Urea acts as a strong denaturant of proteins as it
(1) perturbs electrostatic interactions only
(2) perturbs hydrophobic interactions only
(3) perturbs hydrophobic interactions as well as binds
to peptide groups
(4) perturbs hydrophobic interactions as well as binds
to nonpolar side chains
The correct answer is:
(3) Urea perturbs hydrophobic interactions as well as binds to peptide groups
Explanation:
- Urea is a strong denaturant because it disrupts both hydrophobic interactions and hydrogen bonds in proteins.
- It breaks hydrophobic interactions by increasing the solubility of nonpolar residues, making them more exposed to water.
- Additionally, urea binds to peptide groups, disrupting hydrogen bonding that stabilizes protein secondary structures like α-helices and β-sheets.
Why other options are incorrect:
- (1) Perturbs electrostatic interactions only → Urea affects more than just electrostatic interactions; it also affects hydrogen bonding and hydrophobic forces.
- (2) Perturbs hydrophobic interactions only → Urea also binds to peptide groups, affecting hydrogen bonds.
- (4) Perturbs hydrophobic interactions as well as binds to nonpolar side chains → Urea primarily interacts with peptide groups rather than nonpolar side chains.
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