Compactness of the denatured state of a fast-folding protein measured by submillisecond small-angle x-ray scattering.
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.
Pollack
L
L
Laboratory of Atomic and Solid State Physics, Cornell University, Ithaca, NY 14853, USA.
Tate
M W
MW
Darnton
N C
NC
Knight
J B
JB
Gruner
S M
SM
Eaton
W A
WA
Austin
R H
RH
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
D003574:Cytochrome c Group