Protein Biomolecular Interactions MCQs

Welcome to our comprehensive collection of Multiple Choice Questions (MCQs) on Protein Biomolecular Interactions, a fundamental topic in the field of bioinformatics. Whether you're preparing for competitive exams, honing your problem-solving skills, or simply looking to enhance your abilities in this field, our Protein Biomolecular Interactions 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 Protein Biomolecular Interactions mcq questions that explore various aspects of Protein Biomolecular Interactions problems. Each MCQ is crafted to challenge your understanding of Protein Biomolecular Interactions principles, enabling you to refine your problem-solving techniques. Whether you're a student aiming to ace bioinformatics tests, a job seeker preparing for interviews, or someone simply interested in sharpening their skills, our Protein Biomolecular Interactions MCQs are your pathway to success in mastering this essential bioinformatics topic.

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Protein Biomolecular Interactions MCQs | Page 3 of 7

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Q21.
The linkers between the catalytic domain and the Rossmann domain were conserved in each family.

a.

True

b.

False

c.

May be True or False

d.

Can't say

Discuss
Answer: (a).True
Q22.
Across the different types of catalytic families, the position of the two domains with respect to one another varied, but only within a range of about ______

a.

20°

b.

10°

c.

90°

d.

80°

Discuss
Answer: (c).90°
Q23.
Experimentation is most desirable over computational methods by every means.

a.

True

b.

False

c.

May be True or False

d.

Can't say

Discuss
Answer: (b).False
Q24.
Interactions between proteins can be predicted computationally by looking for sets of genes that occur as a _______

a.

single gene in at least one genome

b.

multiple genes in at least one genome

c.

multiple genes in various genomes

d.

single gene in various genomes

Discuss
Answer: (a).single gene in at least one genome
Q25.
Which of the following is untrue about Electrostatic Complementarity?

a.

The electrostatic properties of biomolecules play an important role in determining interactions

b.

The burial of charged residues at protein-protein/DNA interfaces is thought to be generally net destabilizing with the hydrophobic effect being the primary driving force

c.

Charged groups involved in the biomolecular interface are often stabilized by other polar or oppositely charged groups on the interacting molecule

d.

Charged groups involved in the biomolecular interface are often stabilized by similar polar or same charged groups on the interacting molecule

Discuss
Answer: (d).Charged groups involved in the biomolecular interface are often stabilized by similar polar or same charged groups on the interacting molecule
Q26.
Proteins are dynamic entities that undergo _______

a.

only fluctuation of flexible loop regions about equilibrium positions when in solution

b.

only limited conformational change of amino acid side-chains when in solution

c.

both limited conformational change of amino acid side-chains and fluctuation of flexible loop regions about equilibrium positions when in solution

d.

illimitable or total conformational change of amino acid side-chains when in solution

Discuss
Answer: (c).both limited conformational change of amino acid side-chains and fluctuation of flexible loop regions about equilibrium positions when in solution
Q27.
Typical motions of proteins will be primarily treated by a rigid body model for docking.

a.

True

b.

False

c.

May be True or False

d.

Can't say

Discuss
Answer: (b).False
Q28.
In case of Protein-ligand docking, ______ ligands are often _____ in adapting their shape to fit the receptor binding pocket.

a.

small molecule, highly flexible

b.

large molecule, highly flexible

c.

large molecule, more flexible

d.

small molecule, less flexible

Discuss
Answer: (a).small molecule, highly flexible
Q29.
In Multiple conformation rigid-body method, a ligand is assumed to be able to adopt a number (N) of different _______ that are computed _____ the ligand being docked into the receptor.

a.

low-energy conformations, after

b.

low-energy conformations, prior to

c.

high-energy conformations, prior to

d.

high-energy conformations, after

Discuss
Answer: (b).low-energy conformations, prior to
Q30.
The disadvantage of Multiple conformation rigid-body method is that the active conformation may be missed as the result of a minor structural difference not considered in the ______ ligand conformations. Where, the N is the number of low-energy conformations.

a.

N +1

b.

N

c.

N²

d.

N/2

Discuss
Answer: (b).N
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