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

FEBS Letters

Darby, N.J.¹  van Mierlo, C.P.M.¹  Creighton, T.E.¹ 

[1] MRC Laboratory of Molecular Biology, Hills Road, Cambridge CB2 2QH, UK

关键词: Protein folding: Disulphide intermediate;    Bovine pancreatic trypsin inhibitor;    Nuclear magnetic resonance;    Circular dichroism;    BPTI;    bovine pancreatic trypsin inhibitor;    N-BPTI;    BPTI with the 5–55;    14–38;    and 30–51 disulphide bonds. Unless otherwise stated;    Met-52 has been mutated to Arg;    (5–55);    BPTI with only a single disulphide bond between Cys-5 and -55;    CD;    circular dichroism;    NMR;    nuclear magnetic resonance;    θ;    mean residue ellipticity;   

DOI  :  10.1016/0014-5793(91)80251-W

学科分类：生物化学/生物物理

来源: John Wiley & Sons Ltd.

【 摘 要 】

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.

【 授权许可】

Unknown