Display Settings:

Format

Send to:

Choose Destination
Proteins. 1996 Sep;26(1):66-71.

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

Author information

  • 1Laboratory of Physical Chemistry, ETH-Zentrum, Z├╝rich, Switzerland.

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.

PMID:
8880930
[PubMed - indexed for MEDLINE]

LinkOut - more resources

Other Literature Sources

Molecular Biology Databases

PubMed Commons home

PubMed Commons

0 comments
How to join PubMed Commons

    Supplemental Content

    Loading ...
    Write to the Help Desk