Amino Acids,Peptides and Proteins MCQs

Welcome to our comprehensive collection of Multiple Choice Questions (MCQs) on Amino Acids,Peptides and Proteins, a fundamental topic in the field of Biochemistry. Whether you're preparing for competitive exams, honing your problem-solving skills, or simply looking to enhance your abilities in this field, our Amino Acids,Peptides and Proteins MCQs are designed to help you grasp the core concepts and excel in solving problems.

In this section, you'll find a wide range of Amino Acids,Peptides and Proteins mcq questions that explore various aspects of Amino Acids,Peptides and Proteins problems. Each MCQ is crafted to challenge your understanding of Amino Acids,Peptides and Proteins principles, enabling you to refine your problem-solving techniques. Whether you're a student aiming to ace Biochemistry tests, a job seeker preparing for interviews, or someone simply interested in sharpening their skills, our Amino Acids,Peptides and Proteins MCQs are your pathway to success in mastering this essential Biochemistry topic.

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Amino Acids,Peptides and Proteins MCQs | Page 10 of 31

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Q91.
Affinity chromatography deals with the

a.

specific binding of a protein constituents for another molecule

b.

protein - protein interaction

c.

protein - carbohydrate interaction

d.

none of the above

Discuss
Answer: (a).specific binding of a protein constituents for another molecule
Q92.
A purified protein sample contains 10 ฮผg of protein and has an enzyme activity of 1 m mole of ATP synthesized/sec (1 unit). What is the specific activity of the final purified sample?

a.

1,000 units/mg

b.

10,000 units/mg.

c.

100,000 units/mg

d.

1,000,000 units/mg

Discuss
Answer: (c).100,000 units/mg
Q93.
Proteins separation can be carried out on the basis of

a.

net charge

b.

solubility in salt solutions

c.

size or mass

d.

all of these

Discuss
Answer: (d).all of these
Q94.
The best way to determine the location of protein in the purification scheme is to measure the

a.

rate of ATP synthesis

b.

changes in the refractive index

c.

UV absorption

d.

mass spectroscopy of the protein

Discuss
Answer: (a).rate of ATP synthesis
Q95.
The conformational changes from the T to the R state is initiated by

a.

binding of oxygen to the heme

b.

movement of the proximal histidine towards the heme

c.

movement of the F-helix, which contains the proximal His

d.

reorganization of protein-protein contacts between the individual subunits

Discuss
Answer: (a).binding of oxygen to the heme
Q96.
An allosteric activator

a.

increases the binding affinity

b.

decreases the binding affinity

c.

stabilizes the R state of the protein

d.

both (a) and (c)

Discuss
Answer: (d).both (a) and (c)
Q97.
Bisphosphoglycerate (BPG) cannot bind to the oxygenated R state of hemoglobin because

a.

it is displaced from the heme by oxygen

b.

it is displaced from the heme by movement of the proximal histidine

c.

its binding pocket becomes too small to accommodate BPG

d.

BPG binds to the R state with the same affinity as the T state

Discuss
Answer: (c).its binding pocket becomes too small to accommodate BPG
Q98.
The Hill coefficient (nH) for myoglobin and hemoglobin are respectively

a.

2.8 and 1.0

b.

1.0 and 2.8

c.

1.2 and 4.5

d.

4.5 and 1.2

Discuss
Answer: (b).1.0 and 2.8
Q99.
When protein binds two ligands in a non-cooperative manner, then the x-intercept of the Scatchard Plot is

a.

1

b.

2

c.

not defined

d.

none of the above

Discuss
Answer: (b).2
Q100.
Oโ‚‚ binding to hemoglobin results in

a.

100-fold higher affinity for the last Oโ‚‚ bound than for the first

b.

extensive protein conformational change

c.

both (a) and (b)

d.

100-fold lower affinity for the last Oโ‚‚ bound than for the first

Discuss
Answer: (c).both (a) and (b)
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