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nmdcat.online June 27, 2026

The structural integrity of a protein at its tertiary level is most readily disrupted by agents that break disulfide bonds, such as

A. Detergents like SDS
B. Reducing agents like β-mercaptoethanol
✓
C. High concentrations of urea
D. Cooling to very low temperatures

📝 Explanation

Disulfide bridges (-S-S-) are covalent cross-links formed between cysteine R-groups. They lock the tertiary structure in place. Reducing agents like β-mercaptoethanol break these linkages, which can drastically destabilize the protein's 3D fold, causing unfolding. Detergents and urea primarily disrupt non-covalent interactions.

📖 Additional Information

  • Detergents like SDS
  • Reducing agents like β-mercaptoethanol
  • High concentrations of urea
  • Cooling to very low temperatures

Disulfide bridges (-S-S-) are covalent cross-links formed between cysteine R-groups. They lock the tertiary structure in place. Reducing agents like β-mercaptoethanol break these linkages, which can drastically destabilize the protein's 3D fold, causing unfolding. Detergents and urea primarily disrupt non-covalent interactions.

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