Question:

What is the difference between native protein and denatured protein?

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Denaturation does not affect the primary structure (sequence of amino acids) but causes a loss of the functional three-dimensional structure of the protein.
Updated On: Jun 10, 2025
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Solution and Explanation

Native vs. Denatured Proteins

Native Proteins:

  • These are proteins in their natural, biologically active form.
  • They possess a specific three-dimensional structure essential for their function.
  • Their structure includes well-defined secondary, tertiary, and sometimes quaternary levels of organization.
  • This conformation is stabilized by:
    • Hydrogen bonds
    • Hydrophobic interactions
    • Disulfide bridges
    • Ionic interactions

Denatured Proteins:

  • These proteins have lost their native conformation and, as a result, their biological activity.
  • Denaturation involves the disruption of stabilizing forces, leading to the unfolding of the protein structure.
  • Causes of denaturation include:
    • High or low temperature
    • pH changes
    • Chemical agents (e.g., urea, detergents)
  • Denatured proteins are typically inactive and may become insoluble or form aggregates.

In summary, the functional integrity of a protein is closely tied to its native conformation. Disruption of this structure results in a loss of function.

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