Determination of protein structures consistent with NMR order parameters.
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.
Best
Robert B
RB
Department of Chemistry, University of Cambridge, Lensfield Road, Cambridge CB2 1EW, UK.
Vendruscolo
Michele
M
D015815:Cell Adhesion Molecules / Q000737:chemistry; D003198:Computer Simulation; D006801:Humans; D009682:Magnetic Resonance Spectroscopy; D008956:Models, Chemical; D011487:Protein Conformation; D019063:Tenascin / Q000737:chemistry
D015815:Cell Adhesion Molecules; D019063:Tenascin