Table 1: Comparison between Different Types of Polysaccharides

Starch

Polymer
Components

Amylose

Cellulose

NA

NA

-glucose

Monomers/subunits
Bonds formed between the
subunits

Amylopectin

Glycogen

-1,4 glycosidic
bonds

-glucose

-1,4 glycosidic and -1,6 glycosidic

bonds
Helical

3D shape of a chain

H bonds within the

Bonds formed within the chain
amylose helices

-1,4 glycosidic
bonds
Linear

H bonds formed
within the amylose
helices, and
between the
branches

H bonds within
the helices, and
also between the
branches

H bonds formed
between the
chains

Branching

No

Yes

More than
amylopectin

No

Solubility in water

No

No

No

No

NA

From chains to
microfibrils to
macrofibrils

Energy storage in
animals

Structural role
e.g. formation of
cell wall in plants

Levels of organisation

Functions

NA

NA

Energy storage in plants

Table 2: Comparison between Different Types of Lipids

Class

Triglycerides

Phospholipids

Cholesterols

Components

1 glycerol + 3 fatty acids

1 glycerol + 2 fatty acids

+ 1 phosphate group

4 fused hydrocarbon
rings

Bonds formed between

the components

Ester bonds

Ester bonds

Carbon-carbon (covalent)
bonds

Presence of C=C bonds

Yes
(in fatty acids)

Yes
(in fatty acids)

Yes

1. Energy storage
2. Buoyancy for marine
organisms
Functions

3. Heat insulation
4. Mechanical protection
5. Source of metabolic
water

1. Forming cell
membrane, which
regulate movement of
substances

1. Regulate fluidity of
cell membrane
2. Synthesis of sex
hormones

Table 3: Comparison between Different Protein Structures

Structure

Secondary

Tertiary

Quaternary

Linear sequence
and number of
amino acids

Repeated, local
folding of a
polypeptide chain

Global folding of a
polypeptide chain
into a unique 3dimensional
configuration

Association of > 1
polypeptide chains
(subunit) to form a
protein

Peptide bonds

Hydrogen bonds
formed between the
NH and CO groups of
a.a. within the
backbone

Types

NA

Alpha helix and beta

sheet (parallel & antiparallel)

NA

NA

Presence of
binding sites

NA

NA

Yes

Yes or No (for
collagen only)

Specific
examples

NA

NA

Myoglobin

Collagen,
Haemaglobin

Definition

Bond(s)

Primary

Hydrogen, ionic, disulphide bonds,

hydrophobic interactions between the R
groups of amino acids

Table 4: Comparison between Collagen and Haemaglobin

Criteria
Classification

Collagen
Fibrous

Haemaglobin
Globular

hydrophobic a.a. residues are on the

Arrangement of
hydrophobic a.a. residues are buried in the
exterior, hydrophilic a.a. are buried in
amino acid residues
interior, hydrophilic a.a. are on the exterior.
the interior.
Basic unit
Levels of protein
structures

Tropocollagen comprising three helical Comprises four subunits/two

polypeptide chains
dimmers e.g 11, 22
Primary, secondary, quaternary

identical

Primary, secondary, tertiary, quaternary

Yes, Glycine-X-Y
Repeating a.a.
sequence

X: proline

No

Y: hydroxyproline/hydroxylysine

Cross linking

H bonds between the three chains, Ionic,

hydrogen,
hydrophobic
bnds
covalent bonds between the collagen between the two chains in each dimer,
fibers
hydrogen bonds between the two dimers

Hierarchical
organisation

Tropocollagen molecules assemble to

form collagen fibrils, which further NA
assemble to form collagen fibers.

Staggered
arrangement of the

Yes and this contributes to the banded No

polypeptide chains

appearance

Solubility in water

No, due to presence of proline and

Yes,
glycine which are hydrophobic

Presence of nonNo
protein components

Yes, each subunit consists of a haem

which complexes with an iron ion and
binds with an oxygen molecule.

Presence of binding
No
site

Yes, haem
hydrophobic

binding

pocket

that

is

Table 5: Comparison of the effects of various chemical agents on protein

Agents

Heat/Radiation

How is the protein denatured?

High kinetic energy causes the atoms in
the protein molecule to vibrate violently,
disrupts the bonds holding the 3D
configuration of protein

What are the bonds broken apart?

Hydrogen, ionic, disulphide bonds and
hydrophobic interactions

Ionic, hydrogen bonds.

High concentrations Ionisation of charged R groups, disrupts
of acids, alkali and the bonds holding the 3D conformation of Peptide bonds when subjected to
protein and result in protein coagulation.
salts
prolonged incubation
Heavy metals e.g.
mercury, lead
Organic solvents
and detergents e.g.
alcohol

Reduces proteins electrical property,

increases its insolubility in water and
causes precipitation.

Ionic bonds, hydrogen bonds to a lesser

extent

Disrupts bonds holding the 3D

conformation of protein

Hydrophobic interactions, then hydrogen

bonds