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Updated: Aug 14, 2026

Visualization of ATP Synthase Dimers in Mitochondria by Electron Cryo-tomography
Published on: September 14, 2014
Snapshots of cytochrome c folding
Ekaterina V Pletneva1, Harry B Gray, Jay R Winkler
1Beckman Institute, California Institute of Technology, Pasadena, CA 91125, USA.
Abstract:
Dansyl-to-heme distance distributions [P(r)] during folding have been determined in five variants of Saccharomyces cerevisiae iso-1 ferricytochrome c (labeled at mutant Cys residues 4, 39, 50, 66, and 99) by analysis of fluorescence energy-transfer kinetics. Moment analysis of the P(r) distributions clearly indicates that cytochrome c refolding is not a simple two-state process. After 1 ms of folding, the polypeptide ensemble is not uniformly collapsed and there are site variations in the relative populations of collapsed structures. P(r) distributions reveal structural features of the multiple intermediate species and evolution of the polypeptide ensemble.
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