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

Lois Pollack, Mark W. Tate, Nicholas C. Darnton, James B. Knight, Sol M. Gruner, William A. Eaton, Robert H. Austin

Research output: Contribution to journalArticle

254 Scopus citations

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.

Original languageEnglish (US)
Pages (from-to)10115-10117
Number of pages3
JournalProceedings of the National Academy of Sciences of the United States of America
Volume96
Issue number18
DOIs
StatePublished - Aug 31 1999

All Science Journal Classification (ASJC) codes

  • General

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