆Tyrosine

Glutamine ◆Methionine ◆Valine

Glutamic acid ◆Phenylalanine

 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

The diagram above represents a polypeptide chain.

The peptide bonds between amino acids are
indicated with arrows.
Condensation & Hydrolysis
Two amino
Condensation acids
Amino acids are joined together to
form peptide or polypeptide chains.
A water molecule is released.

Condensation
Hydrolysis

Hydrolysis
Polypeptide chains are broken down
into smaller peptide chains or simple
amino acids. H 2O

A water molecule provides a

hydrogen and hydroxyl group. Peptide
bond
Example: digestion

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
H
Isomerism in Amino Acids
All amino acids, apart from
glycine, show optical isomerism.
An isomer occurs when a
molecule has one molecular Carbon
formula, but can have different atom
structural arrangements.
Optical isomerism relates to the
arrangement of the four bonding
sites on the carbon atom.

Carbon’s tetrahedral bonding arrangement.

The arrows indicate the four carbon bonding sites.
Isomerism in Amino Acids
Most amino acids occur in two possible optical isomers:
D-amino acids.
L-amino acids.

Most amino acids found in proteins exist in the L-form.

COOH COOH

C C
NH2 R

R H2N
H H
D-form of a generic amino acid. L-form of a generic amino acid.
 Proteins
Proteins are macromolecules, consisting of many amino
acids linked together as polypeptide chains.
Each cell contains several hundred to several thousand
proteins.
Human Cytochrome C
Proteins play a key role in the body. They are involved in: (respiratory chain)
Enzyme reactions
Oxidation-reductions, e.g. respiratory chain
Structure
Storage
Transport
Cell signaling
Defense

These two proteins are depicted

Insulin-like growth factor 1 as 3D cartoon and stick models.
(used in cell signaling)
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 protein.
Lysozyme is a single polypeptide
A protein’s conformation is central to its function. strand of 129 amino acids and a
tertiary structure which is part α-
If the shape is altered then the protein may no helix, part β- sheet and part
longer be able to perform its biological role. irregular sections.

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
quaternary: the interaction of two or more
polypeptide chains Hemoglobin has a complex
quaternary structure with
four subunits
 Proteins: Phe
Glu

Primary Structure
Tyr

Ser

The primary (1°) protein structure is Iso

the amino acid sequence.
Hundreds of amino acids link together Phe
to form polypeptide chains.
The chemical interaction (attraction and Ala
repulsion) of the individual amino acids
helps define the final protein shape. Glu
Met Gly

Ala
When amino acids are
linked together they form Ala
a polypeptide chain.
 b

Proteins:
Secondary Structure
The secondary (2°) structure is the
shape of the polypeptides chain.

There are two common types of Hydrogen

secondary structure: bonds

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. Two peptide
chains
Secondary structures are a result of
hydrogen bond interaction between
neighboring CO and NH groups of the
polypeptide backbone.
α-helix β-pleated sheet
 Proteins:
Tertiary Structure
The tertiary (3°) structure of a Heme group
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 bonding (reactions
between two cysteine amino acids).
These form the strongest links.

Weak bonding (ionic and hydrogen).

Hydrophobic interactions. The tertiary structure of a
hemoglobin molecule shows it is
Disulfide bridge
folded around a heme group which
binds oxygen. Disulphide bridges
help maintain the structure.
 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:
Overview
Ser
1° Tyr Glu

Iso Ala Gly

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

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

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 association of 3°

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.

Examples of protein denaturation are seen

in many everyday circumstances:
Cooking food denatures protein and makes it
easier to digest.
Alcohols disinfect by denaturing bacterial
and viral proteins.
Reversible protein denaturation is
Reversible denaturation is involved in waving
responsible for the “perm”.
hair. The keratin protein in hair is denatured
Disulfide linkages are responsible
using a reducing agent, then set, and finally
for keratin’s tertiary structure. These
"glued" back into disulfide bridges by an
are broken and then reset during
oxidizing agent (H2O2).
the chemical 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 protein. bonds and form strong bonds with the
Long exposure can also break carboxyl groups of the R groups and
down the primary structure of the reduce the protein charge. This results
protein. in protein precipitation.

Heat and radiation. Detergents and solvents.

These cause disruption of the These form bonds with the non-polar
bonds in the protein through groups in the protein, thereby
increased energy provided to the disrupting hydrogen bonding.
atoms.
 Protein Denaturation
An everyday example of protein denaturation is cooking eggs:

Raw egg The hydrogen bonds in the The denatured albumin

57 grams in weight egg white albumin are broken protein uncurls and
(about 7.4g or 13% by the heating process during coagulates forming a
protein). cooking. The egg white albumin solid white substance.
protein is heat denatured.
 Categorizing Proteins
Proteins can be categorized
according to their tertiary structure:
Globular proteins

Fibrous proteins α-chain Fibers form due

to cross links
between
collagen
molecules

disulfide ϐ-chain
bond

Bovine insulin (above) is an example Collagen (above) is an example of a

of a small globular protein. It fibrous protein. It consists of three helical
consists of two chains held together polypeptide chains wound around each
by disulfide bridges between other. Hydrogen bonding between glycine
neighboring cysteine (Cys) molecules. residues holds these chains together.
 Globular Proteins
Globular proteins are very
diverse in their structure.
They can exist as single chains or subunit
comprise several chains, as occurs
in hemoglobin and insulin.
subunit
Properties of globular proteins:
Easily soluble in water
Tertiary structure is critical to function
subunit
Polypeptide chains are folded into a
spherical shape subunit
Functions of globular proteins:
Catalytic, e.g. enzymes

Regulatory, e.g. hormones Hemoglobin (above) is a globular protein.

Its heme (iron containing) groups bind
Transport, e.g. hemoglobin
oxygen. The red blood cells which
Protective, e.g. antibodies transport oxygen around the body are
mostly made up of hemoglobin.
 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:

Structural role in cells and organisms, e.g.
collagen in connective tissue, bones, Fibrous proteins (such as collagen
tendons above) often form aggregates because
of their hydrophobic properties.
Contractile, e.g. myosin, actin Collagen makes up about 25% of total
protein in mammals, making it the 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 of
Structural Collagen, keratin
tissues and organs
insulin, glucagon, adrenalin, human
Regulating cellular function (hormones,
Regulatory growth hormone, follicle stimulating
cell signaling)
hormone
Forming the contractile elements in
Contractile myosin, actin
muscle (skeletal, smooth, cardiac)

Functioning to combat invading

Immunological antibodies such as gammaglobulin
microbes

Transport Acting as carrier molecules hemoglobin, myoglobin

Catalyzing metabolic reactions

Catalytic amylase, lipase, lactase, trypsin
(enzymes)
Modifying Proteins
Some proteins are modified to
perform specific roles.
Nucleus
Proteins are produced by ribosomes,
and can be modified at the rough
endoplasmic reticulum, or the Rough
endoplasmic
Golgi apparatus. reticulum
The Golgi apparatus functions
principally as a system for
processing, sorting, and modifying
proteins.
Protein modification can involve the
Golgi
addition of carbohydrates to form a apparatus
glycoprotein, or the addition of fatty
acids to form lipoproteins.
Cell cytosol

Cutaway section of a cell

 Glycoproteins
Glycoproteins are
proteins with Carbohydrate
attached to protein
carbohydrate groups
covalently linked to them.
Plasma
The carbohydrates are
membrane
added at the interior of
rough endoplasmic
reticulum. Some proteins
may have carbohydrates
added to them to form
glycoproteins.
Glucose, mannose and
galactose are often
found in glycoproteins. Cell cytosol

Protein

Enlarged section of a plasma membrane

showing a glycoprotein embedded in it
 Role of Glycoproteins
Carbohydrate groups may help
determine the final destination of a Carbohydrates on cell
glycoprotein within the cell or for export. surfaces may be important in
intercellular recognition, as
Carbohydrate groups help position in the interaction of cells to
or orientate glycoproteins in form tissues and the detection
membranes. The carbohydrate of foreign cells.
groups prevent them from rotating in
the membrane.

Plasma
membrane

Cell cytosol
X
 Enzymes
Enzymes are molecules that act as catalysts
to speed up biological reactions.
Enzymes are not consumed during the
biological reaction.
The compound on which an enzyme acts is
the substrate.
Enzymes can break a single structure into
smaller components or join two or more
substrate molecules together.
Most enzymes are proteins.

Many fruits contain enzymes that are used in

commercial processes. Pineapple (Ananas
comosus, right) contains the enzyme papain
which is used in meat tenderization processes
and also medically as an anti-inflammatory agent.
 Enzyme Examples
Enzyme Role
Stomach enzyme used to break protein down
Pepsin
into peptides. Works at very acidic pH (1.5).

A digestive enzyme that breaks lactose into

Lactase glucose and galactose. Low levels of lactase
can result in lactose intolerance.

A family of enzymes that act on the

Topoisomerase coiled structure of DNA. They cut the DNA
to alter the coiled structure.

A family of enzymes that break down

hyaluronic acid and increase tissue
Hyaluronidase
permeability. Often used during eye surgery
to administer local anesthetics faster.

A naturally occurring enzyme in yeasts,

Zymase widely used in the baking industry to ferment
3D molecular structures for the sugar into ethanol and carbon dioxide.
enzymes pepsin (top) and
hyaluronidase (bottom).
 Enzymes
Enzymes have a specific region where
the substrate binds and where catalysis
occurs. This is called the active site.
The active site is usually a cleft or pocket
at the surface of the enzyme. Substrate
modification occurs at the active site.
Enzymes are substrate-specific, although
specificity varies from enzyme to
enzyme:
High specificity: The enzyme will only bind
with a single type of substrate.
Space filling model of the yeast
Low specificity: The enzyme will bind a
enzyme hexokinase. Its active
range of related substrates, e.g. lipases site lies in the groove (arrowed)
hydrolyze any fatty acid chain.

When a substrate binds to an enzyme’s

active site, an enzyme-substrate
complex is formed.
 Enzyme Active Sites
Substrate molecule:
Substrate molecules are the
chemicals that an enzyme
acts on. They are drawn into
the cleft of the enzyme. Active site:
The active site contains both binding
and catalytic regions. The substrate
is drawn to the enzyme’s surface and
the substrate molecule(s) are
positioned in a way to promote a
reaction: either joining two molecules
Enzyme molecule: together or splitting up a larger one.
The complexity of the
active site is what makes
each enzyme so specific
(i.e. precise in terms of the
substrate it acts on).

This model (above) is an enzyme called

Ribonuclease S, that breaks up RNA
molecules. It has three active sites (arrowed).
 Lock and Key Model
The lock and key model of enzyme action, proposed earlier
this century, proposed that the substrate was simply drawn into
a closely matching cleft on the enzyme molecule.
Substrate Products

Symbolic representation of the lock and key model of enzyme action.

Enzyme 1. A substrate is drawn into the active sites of the enzyme.
2. The substrate shape must be compatible with the enzymes active site in
order to fit and be reacted upon.
3. The enzyme modifies the substrate. In this instance the substrate is
broken down, releasing two products.
 Induced Fit
Model Two substrate
molecules are
drawn into the
More recent studies have revealed cleft of the
that the process is much more likely enzyme.
to involve an induced fit.
The enzyme
The enzyme or the reactants changes shape,
(substrate) change their shape slightly. forcing the substrate
molecules to
The reactants become bound to combine.
enzymes by weak chemical bonds.
This binding can weaken bonds within
the reactants themselves, allowing the
reaction to proceed more readily.
The resulting end
product is released
by the enzyme
which returns to its
normal shape, ready
to undergo more
reactions.
 Enzymes
Enzymes are catalysts; they make it easier for a reaction to take place.
Catalysts speed up reactions by influencing the stability of bonds in the
reactants. They may also provide an alternative reaction pathway, thus
lowering the activation energy needed for a reaction to take place (see
the graph below).
High Without enzyme: The activation
energy required is high.
Amount of energy stored in

Reactant With enzyme: The activation

the chemicals

energy required is lower.

High energy

Product

Low energy

Low
Start Finish
Direction of reaction
 Catabolic Reactions
Catabolic reactions involve the The substrate is
breakdown of a larger molecules into attracted to the enzyme
smaller components, with the release The substrate is by the “active sites”.
subjected to stress,
energy (they are exergonic). which facilitates the
breaking of bonds
Enzymes involved in catabolic
reactions can cause a single
substrate molecule to be drawn into
the active site.
Chemical bonds are broken, causing
the substrate molecule to break apart
to become two separate molecules. Enzyme
Catabolic reactions include:
Digestion: Breakdown of large food
molecules. The substrate is cleaved
and the two products are
released to allow the
Cellular respiration: Oxidative enzyme to work again.
breakdown of fuel molecules such
as glucose.
 Anabolic Reactions The substrate is
attracted to the enzyme
In anabolic reactions, smaller by the “active sites”.
The substrate is
molecules are joined to form larger ones. subjected to stress,
which will aid the
These reactions are endergonic; formation of bonds.
they require the input of energy.
Enzymes involved in anabolic reactions
can cause two substrate molecules
to be drawn into the active site.
New chemical bonds are formed
resulting in the formation of a single Enzyme
molecule.
Examples include:
Protein synthesis: Build up of
polypeptides from peptide units.
The two substrate molecules
Cellular respiration: Oxidative form a single product,
breakdown of fuel molecules such as which is released, freeing the
enzymes to work again.
glucose.
 Effect of Temperature
Enzymes often have a
Optimum temperature
narrow range of for the enzyme
conditions under which
they operate properly.
For most plant and animal
enzymes, there is little
Rapid
activity at low
Rate of reaction
denaturation
temperatures. at high
Too cold for the temperatures
enzyme to
Enzyme activity increases operate
with temperature, until the
temperature is too high for
the enzyme to function.
(See diagram right).
At this point, enzyme
denaturation occurs and
the enzyme can no
longer function. Temperature (°C)
 Effect of pH
Enzymes can be affected by pH.
Extremes of pH (very acid or
alkaline) away from the enzyme Trypsin
Pepsin Urease
optimum can result in
enzyme denaturation.

Enzyme activity
Enzymes are found in very
diverse pH conditions, so they
must be suited to perform in
these specialist environments.
Pepsin is a stomach enzyme and
has an optimal working pH of 1.5,
which is suited for the very acidic 1 2 3 4 5 6 7 8 9 10
conditions of the stomach. Acid Alkaline
pH
Urease breaks down urea and has
an optimal pH of near neutral. See Enzymes often work over a range of pH
diagram right. values, but all enzymes have an optimum
pH where their activity rate is fastest.
Factors Affecting Enzyme
Reaction Rates
Effect of Enzyme Effect of Substrate
Concentration Concentration
Rate of reaction

Enzyme concentration Concentration of substrate

Rate of reaction continues to increase Rate of reaction increases and then plateaus
with an increase in enzyme concentration. with increasing substrate concentration.

This relationship assumes non-limiting This relationship assumes a fixed amount

amounts of substrate and cofactors. of enzyme.
 Enzyme Cofactors
Active
site
Some enzymes require Enzyme is protein only
cofactors to be active. Example: lysozyme

Cofactors are a nonprotein Enzyme

component of an enzyme.
Cofactors can be:
Active
site Prosthetic
organic molecules (coenzymes). group

inorganic ions (e.g. Ca2+, Zn2+).

Enzyme + prosthetic group
Cofactors may be: Enzyme Example:
flavoprotein + FAD
Permanently attached, in which case
they are called prosthetic groups.
Active
Temporarily attached coenzymes, site
which detach after a reaction, and
may participate with another enzyme Enzyme + coenzyme
in other reactions. Coenzyme Example:
dehydrogenases + NAD

Enzyme
 Enzyme Inhibitors
Enzymes can be deactivated by Native
arsenic
enzyme inhibitors.
There are two types of enzyme
inhibitors:
Reversible inhibitors are used to
control enzyme activity. There is Mercury
often an interaction between the
substrate or end product and the
enzymes controlling the reaction.

Irreversible inhibitors bind tightly

and permanently to the enzymes

Photo: US EPA
destroying their catalytic activity.
Irreversible inhibitors usually
covalently modify an enzyme.

Many drug molecules are Some heavy metals (above) are

enzyme inhibitors. examples of poisons which act as
irreversible enzyme inhibitors.
 Irreversible Enzyme
Inhibitors Substrate

Some heavy metals, such as

cadmium (Cd), arsenic (As), and Enzyme
The lipothiamide
lead (Pb) act as irreversible pyrophosphatase
enzyme inhibitors. enzyme with substrate
bound to its active site.
They bind strongly to the sulphydryl
(-SH) groups of the protein,
destroying its catalytic activity.
Most heavy metals, e.g. arsenic,
act as non-competitive inhibitors. Arsenic binds to the
enzyme and causes
Mercury (Hg) is an exception. its shape to change,
preventing the
It acts as a competitive inhibitor,
As substrate from binding
binding directly to a sulphydryl group to the active site.
in the active site of the papain
enzyme.
Poisons, such as arsenic (As), act as an
Heavy metals are retained in the irreversible enzyme inhibitor. It binds to the
lipothiamide pyrophosphatase enzyme altering
body, and lost slowly. its shape so the substrate cannot bind.
 Reversible Inhibitors
Reversible inhibitors are used to control enzyme activity.
There is often an interaction between the substrate or end product
and the enzymes controlling the reaction.

Buildup of the end product or a lack of substrate may deactivate the enzyme. Competitive
inhibition involves competition for the active site.

Noncompetitive inhibitors work either to slow down the rate of reaction, or block the
active site altogether and prevent its functioning (allosteric inhibition).

Competitive inhibitor The substrate can still The substrate cannot

blocks the active bind to the active site bind to the active site
Substrate site. The substrate but the rate of reaction because the active
cannot bind. S is lowered. site is distorted.
S

S S

Enzyme Enzyme Enzyme Enzyme

Noncompetitive Noncompetitive
inhibitor inhibitor
Competitive Noncompetitive Allosteric
No inhibition
inhibition inhibition enzyme inhibitor
 Chromatography
Chromatography is a commonly used technique that is used
when there is a small amount of sample available and we wish
to separate the molecular components of a mixture.
In chromatographic techniques:
The analyte is the substance that is Shell Unocal Arco Chevron Texaco Mobil
Aviation
gas
to be isolated or purified.

The stationary phase is the

substance through which the
solvents and analyte travel through
or bind to (e.g. paper or a silica layer).

The mobile phase is the

analyte-solvent mixture.

A chromatograph takes a chemical Thin layer chromatography of the dye additives

in gasoline. Photo courtesy Zymax Forensics
mixture carried by liquid or gas and
separates it into its component parts.
Paper Chromatography
Set up and procedure
The chromatography paper is folded so it can
be secured by the bung inside the test tube.
The bung also prevents the solvent
evaporating.

Chromatography paper may be treated with

chemicals to stain normally invisible pigments.

A spot of concentrated sample is added using

a pipette and suspended above the solvent.
As the solvent travels up the paper it will carry
the sample with it. The distance the sample
travels depends on its solubility.

A pencil line is used to show the starting point.

Solvent
 Paper Chromatography
To identify the substances in a mixture an
Rf value is calculated using the equation:

Distance traveled by the spot (x)

Rf =
Distance traveled by the solvent (y)

These Rf values can then be compared

with Rf values from known samples or
y
standards, for example:
x
Glycine’s Rf value = 0.50
Alanine’s Rf value = 0.70
Arginine’s Rf value = 0.72
Leucine’s Rf value = 0.91
Chlorophyll Solvent wetting front

Separation Carotene

Four primary pigments of

green plants can easily be
separated and identified using
paper chromatography.
These pigments include two
greenish chlorophyll Xanthophyll
pigments and two yellowish
carotenoid pigments. Chlorophyll a
Pigments are separated
according to differences in
their relative solubilities.
Chlorophyll b
 Simple
Food Tests
Biochemical tests are used to detect the
presence of particular molecules (such A positive Benedict’s test
as lipids, proteins, or carbohydrate). result. The solution turns
The tests are usually quite simple when from blue to orange indicting
the presence of sugar.
large quantities are present.

Sugars: Benedict’s Test

Reagent: Benedict’s solution

Proteins: Biuret test Procedure: Non reducing sugars: The sample is boiled and
diluted with hydrochloric acid, then cooled and
Reagent: Biuret solution neutralized. A test for reducing sugars is then
performed.
Procedure: A sample is added to biuret
Reducing sugars: Benedict’s solution is added
solution and gently heated.
and the sample is placed in a waterbath.

Positive Solution turns from blue to Positive Sample turns from blue to orange.
result: lilac. result:
 Simple Food Tests

A positive test for lipid A positive test for

results in a cloudy- starch results in the
white emulsion. solution turning a
blue-black color.
Lipids: The Emulsion
Test
Reagent: Ethanol
Starch: The Iodine Test
Procedure: The sample is shaken with
Reagent: Iodine
ethanol. After settling, the liquid
portion is distilled and mixed with
water. Procedure: Iodine solution is added to the
sample.
Positive The solution turns into a cloudy-
Positive Blue-black staining occurs.
result: white emulsion of suspended lipid
result:
molecules.
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