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

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

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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 protein...

Topics

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

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