Interpreting Dynamically-Averaged Scalar Couplings in Proteins |
| |
Authors: | Kresten Lindorff-Larsen Robert B Best Michele Vendruscolo |
| |
Institution: | 1. Department of Biochemistry, Institute of Molecular Biology and Physiology, University of Copenhagen, Universitetsparken 13, 2100, Copenhagen ?, DK, Denmark 2. Laboratory of Chemical Physics, NIDDK, National Institutes of Health, Bethesda, Maryland, 20892-0520, U.S.A 3. Department of Chemistry, University of Cambridge, Lensfield Road, Cambridge, CB2 1EW, United Kingdom
|
| |
Abstract: | The experimental determination of scalar three-bond coupling constants represents a powerful method to probe both the structure
and dynamics of proteins. The detailed structural interpretation of such coupling constants is usually based on Karplus relationships,
which allow the measured couplings to be related to the torsion angles of the molecules. As the measured couplings are sensitive
to thermal fluctuations, the parameters in the Karplus relationships are better derived from ensembles representing the distributions
of dihedral angles present in solution, rather than from single conformations. We present a method to derive such parameters
that uses ensembles of conformations determined through dynamic-ensemble refinement – a method that provides structural ensembles
that simultaneously represent both the structure and the associated dynamics of a protein. |
| |
Keywords: | protein dynamics Karplus relationship protein structure scalar couplings |
本文献已被 PubMed SpringerLink 等数据库收录! |
|