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Article

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

Proteins - 1 Sept 1996

Schiffer C A, van Gunsteren W F

Abstract excerpt

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...

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Identifiers

PMID: 8880930
DOI: 10.1002/(SICI)1097-0134(199609)26:1<66::AID-PROT6>3.0.CO;2-E

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PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 7 Sept 2026. Manifest publication-graph-cohort-2026-09-08.1.

Source receipt: pubmed, retrieved 7 Sept 2026.

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