Question:

A protein unfolds when placed in \(8\,M\) urea, but regains activity when urea is removed. What does it show?

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If a denatured protein regains activity after removing denaturant, it shows that folding information is encoded in the amino acid sequence.
Updated On: May 18, 2026
  • Primary structure is destroyed in urea
  • Folding information lies in Amino acid sequence
  • Chaperones are obligatory for folding
  • Disulfide bonds are not required for activity
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The Correct Option is B

Solution and Explanation

Concept:
Protein folding is the process by which a polypeptide chain obtains its functional three-dimensional structure.

Step 1: Understand the role of urea.

Urea is a denaturant. It disrupts weak interactions such as hydrogen bonds and hydrophobic interactions, causing the protein to unfold.

Step 2: Removal of urea.

When urea is removed, the protein regains its original structure and activity. This means the protein can refold correctly.

Step 3: Interpretation.

If a protein can refold after removal of denaturant, it shows that the information required for folding is present in its amino acid sequence. This conclusion is related to Anfinsen's experiment on protein folding. \[ \therefore \text{Correct Answer is (B)} \]
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