Compactness of the denatured state of a fast-folding protein measured by submillisecond small-angle x-ray scattering
Open Access
- 31 August 1999
- journal article
- research article
- Published by Proceedings of the National Academy of Sciences in Proceedings of the National Academy of Sciences of the United States of America
- Vol. 96 (18), 10115-10117
- https://doi.org/10.1073/pnas.96.18.10115
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.This publication has 28 references indexed in Scilit:
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