title: Compactness of the denatured state of a fast-folding protein measured by submillisecond small-angle x-ray scattering.
abstract: Time-resolved small-angle x-ray scattering was used to measure the radius of gyration of cytochrome c after initiation of folding by a pH jump. Submillisecond time resolution was obtained with a microfabricated diffusional mixer and synchrotron radiation. The results show that the protein first collapses to compact denatured structures before folding very fast to the native state.
authors.affiliation: Laboratory of Atomic and Solid State Physics, Cornell University, Ithaca, NY 14853, USA.
authors.forename: L
authors.initials: L
authors.lastname: Pollack
authors.forename: M W
authors.initials: MW
authors.lastname: Tate
authors.forename: N C
authors.initials: NC
authors.lastname: Darnton
authors.forename: J B
authors.initials: JB
authors.lastname: Knight
authors.forename: S M
authors.initials: SM
authors.lastname: Gruner
authors.forename: W A
authors.initials: WA
authors.lastname: Eaton
authors.forename: R H
authors.initials: RH
authors.lastname: Austin
mesh_terms: D018360:Crystallography, X-Ray / Q000295:instrumentation / Q000379:methods; D003574:Cytochrome c Group / Q000737:chemistry* / Q000378:metabolism; D006863:Hydrogen-Ion Concentration; D007700:Kinetics; D011489:Protein Denaturation; D017510:Protein Folding; D013997:Time Factors
chemical_list: D003574:Cytochrome c Group