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 1 of 7

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Q1.
Which of the following is untrue about Amino acid conservation?

a.

It has been known for some time that conservation of residues at the surface of a protein family is often related to function

b.

Conservation of residues at the core of a protein family is often related to function

c.

This may be an enzyme active-site or binding site

d.

Unlike hydrophobicity or electrostatic potential, displaying residue conservation on the molecular surface has no physical or chemical basis

Discuss
Answer: (b).Conservation of residues at the core of a protein family is often related to function
Q2.
Which of the following is untrue about Shape Complementarity?

a.

The complementarity between two proteins or a protein and ligand can be described by surface contact or overlap

b.

The complementarity between two proteins or a protein and ligand can be described by the overall buried surface area of two molecules in contact

c.

The complementarity between two proteins or a protein and ligand can be described by the number of adjacent surface points (atoms or residues)

d.

The hydrophobic effect barely has impact on protein folding

Discuss
Answer: (d).The hydrophobic effect barely has impact on protein folding
Q3.
The burial of surface area (or the maximization of surface contact) is an approximation of the effect of shape complementarity.

a.

True

b.

False

c.

May be True or False

d.

Can't say

Discuss
Answer: (a).True
Q4.
Which of the following is untrue about Grid Representation?

a.

To speed up the matching process the topology of the protein can be simplified from atomic level detail to a series of cubic elements

b.

To speed up the matching process discretizing the 3-dimensional space using a grid is done

c.

Discretizing allows very fast computer matching using search methods such as Fourier transform

d.

Fourier transform is hardly used in computer matching

Discuss
Answer: (d).Fourier transform is hardly used in computer matching
Q5.
In Grid representation, in a translational scan the mobile molecule B moves through the grid representing the static molecule A and a signal describing shape complementarity, fc, is generated for each mapping. Mathematically the correlation function, fc, of fA and fB is given by ______ where N is the number of grid points along the cubic axes i, j, and k and α, β, and γ are the translational vectors of the mobile molecule B relative to the static one A.

a.

fc = \(\sum_{i=1,j=1,k=1}^N\) (fA,i,j,k * fBi+αj+βk+ɣ)

b.

fc = \(\sum_{i=0,j=0,k=0}^N\) (fA,i,j,k * fBi+αj+βk+ɣ)

c.

fc = \(\sum_{i=1,j=1,k=1}^N\) (fA,0,0,0 * fBi+αj+βk+ɣ)

d.

fc = \(\sum_{i=0,j=0,k=0}^N\) (f0,i,j,k * fBi+αj+βk+ɣ)

Discuss
Answer: (a).fc = \(\sum_{i=1,j=1,k=1}^N\) (fA,i,j,k * fBi+αj+βk+ɣ)
Q6.
In Grid representation, the lowest score represents the best surface complementarity for a given translational scan.

a.

True

b.

False

c.

May be True or False

d.

Can't say

Discuss
Answer: (b).False
Q7.
In Property-based measures, displaying physical properties on the molecular surface of molecules can help to guide molecular docking.

a.

True

b.

False

c.

May be True or False

d.

Can't say

Discuss
Answer: (a).True
Q8.
Which of the following is untrue about Hydrophobicity?

a.

The hydrophobic effect plays a dominant role in the folding of proteins

b.

Hydrophobic residues aggregate away from contact with water

c.

Hydrophobic residues aggregate to form hydrophobic cores with more polar residues

d.

Hydrophobic residues form the solvent accessible surface but restrict the solubility of the protein

Discuss
Answer: (d).Hydrophobic residues form the solvent accessible surface but restrict the solubility of the protein
Q9.
Oligomers are often obligate complexes meaning that the free-energy cost of dissociation is high and they exist as oligomers under physiological conditions.

a.

True

b.

False

c.

May be True or False

d.

Can't say

Discuss
Answer: (a).True
Q10.
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
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