On the Mechanism of Renaturation of Proteins Containing Disulfide Bonds

  • Hiroshi Taniuchi
  • A. Seetharama Acharya
  • Generoso Andria
  • Diana S. Parker
Part of the Advances in Experimental Medicine and Biology book series (AEMB, volume 86A)


The renaturation of bovine pancreatic ribonuclease A and hen egg white lysozyme from their reduced forms involves two statistical processes, pairing of half-cystine residues by oxidation and rearrangement of disulfide bonds by enzyme or thiol catalyzed sulfhydryl-disulfide interchange. The stability against sulfhydryl-disulfide interchange of the native or nativelike conformation thus attained, which could be a form containing three native disulfide bonds and one open disulfide bond, causes the system to accumulate the renatured enzyme. Thus, the native-like conformation is associated with the lowest free energy only in the late phase of folding.


Disulfide Bond Conformational Energy Lower Free Energy Gibbs Standard Free Energy Folding Rate 
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Copyright information

© Plenum Press, New York 1977

Authors and Affiliations

  • Hiroshi Taniuchi
    • 1
  • A. Seetharama Acharya
    • 1
  • Generoso Andria
    • 1
  • Diana S. Parker
    • 1
  1. 1.Laboratory of Chemical BiologyNational Institute of Arthritis, Metabolism, and Digestive Diseases, National Institutes of HealthBethesdaUSA

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