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.

SUBMITTER: Pollack L 

PROVIDER: S-EPMC17851 | biostudies-other | 1999 Aug

REPOSITORIES: biostudies-other