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nmdcat.online June 29, 2026

In protein structure, the disulfide bridge is a covalent cross-link that stabilizes the three-dimensional conformation. This bond is formed by the oxidative linkage of the sulfhydryl (-SH) groups of two residues of

A. Methionine
B. Cysteine
✓
C. Serine
D. Threonine

📝 Explanation

The thiol (-SH) group of cysteine's side chain can be oxidized to form a covalent disulfide bond (-S-S-) with another cysteine residue. This bond is critical for stabilizing the tertiary structure of secreted proteins like insulin and immunoglobulins. Methionine contains sulfur but cannot form disulfide bridges.

📖 Additional Information

  • Methionine
  • Cysteine
  • Serine
  • Threonine

The thiol (-SH) group of cysteine's side chain can be oxidized to form a covalent disulfide bond (-S-S-) with another cysteine residue. This bond is critical for stabilizing the tertiary structure of secreted proteins like insulin and immunoglobulins. Methionine contains sulfur but cannot form disulfide bridges.

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