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Biophys Chem. 2002 Dec 10;101-102:57-65.

Submolecular cooperativity produces multi-state protein unfolding and refolding.

Author information

  • 1Johnson Research Foundation, Department of Biochemistry and Biophysics, University of Pennsylvania School of Medicine, Philadelphia, PA 19104-6059, USA. walter@hxiris.med.upenn.edu

Abstract

Hydrogen exchange experiments show that cytochrome c and other proteins under native conditions reversibly unfold in a multi-step manner. The step from one intermediate to the next is determined by the intrinsically cooperative nature of secondary structural elements, which is retained in the native protein. Folding uses the same pathway in the reverse direction, moving from the unfolded to the native state through relatively discrete intermediate forms by the sequential addition of native-like secondary structural units.

Copyright 2002 Elsevier Science B.V.

PMID:
12487989
[PubMed - indexed for MEDLINE]

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