✦ LIBER ✦

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

✍ Scribed by Schiffer, Celia A.; van Gunsteren, Wilfred F.

Publisher: John Wiley and Sons
Year: 1996
Tongue: English
Weight: 753 KB
Volume: 26
Category: Article
ISSN: 0887-3585
DOI: 10.1002/(sici)1097-0134(199609)26:1<66::aid-prot6>3.0.co;2-e

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✦ Synopsis

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 [5-551 and [30-511. 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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