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Simultaneous Definition of High Resolution Protein Structure and Backbone Conformational Dynamics using NMR Residual Dipolar Couplings
Author(s) -
Bouvignies Guillaume,
Markwick Phineus R. L.,
Blackledge Martin
Publication year - 2007
Publication title -
chemphyschem
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.016
H-Index - 140
eISSN - 1439-7641
pISSN - 1439-4235
DOI - 10.1002/cphc.200700353
Subject(s) - residual dipolar coupling , residual , chemistry , chemical physics , molecular dynamics , dipole , protein dynamics , biomolecular structure , dynamics (music) , anisotropy , computational chemistry , protein structure , magnetic dipole–dipole interaction , crystallography , biological system , physics , computer science , organic chemistry , algorithm , biochemistry , optics , acoustics , biology
Despite the importance of molecular dynamics for biological activity, most approaches to protein structure determination, whether based on crystallographic or solution studies, propose three‐dimensional atomic representations of a single configuration that take no account of conformational fluctuation. Non‐averaged anisotropic NMR interactions, such as residual dipolar couplings, that become measurable under conditions of weak alignment, provide sensitive probes of both molecular structure and dynamics. Residual dipolar couplings are becoming increasingly powerful for the study of proteins in solution. In this minireview we present their use for the simultaneous determination of protein structure and dynamics.