Characterization of Intrinsically Disordered Proteins by Analytical Ultracentrifugation

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.