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 13 of 31

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Q121.
For the unfolding reaction of Protein G, ฮ”H° =210.6 kJ/mol, this means that

a.

unfolding is favored enthalpically

b.

folding is favored enthalpically

c.

the entropy is positive at all temperatures

d.

the entropy is negative at all temperatures

Discuss
Answer: (b).folding is favored enthalpically
Q122.
Attractive Vander Waals forces occur between

a.

apolar molecules in the liquid state

b.

any pair of nearby atoms

c.

polar molecules in the solid state

d.

only if other forces are less favorable

Discuss
Answer: (b).any pair of nearby atoms
Q123.
Which of the following forces is the most favorable for protein folding?

a.

Conformational entropy

b.

Hydrophobic Interactions

c.

Vander Waals interactions

d.

Hydrogen bonds

Discuss
Answer: (b).Hydrophobic Interactions
Q124.
At the midpoint of a temperature transition curve,

a.

half of the protein is denatured

b.

Keq = 1.0 and ฮ”G = 0

c.

[Native] = [Unfolded]

d.

All of these

Discuss
Answer: (d).All of these
Q125.
Buried hydrophobic side chains in a globular protein fit into a hole formed by the side chains of

a.

1-3 other amino acids

b.

5-7 other amino acids

c.

9-12 other amino acids

d.

13-15 other amino acids

Discuss
Answer: (b).5-7 other amino acids
Q126.
Which of the following is the most correct?

a.

Charged amino acids are never buried in the interior of a protein

b.

Charged amino acids are seldom buried in the interior of a protein

c.

All hydrophobic amino acids are buried when a protein folds

d.

Tyrosine is only found in the interior of proteins

Discuss
Answer: (b).Charged amino acids are seldom buried in the interior of a protein
Q127.
Which of the following forces is the most unfavorable for protein folding?

a.

Conformational entropy

b.

Hydrophobic interactions

c.

Vander Waals interactions

d.

Electrostatic interactions

Discuss
Answer: (a).Conformational entropy
Q128.
Since ฮ”G° = -RTlnK

a.

a 10-fold increase in K decreases ฮ”G° by about 10-fold

b.

a 10-fold decrease in K decreases ฮ”G° by about 2.3*RT

c.

a 10-fold increase in K decreases ฮ”G° by about 2.3*RT

d.

a 10-fold decrease in K increases ฮ”G° by about 10-fold

Discuss
Answer: (c).a 10-fold increase in K decreases ฮ”G° by about 2.3*RT
Q129.
The correlation between free energy ฮ”G transfer between the aqueous/organic phases and the surface area of amino acid residues

a.

reflects the reduction in solvent-accessible area during protein folding

b.

is only meaningful for the polar amino acids

c.

ignores the important contribution of the peptide bond

d.

is similar to effects seen with SDS denaturation

Discuss
Answer: (a).reflects the reduction in solvent-accessible area during protein folding
Q130.
If the egg white protein, ovalbumin, is denatured in a hard-boiled egg, then which of the following is least affected?

a.

The primary structure of ovalbumin

b.

The secondary structure of ovalbumin

c.

The tertiary structure of ovalbumin

d.

The quaternary structure of ovalbumin

Discuss
Answer: (a).The primary structure of ovalbumin
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