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nmdcat.online July 11, 2026

The three-dimensional shape of an enzyme, crucial for its catalytic activity, is primarily maintained by

A. Peptide bonds linking amino acids in the polypeptide chain
B. Weak non-covalent interactions and disulfide bridges
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C. Covalent cross-links formed between enzyme and cofactor
D. Hydrophobic exclusion of water molecules from the active site

📝 Explanation

The tertiary structure of an enzyme, which dictates the shape of the active site, is stabilized by hydrogen bonds, ionic interactions, hydrophobic interactions, van der Waals forces, and covalent disulfide bonds.

📖 Additional Information

  • Peptide bonds linking amino acids in the polypeptide chain
  • Weak non-covalent interactions and disulfide bridges
  • Covalent cross-links formed between enzyme and cofactor
  • Hydrophobic exclusion of water molecules from the active site

The tertiary structure of an enzyme, which dictates the shape of the active site, is stabilized by hydrogen bonds, ionic interactions, hydrophobic interactions, van der Waals forces, and covalent disulfide bonds.

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