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When a native globular protein is subjected to a drastic change in pH, it undergoes denaturation. Which of the following correctly identifies the fate of the chemical bonds during this process?

Options

  1. APeptide bonds are disrupted while hydrogen bonds remain intact.
  2. BHydrogen bonds are disrupted while peptide bonds remain intact.
  3. CBoth peptide bonds and hydrogen bonds are disrupted.
  4. DGlycosidic linkages are disrupted while peptide bonds remain intact.

Correct answer

B. Hydrogen bonds are disrupted while peptide bonds remain intact.

Step-by-step solution

A drastic change in pH causes denaturation of the globular protein. During denaturation, the secondary and tertiary structures of the protein are destroyed. These higher-order structures are stabilized by non-covalent interactions such as hydrogen bonds, van der Waals forces, and electrostatic forces. Thus, hydrogen bonds are disrupted, leading to the uncoiling of the protein. The primary structure of the protein, however, remains intact. The primary structure is stabilized by strong covalent peptide bonds between

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