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2-Example-Test-Questions-To Answer-First

This document contains instructions for a 30-minute in-semester biochemistry test consisting of 20 multiple choice questions. Students are provided with a data sheet on amino acids and instructed to fill out their identifying information on an answer sheet and choose one answer for each question using a pencil or pen. The test covers topics such as enzyme kinetics, protein structure, and amino acid properties.

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shaheen
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© © All Rights Reserved
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23 views

2-Example-Test-Questions-To Answer-First

This document contains instructions for a 30-minute in-semester biochemistry test consisting of 20 multiple choice questions. Students are provided with a data sheet on amino acids and instructed to fill out their identifying information on an answer sheet and choose one answer for each question using a pencil or pen. The test covers topics such as enzyme kinetics, protein structure, and amino acid properties.

Uploaded by

shaheen
Copyright
© © All Rights Reserved
Available Formats
Download as PDF, TXT or read online on Scribd
You are on page 1/ 6

This question paper must be Name:………………………………...

returned. Candidates are not


permitted to remove any part Student No.:………………………….
of it from the examination room.

IN-SEMESTER TEST 2018

CBMS201/CBMS621 Biochemistry and Cell Biology

Time allowed: 30 minutes

Total number of questions: 20 multiple choice questions only.


(Note that the paper is printed on both sides)

Total marks: 20 (1 mark for each question): 10% of the final assessment.

Instructions:
1. Non-programmable calculators may be used. No other materials allowed.

2. A data sheet has been provided – please return the question paper intact.

3. ANSWER ALL QUESTIONS, CHOOSING THE BEST ANSWER FOR EACH.

4. ANSWER THE QUESTIONS ON THE GENERAL PURPOSE ANSWER


SHEET PROVIDED USING EITHER
 2B PENCIL (PREFERRED, OR
 BLUE or BLACK PEN.

5. FILL IN YOUR NAME IN THE "NAME" SECTION

6. FILL IN YOUR STUDENT NUMBER IN THE "IDENTIFICATION NUMBER"


SECTION.

7. FILL COMPLETELY ONE OF THE FIVE OVALS FOR QUESTIONS 1-20.


DATA SHEET: AMINO ACIDS

2
IN ANSWERING QUESTIONS 1-4, REFER TO THE STRUCTURE OF THE
FULLY PROTONATED TRIPEPTIDE SHOWN AND THE DATASET PROVIDED.

The pKa values of the


ionizable groups on this
tripeptide are:
i. -COOH = 2.4
ii. -NH2 = 10.8
iii. R group of the middle residue = 4.0

1. What is the primary sequence of the tripeptide using the three letter amino acid
code?
A. Met-Glu-Gly
B. Met-Gln-Ala
C. Cys-Glu-Ala
D. Met-Glu-Gly
E. Cys-Gln-Ala

2. Based on the pKa values provided, the average charge on each ionizable group at
pH 7.0 are:
A. -COOH = -1, -NH2 = +1, R group of the middle residue = 0
B. -COOH = -1, -NH2 = +1, R group of the middle residue = -0.5
C. -COOH = 0, -NH2 = +1, R group of the middle residue = -0.5
D. -COOH = -1, -NH2 = +1, R group of the middle residue = -1
E. -COOH = -1, -NH2 = +0.5, R group of the middle residue = -1

3. Using the pKa values given, what is the pI of this tripeptide?


A. 6.4
B. 4.0
C. 3.2
D. 2.4
E. 1.2

4. Carboxypeptidease can be used to cleave this tripeptide specifically at the peptide


bond:
A. Glu-Gly
B. Glu-Ala
C. Gln-Ala
D. Met-Glu
E. Cys-Glu.

3
5. Which of the following statements is NOT true about enzyme regulation?
A. The activity of an enzyme is covalently affected by allosteric regulators.
B. The reaction rate slows as equilibrium is approached.
C. Enzymes can be inactivated by the addition of a functional group.
D. Enzymes can be inhibited by the products they produce.
E. Coenzyme and substrate availability can regulate enzyme reaction rate.

6. Treatment of any protein with dansyl chloride allows the determination of:
A. the amino acid sequence from the N-terminus.
B. the amino acid sequence from the C-terminus.
C. the disulfide linkages present in the protein.
D. the N-terminal amino acid.
E. the C-terminal amino acid.

7. Oxamate is a structural analogue of pyruvate and inhibits the enzyme L-lactate


dehydrogenase (LDH), by binding to the active site. This is an example of:
A. competitive inhibition.
B. noncompetitive inhibition.
C. uncompetitive inhibition.
D. mixed mode inhibition.
E. none of the above.

8. In an uncompetitive inhibition by a substrate analogue, compared to the normal


reaction, the kinetic parameters show the following changes
A. Km is the same; Vmax is lower and Km/Vmax increases.
B. Km is lower; Vmax is lower and Km/Vmax is the same.
C. Km is higher; Vmax is the same and Km/Vmax increases.
D. Km is the same; Vmax is higher and Km/Vmax decreases.
E. Km; Vmax and Km/Vmax are the same.

9. Inhibitor X binds to an enzyme at a site different to the active site. What is the
best description of the nature of this inhibition?
A. competitive inhibition.
B. noncompetitive inhibition.
C. uncompetitive inhibition.
D. B and C.
E. B or C.

4
REFER TO THE FOLLOWING INFORMATION TO ANSWER QUESTIONS 10-13.
You are given an octapeptide (peptide with 8 residues) with the sequence:
in one letter code: AVGWRVKS or
in three letter code: Ala-Val-Gly-Trp-Arg-Val-Lys-Ser
and two enzymes with protease activity: trypsin and chymotrypsin.
10. How many fragment peptides will trypsin digestion of the octapeptide generate?
A. 1
B. 2
C. 3
D. 4
E. 5.

11. Following trypsin digestion, what would be the best method to separate the
resulting peptides?
A. Salting-in
B. Ultracentrifugation
C. Gel electrophoresis.
D. Gel-filtration chromatography
E. Ion exchange chromatography

12. How many fragment peptides will chymotrypsin digestion of the octapeptide
generate?
A. 1
B. 2
C. 3
D. 4
E. 5.

13. Following chymotrypsin digestion, what would be the best method to separate
the resulting peptides?
A. Salting-in
B. Ultracentrifugation
C. Gel-filtration chromatography
D. Ion exchange chromatography
E. Gel electrophoresis.

14. Cyanogen bromide is an enzyme that cleaves proteins on:


A. the carboxyl side of Met amino acid residue
B. the carboxyl side of Cys or Met amino acid residues
C. the amino side of Met amino acid residue
D. the amino side of Cys or Met amino acid residues
E. none of the above as cyanogen bromide has no protease activity.

5
15. Which amino acid has a side-chain with a pKa near 7, and is therefore often
involved in general acid-base catalysis?
A. arginine.
B. histidine.
C. Lysine.
D. aspartate.
E. glutamate.
16. What is the zeroth level of protein structure?
A. the amino acid sequence of the protein.
B. the arrangement of secondary structural elements in a single polypeptide chain.
C. the arrangement of subunits in a multisubunit protein.
D. the arrangement of the protein backbone into secondary structural units.
E. the amino acid composition of a protein.

17. What is the quaternary structure of a protein?


A. the amino acid sequence of the protein.
B. the arrangement of secondary structural elements in a single polypeptide chain.
C. the arrangement of subunits in a multisubunit protein.
D. the arrangement of the protein backbone into secondary structural units.
E. the amino acid composition of a protein.

18. ALL types of enzymes carry out catalysis of biochemical reactions by


A. providing an alternate reaction pathway.
B. increasing the spontaneity (G) of the reaction.
C. lowering the activation energy of the reaction.
D. altering the concentration of the reactants to achieve a favourable G
E. selecting only the forward reaction, from reactants to products.

19. Which one of the following is NOT a feature of enzymes?


A. regulation.
B. catalytic activity.
C. specifity.
D. active site.
E. ability to change G of the reaction.

20. Enzyme active sites have the greatest complementarity to:


A. substrate.
B. product.
C. both substrate and product.
D. transition state.
E. allosteric modulator.

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