Ultrafast dynamics of protein collapse from single-molecule photon statistics.
- Nettels D *Biochemisches Institut, Universität Zürich, Winterthurerstrasse 190, 8057 Zürich, Switzerland.
- Gopich IV
- Hoffmann A
- Schuler B
- 2007-02-16
Published in:
- Proceedings of the National Academy of Sciences of the United States of America. - 2007
Fluorescence Resonance Energy Transfer
Heat-Shock Proteins
Peptides
Photons
Protein Denaturation
Protein Folding
Thermodynamics
Thermotoga maritima
English
We use the statistics of photon emission from single molecules to probe the ultrafast dynamics of an unfolded protein via Förster resonance energy transfer. Global reconfiguration of the chain occurs on a time scale of approximately equal 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.
- Language
-
- English
- Open access status
- bronze
- Identifiers
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- DOI 10.1073/pnas.0611093104
- PMID 17301233
- Persistent URL
- https://sonar.rero.ch/global/documents/219569
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