A hybrid approach to theoretical analysis of bovine pancreatic trypsin inhibitor

T. Thacher, H. Rabitz

Research output: Contribution to journalArticle

10 Scopus citations

Abstract

A static analysis of bovine pancreatic trypsin inhibitor (BPTI) is presented based on a new discrete/continuum approach to modeling the dynamics of biomolecules. This hybrid method utilizes knowledge of the intramolecular potential and molecular configuration to generate a field of elastic modulus tensors. These tensors, which relate the local stress and strain for each atom in the biomolecule, can be used to judge the local rigidity as well as indicate regions of high stress. Comparing the tensor fields for an unrelaxed and a relaxed configuration, the microscopic structure of BPTI is found to be anisotropic and to have regions of stress even when it is relaxed in the potential field. However, when these fields are averaged over the whole protein or over individual residues the structure becomes more isotropic and the stressed regions vanish. Using these averaged tensors, we calculated bulk properties such as Young's modulus and the Lamé constants and they agreed with previously reported values.

Original languageEnglish (US)
Pages (from-to)695-704
Number of pages10
JournalBiophysical Journal
Volume54
Issue number4
DOIs
StatePublished - 1988

All Science Journal Classification (ASJC) codes

  • Biophysics

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