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

Proc Natl Acad Sci U S A. 1999 Aug 31;96(18):10115-7. doi: 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.

Publication types

  • Research Support, Non-U.S. Gov't
  • Research Support, U.S. Gov't, Non-P.H.S.
  • Research Support, U.S. Gov't, P.H.S.

MeSH terms

  • Crystallography, X-Ray / instrumentation
  • Crystallography, X-Ray / methods
  • Cytochrome c Group / chemistry*
  • Cytochrome c Group / metabolism
  • Hydrogen-Ion Concentration
  • Kinetics
  • Protein Denaturation*
  • Protein Folding*
  • Time Factors

Substances

  • Cytochrome c Group