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nmdcat.online June 27, 2026

The concept that the primary sequence of a protein dictates its final three-dimensional conformation is primarily demonstrated by the observation that

A. Denatured proteins can spontaneously refold into their native structure under appropriate conditions
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B. All proteins fold into an identical β-pleated sheet regardless of their sequence
C. The peptide backbone is flexible, so sequence has no effect on shape
D. Molecular chaperones edit the amino acid sequence during folding

📝 Explanation

The Anfinsen experiment with ribonuclease showed that the amino acid sequence contains all the information needed for the protein to fold into its correct tertiary structure. Upon removal of a denaturant, the protein refolded spontaneously, proving structure is sequence-determined.

📖 Additional Information

  • Denatured proteins can spontaneously refold into their native structure under appropriate conditions
  • All proteins fold into an identical β-pleated sheet regardless of their sequence
  • The peptide backbone is flexible, so sequence has no effect on shape
  • Molecular chaperones edit the amino acid sequence during folding

The Anfinsen experiment with ribonuclease showed that the amino acid sequence contains all the information needed for the protein to fold into its correct tertiary structure. Upon removal of a denaturant, the protein refolded spontaneously, proving structure is sequence-determined.

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