Compactness of the denatured state of a fast-folding protein measured by submillisecond small-angle x-ray scattering.

Pollack, L; Tate, M W; Darnton, N C; Knight, J B; Gruner, S M; Eaton, W A; Austin, R H · Proc Natl Acad Sci U S A · 1999

basic_science · Level V

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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.

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