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PMID: 17301233 Published · ppublish English Journal Article Research Support, N.I.H., Intramural Research Support, Non-U.S. Gov't

Ultrafast dynamics of protein collapse from single-molecule photon statistics.

Proceedings of the National Academy of Sciences of the United States of America ·Vol. 104 ·No. 8 ·2007-02-20 ·Pages 2655-60

Nettels D, Gopich IV, Hoffmann A, Schuler B

Abstract

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.

MeSH Terms
Fluorescence Resonance Energy Transfer Heat-Shock Proteins/chemistry,metabolism Peptides/chemistry,metabolism Photons Protein Denaturation Protein Folding Thermodynamics Thermotoga maritima/metabolism
Chemicals
Heat-Shock Proteins Peptides
Authors & Affiliations
4 authors, click to expand affiliations / ORCID
Nettels Daniel
*Biochemisches Institut, Universität Zürich, Winterthurerstrasse 190, 8057 Zürich, Switzerland.
Gopich Irina V
Hoffmann Armin
Schuler Benjamin
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Article Info
Journal
Proceedings of the National Academy of Sciences of the United States of America
Abbr.
Proc Natl Acad Sci U S A
ISSN
0027-8424
DOI
10.1073/pnas.0611093104
Published
2007-02-20
Epub
2007-00-14
Pages
2655-60
Language
English
Region
United States
NLM ID
7505876
PMCID
PMC1815237
Subset
IM
Grants
Intramural NIH HHS · United States
External Links
PubMed source DOI: 10.1073/pnas.0611093104 PMC Full Text View journal details
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