Structural stability of disulfide mutants of basic pancreatic trypsin inhibitor: a molecular dynamics study

UMMS Affiliation

Department of Biochemistry and Molecular Pharmacology



Document Type


Medical Subject Headings

Aprotinin; Computer Simulation; Crystallography; Disulfides; Models, Molecular; Mutation; Phosphates; Protein Conformation; Protein Folding


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.

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Citation: Proteins. 1996 Sep;26(1):66-71.

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