QUESTION 2

B) State an example of coenzyme.

NAD (nicotineamideadenine dinucleotide), NADP (nicotineamide adenine dinucleotide
phosphate) and FAD (flavin adenine dinucleotide).
C) Induced fit model in enzymatic reactions.
The active site of an enzyme will undergo a conformational change when binding a substrate, to
improve the fit.
D) Given are two Km values: 4.5mM and 10mM. Elucidate which Km produces higher
affinity of substrate to enzyme.
High values of Km correspond to low enzyme affinity for substrate. Low Km values for an
enzyme correspond to high affinity for substrate. 4.5mM produces higher affinity of a substrate
to enzyme compared to 10mM.
E) The urea cycle excretes excess nitrogen from animals back to the environment. Give
the name of a compound that is linked to the TCA cycle.
Fumarate
F) By using the chemical structure of zwitterions, explain the reaction on the zwitterions
if the pH of the solution is increased.
In basic solution high pH, amino acids zwitterions lose proton from their acidic groups to leave
only negatively charged groups.

G) Compare ion exchange chromatography and affinity chromatography.

QUESTION 3
A) State the monomer of carbohydrates.
Glucose, Galactose, Fructose

B) Give examples of disaccharide.

Maltose, Lactose, Sucrose.

C) Describe fate of pyruvate during vigorous exercise.

In vertebrates under anaerobic conditions, the most important pathway for the regeneration
of NAD+ is reduction of pyruvate to lactate. Lactate dehydrogenase is a tetrametric
isoenzyme consisting of H and M subunit; H4 predominates in heart muscle, and M4 is
skeletal muscle.
While lactate fermentation allows glycolysis to continue, it increases the concentration of
lactate and also of H+ in muscle tissue. When blood lactate reaches about 0.4mg/100mL,
muscle tissue becomes almost completely exhausted.
D) Glucose has a chemical formula C6H12O6. Illustrate the Haworth projection of B-D-
Glucose.

E) Distinguish between amylose and glycogen.

Amylose is a continuous, unbranched chain of up to 4000 a-D-glucose units joined by a-1,4-
glycosidic bonds.
Glycogen is a branched chain polymer of a-D-glucose like amylopectin. Consists of a chain
of a-1,4-glycosidic bonds and branches created by a-1,6-glycosidic bond.
F) Illustrate the TCA cycle.

QUESTION 4
A) Illustrate the triacylglycerol structure.

B) Two questions
a. State the classes of lipids.
Triglyceride, phosphoacylglycerol, sphingolipids, waxes, terpenes, and steroids.
b. Briefly describe unsaturated fatty acids.
Hydrocarbons contain at least one double bond. Double bond will produce kinks
in the fatty acid. Example: palmitoleic acid and oleic acid.
 C) Explain the consequences for a person who undergoes Atkin’s diet (high in lipid,
low in carbohydrate)

D) Biological membranes possess fluid properties which depend on the composition

of the bilayer.
a. Illustrate a simple diagram to represent a lipid bilayer membrane. Label the
hydrophobic and hydrophilic portion of the membrane.

Hydrophobic – inside
Hydrophilic – outside

b. Compare the functional groups between the hydrophilic and hydrophobic

portions of the membrane.
Hydrophilic – polar (carboxyl group)
Hydrophobic – nonpolar (methyl group)

QUESTION 5
A) Two questions
a. Define codon and anticodon.
Codon is a three base sequence on the mRNA molecule that provides the code
for a particular amino acid. Codon is from mRNA.
Anticodon is a three base sequence on the transfer RNA molecule that is
complementary to mRNA codon. Anticodon is from tRNA.

b. State one of the stop codons.

UAG, UAA or UGA.

B) Find the complete base composition of double-stranded eukaryotic DNA that

contains 28% adenine.
If 28% are adenine, then 28% must also be thymine. 28+28=56%. So 100-56 gives you
the remaining percentage which = 44% this must be split between cytosine and guanine
which therefore are 22% each.
C) Describe the steps in RNA translation.
 Initiation – amino acids are activated and covalently bonded to the tRNA to formed
aminoacyl-tRNA. Aminoacyl-tRNA bound to the mRNA at the site encodes the start
of polypeptide synthesis. mRNA and the ribosomes are bound to each other.
 Chain elongation – Aminoacyl-tRNA forms a complex with ribosome and mRNA. A
peptide bind is formed between the first and second amino acids. First tRNA
molecule breaks away and moves back into the cytoplasm. The ribosome move
along the mRNA strand, one codon at a time, leading to the placement of the correct
amino acid in position on the growing polypeptide chain.
 Termination – When a stop codon is reached, translation ceases and the polypeptide
chain is completed and released from ribosome. Many ribosomes can move along
the same mRNA molecule leading to the synthesis of large numbers of polypeptide
chains in a short period of time. All stages requires enzymes and a source of energy.