title: Characterization of Intrinsically Disordered Proteins by Analytical Ultracentrifugation.
abstract: Intrinsically disordered proteins have traditionally been largely neglected by structural biologists because a lack of rigid structure precludes their study by X-ray crystallography. Structural information must therefore be inferred from physicochemical studies of their solution behavior. Analytical ultracentrifugation yields important information about the gross conformation of an intrinsically disordered protein. Sedimentation velocity studies provide estimates of the weight-average sedimentation and diffusion coefficients of a given macromolecular state of the protein.
authors.affiliation: National Center for Macromolecular Hydrodynamics, School of Biosciences, University of Nottingham, Nottingham, United Kingdom; ISIS Spallation Neutron and Muon Source and Research Complex at Harwell, Rutherford-Appleton Laboratory, Oxford, United Kingdom. Electronic address: david.scott@nottingham.ac.uk.
authors.forename: David J
authors.initials: DJ
authors.lastname: Scott
authors.affiliation: School of Chemistry and Molecular Biosciences, University of Queensland, Brisbane, Queensland, Australia.
authors.forename: Donald J
authors.initials: DJ
authors.lastname: Winzor
mesh_terms: D000465:Algorithms; D000818:Animals; D002499:Centrifugation, Density Gradient; D064267:Intrinsically Disordered Proteins / Q000737:chemistry* / Q000302:isolation & purification; D008970:Molecular Weight; D011487:Protein Conformation
chemical_list: D064267:Intrinsically Disordered Proteins
keywords: Diffusion coefficient; Intrinsically disordered proteins; Lamm equation; Sedimentation coefficient