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Exam 11 October 2009, questions

Introduction to Biochemistry and Microbiology (University of KwaZulu-Natal)

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UNIVERSITY OF KWAZULU-NATAL (WESTVILLE CAMPUS)

DEGREE EXAMINATIONS: NOVEMBER 2007
SCHOOL OF BIOCHEMISTRY, GENETICS, MICROBIOLOGY AND PLANT PATHOLOGY

BIMI120 : INTRODUCTORY BIOCHEMISTRY AND MICROBIOLOGY

SECTION A : BIOCHEMISTRY

TIME: 90 minutes EXAMINERS : Prof. M. Ariatti MARKS: 100

Prof. [Link]
Dr. M. Singh
Dr. B. Masola
Mr. P. Govender
MODERATOR : Dr. C. Niesler

INSTRUCTIONS :
♦ ANSWER 5 QUESTIONS ONLY.
♦ STRUCTURES TO BE INCLUDED IN YOUR ANSWER UNLESS OTHERWISE STATED.

QUESTION 1: 20 MARKS

a) Give the complete unabbreviated name for the tetrapeptide gly-cys-ser-trp. Name the N
and C terminal amino acids. [3]

b) What do you understand by the term zwitterion? Give its structure. [3]

c) List five biological functions of proteins and give an example for each. [5]

d) Define the following terms:

i. primary protein structure
ii. nucleoside [2]

d) Describe five important features of the DNA double helix and name two forces that
stabilize this helix. [7]

QUESTION 2 ON PAGE 2/….

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QUESTION 2: 20 MARKS

a) Name and give the shorthand notations of one saturated fatty acid, and one unsaturated
fatty acid. [2]

b) Why is the triglyceride from plant seeds usually liquid whilst triglyceride in animal fat is
usually solid? [2]

c) Which lipids are the main components of biological membranes? With the aid of
illustrations, explain why you think they are suited for inclusion in biological membranes.
[4]
d) The structure of cholesterol contains: (Indicate correct answer in answer booklet)
i. a carboxyl group and four fused rings
ii. one hydroxyl group and four fused rings, one of which is a cyclopentano ring.
iii. one hydroxyl group and three fused rings, one of which is a cycloheptano ring.
iv. two hydroxyl groups and three fused rings . [2]

e) Glucose is: (Indicate correct answer in answer booklet)

i. found at the non-reducing end of lactose
ii. a hexose and a ketose
iii. a hexose and an aldose
iv. a pentose and an aldose. [2]

f) Draw the β-anomer of maltose. [2]

g) Define the term ‘heteroglycan’. [2]

h) Compare and contrast the structures of amylose and glycogen. [4]

QUESTION 3: 20 MARKS

a) Discuss the role of the following nucleic acid sequences in protein synthesis :
i. template strand of DNA
ii. triplet codons of mRNA
iii. tRNA anticodon
iv. tRNA 3’ CCA stem
v. mRNA codons UAG, UAA, or UGA. [10]

b) What do you understand by the concept “gene cloning”? [10]

QUESTION 4 ON PAGE 3/….

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QUESTION 4: 20 MARKS

a) Briefly outline the fate of dietary carbohydrates. [5]

b) Give two reactions in glycolysis in which ATP is synthesized? [5]

c) List the two main products of glycolysis (excluding ATP) indicating how much of each
product is produced per molecule of glucose. [3]

d) Give details of the reaction that links glycolysis and the Kreb’s cycle (also known as
the Citric acid cycle or tricarboxylic acid cycle). [3]

e) Name four major products of the Kreb’s cycle. [2]

f) Under anaerobic conditions pyruvate is not oxidized by the Kreb’s cycle. What then is its
metabolic fate? [2]

QUESTION 5: 20 MARKS

a) Define the first law of thermodynamics and indicate its relevance to biochemical
processes. [4]

b) Define the following:

(i) Gibb’s free energy
(ii) Exergonic reaction. [3]

c) Give an equation that one can use to calculate the Gibb’s free energy change (∆G) for a
biochemical reaction under non standard conditions. Indicate what information the value
of ∆G gives about the reaction. [5]

d) Give two reasons for why certain biochemical compounds have high energy (or high
group transfer potential). [4]

e) State the function of the electron transport chain. [4]

QUESTION 6 ON PAGE 4/….

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QUESTION 6: 20 MARKS

Write down the letter corresponding to the correct answer in your answer book.

1. Enzyme biocatalysts can be

(A). Lipid
(B). RNA
(C). DNA
(D). Protein
(E). B and D only [2]

2. The x-ray structure of which enzyme was the first to be elucidated in 1965.
(A). Urease
(B). Pepsin
(C). Carboxypeptidase
(D). Amylase
(E). Lysozyme [2]

3. The free energy of activation (∆G‡) is,

(A). the difference between the substrate and the transition state.
(B). the difference between the product and the transition state.
(C). the difference between the substrate and the product.
(D). All of the above
(E). None of the above. [2]

4. Isomerases and hydrolases are numerically listed respectively by the International Enzyme
Commission as,
(A). Classes 6 and 3
(B). Classes 4 and 6
(C). Classes 1 and 2
(D). Classes 5 and 3
(E). Classes 2 and 5 [2]

5. Which class of enzymes catalyzes bond formation between two substrate molecules? The
energy for these reactions is usually supplied by the hydrolysis of ATP.
(A). Lyases
(B). Hydrolases
(C). Transferases
(D). Oxidoreductases
(E). Ligases [2]

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6. An esterase and epimerase belong to the following classes of enzymes respectively.

(A). Transferases and isomerases
(B). Hydrolases and isomerase
(C). Oxidoreductases and lyases
(D). Hydrolases and ligases
(E). Isomerases and hydrolases [2]

7. The following applies to the induced-fit model of enzyme-substrate recognition.

(A). also referred to as dynamic recognition and only the substrate is distorted.
(B). also referred to as dynamic recognition and only the enzyme is distorted.
(C). also referred to as static recognition and both the enzyme and substrate are distorted.
(D). also referred to as static recognition and only the enzyme is distorted..
(E). also referred to as dynamic recognition and both the enzyme and substrate are
distorted [2]

8. NADP+ is a cofactor that is classified as a,

(A). Cosubstrate
(B). Prosthetic group
(C). Metal ion of metalloenzymes
(D). Activator ion
(E). None of the above [2]

9. Prosthetic groups are a subclass of coenzymes that are,

(A). Organic nonprotein chemical factors that are noncovalently bonded to an enzyme.
(B). Inorganic nonprotein chemical factors that are noncovalently bonded to an enzyme.
(C). Organic nonprotein chemical factors that are covalently bonded to an enzyme.
(D). Inorganic nonprotein chemical factors that are covalently bonded to an enzyme.
(E). None of the above. [2]

10. Enzymatic reactions generally occur under the following conditions.

(A). 55°C, alkaline pH and atmospheric pressure.
(B). 37°C, neutral pH and atmospheric pressure.
(C). 17°C, neutral pH and low pressure.
(D). 27°C, acidic pH and high pressure.
(E). None of the above [2]

END OF PAPER

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