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BIO NMDCAT BIOLOGICAL MOLECULES
nmdcat.online June 27, 2026

When a protein is subjected to extreme pH or high temperature, the disruption of its functional three-dimensional shape is primarily due to the breakage of

A. Peptide bonds
B. Weak interactions like hydrogen and ionic bonds
✓
C. Glycosidic linkages
D. Phosphodiester bonds

📝 Explanation

Denaturation unfolds a protein by disrupting the non-covalent interactions (hydrogen bonds, ionic bonds, hydrophobic interactions) that stabilize secondary, tertiary, and quaternary structures. The primary structure's covalent peptide bonds usually remain intact.

📖 Additional Information

  • Peptide bonds
  • Weak interactions like hydrogen and ionic bonds
  • Glycosidic linkages
  • Phosphodiester bonds

Denaturation unfolds a protein by disrupting the non-covalent interactions (hydrogen bonds, ionic bonds, hydrophobic interactions) that stabilize secondary, tertiary, and quaternary structures. The primary structure's covalent peptide bonds usually remain intact.

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