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

AUTOR(ES)

Pollack, Lois

FONTE

The National Academy of Sciences

RESUMO

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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