Practice Questions

The induced-fit model proposes that an enzyme active site is

A. Completely rigid
B. Flexible and changes shape after substrate binding
C. Formed only after ATP binding
D. Located outside the protein

Substrate binding induces conformational changes that optimize catalysis.

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Jun 29, 2026

Myoglobin is especially suited for

A. Oxygen transport
B. Oxygen storage in muscle
C. Carbon dioxide transport
D. Electron transport

Myoglobin has a high oxygen affinity and releases oxygen only at low oxygen tension.

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Jun 29, 2026

pI = (2.34 + 9.60)/2 = 5.97.

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Jun 29, 2026

Vitamin C deficiency causes scurvy because it prevents

A. Peptide bond formation
B. α-Helix formation
C. Hydroxylation of proline, destabilizing collagen
D. Protein synthesis

Hydroxyproline stabilizes the collagen triple helix through hydrogen bonding.

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Jun 29, 2026

Protein concentration is commonly estimated by measuring absorbance at

A. 260 nm
B. 280 nm
C. 340 nm
D. 540 nm

Tryptophan and tyrosine absorb ultraviolet light strongly near 280 nm.

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Jun 29, 2026

Anfinsen’s experiment demonstrated that

A. Chaperones are always required
B. Primary sequence contains all information for protein folding
C. ATP is needed for protein folding
D. Disulfide bonds determine sequence

RNase A spontaneously refolded after denaturation, proving sequence determines structure.

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Jun 29, 2026

The coiled-coil structure of α-keratin is stabilized mainly by

A. Peptide bonds
B. Hydrogen bonds with water
C. Hydrophobic interactions between helices
D. Glycosidic bonds

Hydrophobic residues at heptad repeat positions interlock to stabilize the coiled-coil.

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Jun 29, 2026

Amphipathic α-helices are commonly found

A. Buried inside globular proteins
B. Spanning membranes or lining channels
C. In collagen
D. In silk fibroin

Amphipathic helices possess hydrophobic and hydrophilic faces suited for membrane environments.

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Jun 29, 2026

A protein domain is considered part of the

A. Primary structure
B. Secondary structure
C. Tertiary structure
D. Quaternary structure

Domains are independently folded structural units within one polypeptide.

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Jun 29, 2026

The hydrophobic effect in protein folding is primarily driven by an increase in the

A. Protein enthalpy
B. Entropy of surrounding water
C. Number of peptide bonds
D. Salt concentration

Burying hydrophobic residues releases ordered water molecules, increasing entropy.

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Jun 29, 2026
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