Protein Structure, Folding and Function - Structure and Function of Biomolecules - Life Sciences Previous Year Questions

1

2008 · Life Sciences · Structure and Function of Biomolecules · Protein Structure, Folding and Function

Life Sciences (XL) 2008

Zinc fingers are characteristics of

A

blood clotting proteins

B

RNA chaperones

C

DNA binding proteins

D

lysosomal hydrolases

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2

2011 · Life Sciences · Structure and Function of Biomolecules · Protein Structure, Folding and Function

Life Sciences (XL) 2011

Collagen, α-keratin and tropomyosin have common structural features. They are P) disulfide bridges to neighboring proteins. Q) repeating sequences of amino acids R) a high β-sheet content S) superhelical coiling

A

P, Q

B

Q, R

C

Q, S

D

P, R

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3

2011 · Life Sciences · Structure and Function of Biomolecules · Protein Structure, Folding and Function

Life Sciences (XL) 2011

Which of the following amino acid change (mutation) would MOST adversely affect the structure of an α-helix?

A

A valine residue changed to an isoleucine residue

B

A methionine residue changed to a proline residue

C

An aspartic acid residue changed to a glutamic acid residue

D

A histidine residue changed to an arginine residue

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4

2012 · Life Sciences · Structure and Function of Biomolecules · Protein Structure, Folding and Function

Life Sciences (XL) 2012

Which one of the following pairs of amino-acids in the protein has high propensity to take up the α-helix conformation?

A

Gly-Asp

B

Pro-His

C

Gly-Pro

D

Ala-Arg

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5

2012 · Life Sciences · Structure and Function of Biomolecules · Protein Structure, Folding and Function

Life Sciences (XL) 2012

Which one of the following closely defines ‘Molten Globule’ state of a protein?

A

State with high degree of secondary structure and loss of tertiary structure

B

State with complete loss of secondary structure

C

Completely unfolded state

D

Loss of quaternary structure

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6

2013 · Life Sciences · Structure and Function of Biomolecules · Protein Structure, Folding and Function

Life Sciences (XL) 2013

Which one of the following amino acids has a higher propensity for cis peptide bond formation?

A

Histidine

B

Cysteine

C

Glycine

D

Proline

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7

2013 · Life Sciences · Structure and Function of Biomolecules · Protein Structure, Folding and Function

Life Sciences (XL) 2013

The length of an \(\alpha\)-helix composed of 36 amino acid residues is

A

10 Å

B

54 Å

C

27 Å

D

360 Å

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8

2019 · Life Sciences · Structure and Function of Biomolecules · Protein Structure, Folding and Function

Life Sciences (XL) 2019

A protein in denatured state (D) is in equilibrium with native state (N).
D ⇌ N
At 360 K, both N and D states are equally populated. If the standard entropy change for the reaction at this temperature ΔS° = -139 J K⁻¹ mol⁻¹, then the corresponding standard enthalpy change ΔH° for the reaction in kJ mol⁻¹ (rounded off to one decimal place) is ____

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9

2019 · Life Sciences · Structure and Function of Biomolecules · Protein Structure, Folding and Function

Life Sciences (XL) 2019

The crystal structure of a peptide has an ordered structural repeat of amino acids with a distance of ~ 6.5 Å between the alternate Cα atoms. Which one of the following pair of dihedral angles (Φ and Ψ) accurately represents the peptide structure?

A

Φ ≈ -60°, Ψ ≈ -50°

B

Φ ≈ -120°, Ψ ≈ -50°

C

Φ ≈ -60°, Ψ ≈ +120°

D

Φ ≈ -120°, Ψ ≈ +120°

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10

2019 · Life Sciences · Structure and Function of Biomolecules · Protein Structure, Folding and Function

Life Sciences (XL) 2019

The dipeptide with least rotational barrier in the peptide bond is

A

Option A

B

Option B

C

Option C

D

Option D

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11

2020 · Life Sciences · Structure and Function of Biomolecules · Protein Structure, Folding and Function

Life Sciences (XL) 2020

One mole of a native protein upon N-terminal analysis yielded one mole each of Asp and Val. Therefore, the protein in its native state exists as a

A

Monomer

B

Homo-dimer

C

Hetero-dimer

D

Tetramer

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12

2022 · Life Sciences · Structure and Function of Biomolecules · Protein Structure, Folding and Function

Life Sciences (XL) 2022

Which among the following statements are true with respect to protein denaturation?

A

There may be an increase in α-helix and β-sheet structure

B

It is an irreversible process

C

When fully denatured, globular proteins resemble a random coil

D

The peptide bonds are broken

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13

2024 · Life Sciences · Structure and Function of Biomolecules · Protein Structure, Folding and Function

Life Sciences (XL) 2024

A newly identified viral protein contains one long α-helix spanning 60 amino acid residues. The number of main chain H-bonds formed in this helix is __________.
(Answer in integer)

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14

2026 · Life Sciences · Structure and Function of Biomolecules · Protein Structure, Folding and Function

Life Sciences (XL) 2026

The following diagram represents energy states of different protein folding steps, which includes-
1. Folded
2. Transition
3. Molten globule
4. Unfolded
[Diagram: Energy vs Conformational states, with points P, Q, R, S]
Find the correct match of folding steps (1 to 4) with the energy state (P to S) in the diagram.

A

1-S, 2-R, 3-Q, 4-P

B

1-S, 2-R, 3-P, 4-Q

C

1-R, 2-Q, 3-S, 4-P

D

1-P, 2-Q, 3-R, 4-S

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15

2026 · Life Sciences · Structure and Function of Biomolecules · Protein Structure, Folding and Function

Life Sciences (XL) 2026

In a α-helix, the R-groups on the amino acid residues

A

are found on the outside of the helix

B

participate in the backbone H-bonding that stabilize the helix

C

allow formation of right-handed helices

D

allow formation of left-handed helices

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