Determination of protein structures consistent with NMR order parameters

J Am Chem Soc. 2004 Jul 7;126(26):8090-1. doi: 10.1021/ja0396955.

Abstract

Order parameters obtained from NMR experiments characterize distributions of bond vector orientations. Their interpretation, however, usually requires the assumption of a particular motional model. We propose a multiple-copy simulation method in which the experimental order parameters are used as restraints in conjunction with a standard molecular force field. The latter effectively acts as a sophisticated motional model, allowing ensembles of structures consistent with the experimental order parameters to be determined.

MeSH terms

  • Cell Adhesion Molecules / chemistry
  • Computer Simulation
  • Humans
  • Magnetic Resonance Spectroscopy*
  • Models, Chemical*
  • Protein Conformation*
  • Tenascin / chemistry

Substances

  • Cell Adhesion Molecules
  • Tenascin