title: X-ray solution scattering studies of protein folding.
abstract: Protein folding is a reaction in which an extended polypeptide chain acquires maximal packing through formation of secondary and tertiary structures. Compactness and shape are, therefore, critical properties characterizing the process of protein folding. Because the stability of the native state is determined by the subtle free energy balance between the native and denatured states, the characterization of the denatured state is also essential to understand the conformational stability of the native state. We show that solution X-ray scattering is the best technique available today to address these problems. Although the structural resolution of the unfolded or compact denatured states elucidated from solution X-ray scattering is low, it provides a variety of information complementary to that obtained by NMR or X-ray crystallography.
authors.affiliation: Department of Earth and Space Science, Osaka University, Japan. kataoka@ess.sci.osaka-u.ac.jp
authors.forename: M
authors.initials: M
authors.lastname: Kataoka
authors.forename: Y
authors.initials: Y
authors.lastname: Goto
mesh_terms: D000818:Animals; D018360:Crystallography, X-Ray; D006801:Humans; D009682:Magnetic Resonance Spectroscopy; D017510:Protein Folding; D011506:Proteins / Q000737:chemistry*
chemical_list: D011506:Proteins