title: Simultaneous definition of high resolution protein structure and backbone conformational dynamics using NMR residual dipolar couplings.
abstract: 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.
authors.affiliation: Institut de Biologie Structurale, 41 Rue Jules Horowitz, 38027, Grenoble, France.
authors.forename: Guillaume
authors.initials: G
authors.lastname: Bouvignies
authors.forename: Phineus R L
authors.initials: PR
authors.lastname: Markwick
authors.forename: Martin
authors.initials: M
authors.lastname: Blackledge
mesh_terms: D055598:Chemical Phenomena; D002627:Chemistry, Physical; D008958:Models, Molecular; D019906:Nuclear Magnetic Resonance, Biomolecular; D011487:Protein Conformation; D011506:Proteins / Q000737:chemistry*; D013816:Thermodynamics
chemical_list: D011506:Proteins