Determination of Protein Structures Consistent with NMR Order Parameters

2004/06/15 by Robert B. Best, Michele Vendruscolo · 1 voice
Biochemistry, Genetics and Molecular Biology · Chemistry · #Protein Structure and Dynamics #RNA and protein synthesis mechanisms #Molecular spectroscopy and chirality

paper · doi:10.1021/ja0396955

openalex publication_date 2004/06/15 · openalex created_date 2025/10/10 · openalex updated_date 2026/07/16

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.

Discussions

• We could maybe study these changes in dynamics using MD, but the changes are smaller than the errors of conventional MD. Fortunately, Rob Best & Michele Vendruscolo had developed an approach to gener [bsky, 1 points, 1 comments]

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