The 5-55 single-disulphide intermediate in folding of bovine pancreatic trypsin inhibitor

N.J. Darby, C.P.M. van Mierlo, T.E. Creighton

Research output: Contribution to journalArticleAcademicpeer-review

33 Citations (Scopus)

Abstract

An analogue of the BPTI folding intermediate that contains only the disulphide bond between Cys-5 and Cys-55 has been prepared by mutation or the other four Cys residues to Ser. On the basis of its circular dichroism and 1H-nuclear magnetic resonance spectra and its electrophoretic mobility, this intermediate is shown to be at least partially folded at low temperatures. This probably accounts for several of the unique properties of this intermediate observed during folding.

Original languageEnglish
Pages (from-to)61-64
JournalFEBS Letters
Volume279
Issue number1
DOIs
Publication statusPublished - 11 Feb 1991

Keywords

  • Bovine pancreatic trypsin inhibitor
  • Nuclear magnetic resonance, Circular dichroism
  • Protein folding: Disulphide intermediate

Fingerprint Dive into the research topics of 'The 5-55 single-disulphide intermediate in folding of bovine pancreatic trypsin inhibitor'. Together they form a unique fingerprint.

  • Cite this