Ultrafast dynamics of protein collapse from single-molecule photon statistics
- 20 February 2007
- journal article
- Published by Proceedings of the National Academy of Sciences in Proceedings of the National Academy of Sciences of the United States of America
- Vol. 104 (8), 2655-2660
- https://doi.org/10.1073/pnas.0611093104
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.This publication has 69 references indexed in Scilit:
- Characterizing the unfolded states of proteins using single-molecule FRET spectroscopy and molecular simulationsProceedings of the National Academy of Sciences of the United States of America, 2007
- Mapping protein collapse with single-molecule fluorescence and kinetic synchrotron radiation circular dichroism spectroscopyProceedings of the National Academy of Sciences of the United States of America, 2007
- End-to-end distance distributions and intrachain diffusion constants in unfolded polypeptide chains indicate intramolecular hydrogen bond formationProceedings of the National Academy of Sciences of the United States of America, 2006
- Specificity of the Initial Collapse in the Folding of the Cold Shock ProteinJournal of Molecular Biology, 2006
- Effects of Denaturants on the Dynamics of Loop Formation in PolypeptidesBiophysical Journal, 2006
- Sub-microsecond Protein FoldingJournal of Molecular Biology, 2006
- Thermal denaturation and folding rates of single domain proteins: size mattersPolymer, 2004
- Effects of Chain Stiffness on the Dynamics of Loop Formation in Polypeptides. Appendix: Testing a 1-Dimensional Diffusion Model for Peptide DynamicsThe Journal of Physical Chemistry B, 2002
- Microscopic theory of protein folding rates. II. Local reaction coordinates and chain dynamicsThe Journal of Chemical Physics, 2001
- Brownian motion in a field of force and the diffusion model of chemical reactionsPhysica, 1940