4.

(a) Triglycerides are formed by the ester linkage of 3 fatty acids to one molecule of
glycerol. Glycerol is an alcohol with 3 carbon atoms and 3 hydroxyl (-OH) groups which
can form ester bonds with carboxyl groups of fatty acids. A fatty acid consists of a long
unbranched hydrocarbon chain, usually 16 or 18 carbon atoms with a carboxyl group(-
COOH) at one end. The 3 fatty acids may all be the same in a single triglyceride.
Saturated fatty acids have no double bonds between carbon atoms. Unsaturated fatty
acids have one or more double bonds between carbon atoms which cause kinks in the
chains prevent them from packing closely together. This lowers the temperature at
which a lipid melts. Monounsaturated triglycerides have one double bond in their fatty
acids while polyunsaturated triglycerides have two or more double bonds.
(b)

A triglyceride is formed when 3 hydroxyls(-OH) groups of a single glycerol molecule

react with the carboxyl group (-COOH) of 3 fatty acids by forming ester bonds.
Triglycerides can be either saturated or unsaturated depending on the composition of
the fatty acid chains. Triglycerides function as a long-term storage form of energy in
human bonds. Because of the long carbon chains, triglycerides are nearly nonpolar
molecules and do not dissolve in polar solvents such as water.
Through a process known as lipolysis, triglycerides are broken down to release fatty
acids from monoacylglycerol in the intestine while simultaneously secreting lipases and
bile. The triglycerides can be reconstructed in the enterocytes to incorporate cholesterol
and proteins to form chylomicrons.
5.(a)

Cholesterol has hydrocarbon ring and hydrocarbon tail which are nonpolar and
hydrophobic. It has hydroxyl group is polar and hydrophilic. Cholesterol functions to
immobilize the outer surface of the membrane to reduce fluidity. It makes the
membrane less permeable to very small water-soluble molecules that would freely
cross.
(b) Cholesterol is a component of cell membranes that helps to maintain the fluidity of
the cell membrane. This can reduce membrane fluidity at high temperature by reducing
phospholipid movement. Cholesterol synthesized the bile which involved in metabolism
of lipid. It maintains the integrity and fluidity of cell membranes and to serve as a
precursor for the synthesis of substances that are vital for the organism including
steroid hormones, bile acids and vitamin D.

!.(a) Primary structure refers to the number, type and linear sequence of amino acids
which is joined by peptide bonds in the polypeptide with protein molecule. Peptide
bonds are responsile for primary structure.
Secondary structure refers to repeating coiled or folded pattern of polypeptide chain to
form localized structure. In polypeptide chains, some proteins are coiled to form -helix
while some are folded to form -pleated sheet. They are stabilized by intra-chain by
hydrogen bonds between peptide bonds along polypeptide backbone. Many hydrogen
bonds are formed between oxygen on carboxyl group of amino acid and hydrogen on
amino group of another amino acid.
Tertiary structure means that one polypeptide chain of secondary structure may further
coiled into a globular shape which is maintained by bonds and interactions among R
groups. The overall 3-D globular shape of a polypeptide are formed from the
interactions between R groups of amino acids or between R groups and polypeptide
backbone. Tertiary structure are maintained by 4 type of interactions between R groups
which are hydrogen bonds, ionic bonds, disulphide bridges and hydrophobic
interactions and Van der waals.
Quaternary structure are overall functional protein structure that results from the
aggregation of 2 or more polypeptide chain that arrange to form a functional protein.
Quaternary structure is composed of 2 or more polypeptide chains, interacting in
specific ways to form biologically active protein. Each polypeptide chain in a protein
which called a subunit are held together by hydrogen bond, hydrophobic interaction,
ionic bond and disulphide bridges.
(b) Hydrophobic interaction is one type of interaction that plays a major role in the
correct folding of a protein. As a polypeptide folds into its correct shape, amino acids
with nonpolar side chains usually cluster at core of protein, staying away from water.
Once the nonpolar amino acids have formed nonpolar core of the protein, weak van der
waals forces stabilize the protein. Furthermore, hydrogen bonds and ionic interactions
between polar, charged amino acids contribute to the tertiary structure.
2.(a) Globular proteins have coiled and folded polypeptide chains into globular shape
while fibrous proteins have long parallel polypeptide chains. Globular proteins have
globular structure maintained by hydrogen, ionic, disulphide bonds, hydrophobic
interactions and van der waals interactions while fibrous proteins have polypeptide
chains form helical structures or pleated sheets held by hydrogen bonds. In globular
proteins, tertiary structure determines ite metabolic functions while in fibrous proteins,
secondary structure most important in carrying out its structural and supporting
function. Globular proteins have relatively unstable structure while fibrous proteins
have stable structure. Globular proteins are usually soluble in water and can form
colloidal suspension while fibrous proteins are insoluble in water.
(b) Enzymatic proteins are biological catalyst that catalyses hydrolysis of complex food
to simple, soluble substances. Structural proteins provides structure and support to the
shape of the cells. Transport proteins are proteins that carry lipids in blood forming
liproprotein complexes. Hormonal proteins help in the coordination of body activities of
an organism. Receptor proteins acts as receptors for binding to hormone,
neurotransmitter. Storage proteins are storage of amino acids. Marker proteins act as
maker for cell in cell recognition. Nutritional proteins provide the body with essential
amino acids, nitrogen and sulfur.
(c) (i) egg albumen, haemoglobin
(ii) Simple proteins consist only of amino acids while conjugated proteins contain
protein and non-protein material (prosthethic group).
3.(a) A collagen molecule consists of 3 helical polypeptide chains wound around one
another and held by hydrogen bonds. The triple helices are joined together by covalent
bonds between the adjacent chains to form fibrils. The fibrils are then held together to
form thicker and stronger collagen fibres. It provides tendons and ligaments with tensile
strength and skin with elasticity.
(b) Haemoglobin is composed of 4 subunits each containing a cofactor known as haem
group that includes an iron atom center. The main component that binds with oxygen is
the iron. Each molecule of haemoglobin is capable of carrying 4 oxygen molecules. Each
subunits have one polypeptide chain and one heme group. All haemoglobin carry the
same prosthethic heme group iron protoporphyrin IX associated with a polypeptide
chain of 141(alpha) and 146(beta) amino acid residues.
(c) Haemoglobin is globular and has a tertiary structure while collagen is fibrous and lack
of a tertiary structure. Haemoglobin is a conjugated protein while collagen is a simple
protein. Haemoglobin has a functional role while collagen has a structural role.
4.(a) (i) Protein denaturation is the process in which protein loses is original shape due
to disruption of weak chemical bonds and interactions within a protein and become
biologically inactive. Protein renaturation is a process where a denatured proteins will
sometimes spontaneously refold into its original structure provided the physical and
chemical environment are restored to normal, with the denaturing agent removed.
(ii) Heat or radiation. Increased kinetic energy is supplied causing the atoms of protein
to vibrate violently; breaking the hydrogen ionic bonds. Coagulation of proteins occurs.
Strong acids and strong alkalis. Additional H+ ions in acids combine with COO- groups in
amino acids to form COOH. Reduced H+ ions in alkalis causes NH3+ groups in amino
acids to release H+ ions to the alkaline medium to form NH2. Ionic bonds are then
broken.
(b) (i) Protein is amphoteric molecule that have both basic and acidic group. Proteins are
amphoteric in water which means proteins can act either as acids or bases. Acidic part
consists of carboxyl group(-COOH) whle basic part consists of amino group(NH2).
(ii) Buffer resists the tendency to alter its pH even when small amounts of acids or alkalis
are added to it. It resists changes in acidity and alkalinity. The amino group and carboxyl
group in amino acids and proteins can act as buffer in aqueous solution to maintain the
pH of the body’s internal fluid.
(iii) Colloid are mixture made up of a liquid ad particles. Due to the particles large size
particles remain dispersed in liquid. Cytoplasm of cell acts as a colloidal system. Plasma
membrane are major colloids in blood plasma that cannot move across blood capillaries
and affect osmotic pressure of blood.