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Structural stability of disulfide mutants of basic pancreatic trypsin inhibitor: A molecular dynamics study
Author(s) -
Schiffer Celia A.,
van Gunsteren Wilfred F.
Publication year - 1996
Publication title -
proteins: structure, function, and bioinformatics
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.699
H-Index - 191
eISSN - 1097-0134
pISSN - 0887-3585
DOI - 10.1002/(sici)1097-0134(199609)26:1<66::aid-prot6>3.0.co;2-e
Subject(s) - chemistry , molecular dynamics , folding (dsp implementation) , counterion , disulfide bond , mutant , protein folding , structural stability , trypsin , crystallography , biophysics , biochemistry , ion , computational chemistry , enzyme , biology , organic chemistry , structural engineering , electrical engineering , gene , engineering
The structure and folding of basic pancreatic trypsin inhibitor (BPTI) has been studied extensively by experimental means. We report a computer simulation study of the structural stability of various disulfide mutants of BPTI, involving eight 250‐psec molecular dynamics simulations of the proteins in water, with and without a phosphate counterion. The presence of the latter alters the relative stability of the single disulfide species [5–55] and [30–51]. This conclusion can explain results of mutational studies and the conservation of residues in homologues of BPTI, and suggests a possible role of ions in stabilizing one intermediate over another in unfolding or folding processes. © 1996 Wiley‐Liss, Inc.