期刊
PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA
卷 104, 期 8, 页码 2655-2660出版社
NATL ACAD SCIENCES
DOI: 10.1073/pnas.0611093104
关键词
correlation; fluorescence; Hanbury Brown and Twiss; photon bunching; protein folding
资金
- Intramural NIH HHS Funding Source: Medline
We use the statistics of photon emission from single molecules to probe the ultrafast dynamics of an unfolded protein via Forster resonance energy transfer. Global reconfiguration of the chain occurs on a time scale of approximate to 50 ns and slows down concomitant with chain collapse under folding conditions. These diffusive dynamics provide a missing link between the phenomenological chemical kinetics commonly used in protein folding and a physical description in terms of quantitative free energy surfaces. The experiments demonstrate the potential of single-molecule methods in accessing the biologically important nanosecond time scales even in heterogeneous populations.
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