Premium
The 5–55 single‐disulphide intermediate in folding of bovine pancreatic trypsin inhibitor
Author(s) -
Darby N.J.,
van Mierlo C.P.M.,
Creighton T.E.
Publication year - 1991
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/0014-5793(91)80251-w
Subject(s) - chemistry , folding (dsp implementation) , circular dichroism , crystallography , trypsin , protein folding , stereochemistry , biochemistry , enzyme , electrical engineering , engineering
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 1 H‐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.