title: Direct prediction of NMR residual dipolar couplings from the primary sequence of unfolded proteins.
abstract: Conformational analysis: an approach to the prediction of RDCs from disordered protein chains, integrating the effect of nearest neighbors and the alignment characteristics of the statistical coil, is reported. NMR residual dipolar couplings (RDC) are sensitive probes of conformational sampling in unfolded proteins.
authors.affiliation: Protein Dynamics and Flexibility, Institut de Biologie Structurale Jean-Pierre Ebel, CNRS-CEA-UJF UMR, Grenoble, France.
authors.forename: Jie-rong
authors.initials: JR
authors.lastname: Huang
authors.forename: Valéry
authors.initials: V
authors.lastname: Ozenne
authors.forename: Malene Ringkjøbing
authors.initials: MR
authors.lastname: Jensen
authors.forename: Martin
authors.initials: M
authors.lastname: Blackledge
mesh_terms: D008958:Models, Molecular; D019906:Nuclear Magnetic Resonance, Biomolecular / Q000379:methods; D011487:Protein Conformation; D017510:Protein Folding; D058767:Protein Unfolding; D011506:Proteins / Q000737:chemistry*
chemical_list: D011506:Proteins