title: Interpreting dynamically-averaged scalar couplings in proteins.
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.
authors.affiliation: Department of Biochemistry, Institute of Molecular Biology and Physiology, University of Copenhagen, Universitetsparken 13, 2100, Copenhagen Ø, DK, Denmark. klindorff-larsen@aki.ku.dk
authors.forename: Kresten
authors.initials: K
authors.lastname: Lindorff-Larsen
authors.forename: Robert B
authors.initials: RB
authors.lastname: Best
authors.forename: Michele
authors.initials: M
authors.lastname: Vendruscolo
mesh_terms: D008958:Models, Molecular; D019906:Nuclear Magnetic Resonance, Biomolecular; D011485:Protein Binding; D011487:Protein Conformation; D011506:Proteins / Q000737:chemistry*; D025801:Ubiquitin / Q000737:chemistry
chemical_list: D011506:Proteins; D025801:Ubiquitin