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Conformations of intermediates in the folding of the pancreatic trypsin inhibitor.

Authors
  • States, D J
  • Creighton, T E
  • Dobson, C M
  • Karplus, M
Type
Published Article
Journal
Journal of molecular biology
Publication Date
Jun 05, 1987
Volume
195
Issue
3
Pages
731–739
Identifiers
PMID: 2443711
Source
Medline
License
Unknown

Abstract

Intermediates in the folding pathway of the bovine pancreatic trypsin inhibitor (PTI) have been examined by 1H nuclear magnetic resonance (n.m.r.). The intermediates were trapped during the reoxidation and consequent refolding of reduced PTI by alkylating free thiols; each intermediate contained different disulphide linkages. The n.m.r. spectra reveal that conformational features of the native protein are present in the intermediate containing just one of the three normal disulphide linkages (30-51). As additional normal disulphide bonds are formed, the conformation becomes more similar to that of the native protein. Introduction of additional but incorrect disulphide bonds does not lead to an increase in observable globular structure. A description of the folding process in terms of the conformations of the different intermediates is proposed. The significance of these results for the general mechanism of protein folding is outlined.

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