Question:

During deturation which bonds in protein structure are NOT broken:

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Deturation affects higher-order structures ($2^\circ, 3^\circ, 4^\circ$) while keeping the primary structure ($1^\circ$ peptide bonds) intact.
Proteolysis is required to break peptide bonds, which is distinct from deturation.
Updated On: Jul 28, 2026
  • Disulphide bonds
  • Hydrogen bonds
  • Ionic bonds
  • Peptide bonds
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The Correct Option is D

Solution and Explanation

Step 1: Understanding the Question:
The question asks to identify which chemical bonds remain intact during protein deturation.

Step 2: Key Formula or Approach:

Protein structure is organized into four levels:
Primary structure: Sequence of amino acids linked covalently by peptide bonds.

Secondary, Tertiary, Quaterry structures: Maintained by non-covalent interactions (hydrogen bonds, ionic bonds, hydrophobic interactions) and covalent disulfide bridges.
Deturation disrupts higher-order structures without breaking primary covalent backbone bonds.

Step 3: Detailed Explation:


Definition of Deturation: Deturation refers to the unfolding of a protein's tive three-dimensiol tertiary or secondary structure under stress conditions such as high heat, extreme pH, organic solvents, or chaotropic agents (e.g., urea, guanidinium chloride).

Bonds Affected: Deturation disrupts weak non-covalent interactions (hydrogen bonds, ionic interactions/salt bridges, van der Waals forces) and can reduce disulfide linkages if reducing agents are present.

Preservation of Peptide Bonds: The covalent peptide bonds (amide linkages) forming the primary backbone of the polypeptide chain are robust and require enzymatic cleavage or harsh chemical acid/base hydrolysis to break. Thus, primary structure remains completely intact after deturation.

Step 4: Fil Answer:

Peptide bonds holding together the primary amino acid sequence are NOT broken during protein deturation.
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