Title
Structural stability of disulfide mutants of basic pancreatic trypsin inhibitor: a molecular dynamics study
UMMS Affiliation
Department of Biochemistry and Molecular Pharmacology
Publication Date
1996-09-01
Document Type
Article
Subjects
Aprotinin; Computer Simulation; Crystallography; Disulfides; Models, Molecular; Mutation; Phosphates; Protein Conformation; Protein Folding
Disciplines
Biochemistry, Biophysics, and Structural Biology | Pharmacology, Toxicology and Environmental Health
Abstract
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.
Source
Proteins. 1996 Sep;26(1):66-71.
Journal/Book/Conference Title
Proteins
Related Resources
PubMed ID
8880930
Repository Citation
Schiffer, Celia A. and van Gunsteren, Wilfred F., "Structural stability of disulfide mutants of basic pancreatic trypsin inhibitor: a molecular dynamics study" (1996). Biochemistry and Molecular Pharmacology Publications and Presentations. 94.
https://escholarship.umassmed.edu/bmp_pp/94