Structural stability of disulfide mutants of basic pancreatic trypsin inhibitor: a molecular dynamics study
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.
Celia A. Schiffer and Wilfred F. van Gunsteren. "Structural stability of disulfide mutants of basic pancreatic trypsin inhibitor: a molecular dynamics study" Proteins 26.1 (1996).
Available at: http://works.bepress.com/celia_schiffer/36