Determination of Protein Structures Consistent with NMR Order Parameters
- 15 June 2004
- journal article
- research article
- Published by American Chemical Society (ACS) in Journal of the American Chemical Society
- Vol. 126 (26) , 8090-8091
- https://doi.org/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.Keywords
This publication has 11 references indexed in Scilit:
- Orientation restraints in molecular dynamics simulations using time and ensemble averagingJournal of Magnetic Resonance, 2003
- Dynamics and Entropy of a Calmodulin−Peptide Complex Studied by NMR and Molecular DynamicsBiochemistry, 2002
- Effective energy function for proteins in solutionProteins-Structure Function and Bioinformatics, 1999
- Molecular Dynamics of Staphylococcal Nuclease: Comparison of Simulation with 15N and 13C NMR Relaxation DataJournal of the American Chemical Society, 1998
- Reversible unfolding of fibronectin type III and immunoglobulin domains provides the structural basis for stretch and elasticity of titin and fibronectin.Proceedings of the National Academy of Sciences, 1994
- Coupling constants as restraints in ensemble distance driven dynamicsBiopolymers, 1994
- NMR order parameters and free energy: an analytical approach and its application to cooperative calcium(2+) binding by calbindin D9kJournal of the American Chemical Society, 1993
- Structure of a Fibronectin Type III Domain from Tenascin Phased by MAD Analysis of the Selenomethionyl ProteinScience, 1992
- CHARMM: A program for macromolecular energy, minimization, and dynamics calculationsJournal of Computational Chemistry, 1983
- Model-free approach to the interpretation of nuclear magnetic resonance relaxation in macromolecules. 2. Analysis of experimental resultsJournal of the American Chemical Society, 1982