title: Fully reduced ribonuclease A does not expand at high denaturant concentration or temperature.
abstract: The dimensions of a denatured protein, fully reduced ribonuclease A (r-RNase A), have been measured using synchrotron-based small angle X-ray scattering. The radius of gyration, 34-35 A, is unchanged from 0-6 M guanidinium chloride and from 20-90 degrees C at pH 2.5, and agrees with the known scaling behavior for a multitude of chemically denatured states. The polypeptide is behaving as a statistical coil in the non-interacting, high-temperature limit.
authors.affiliation: Department of Biochemistry and Molecular Biology, The University of Chicago, Chicago, IL 60637, USA. jjacob@amgen.com
authors.forename: Jaby
authors.initials: J
authors.lastname: Jacob
authors.forename: Robin S
authors.initials: RS
authors.lastname: Dothager
authors.forename: P
authors.initials: P
authors.lastname: Thiyagarajan
authors.forename: Tobin R
authors.initials: TR
authors.lastname: Sosnick
mesh_terms: D031541:Fluorescence Resonance Energy Transfer; D010084:Oxidation-Reduction; D011489:Protein Denaturation; D017510:Protein Folding; D012259:Ribonuclease, Pancreatic / Q000737:chemistry*; D053838:Scattering, Small Angle; D012996:Solutions; D013696:Temperature; D014867:Water; D014961:X-Ray Diffraction
chemical_list: D012996:Solutions; D014867:Water; D012259:Ribonuclease, Pancreatic