ArticleThe Journal of chemical physics2009
A one-dimensional free energy surface does not account for two-probe folding kinetics of protein alpha(3)D.
Article in The Journal of chemical physics, 2009. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 13 papers.
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Who cites it
13 citing papers in PubMed.
- Three-color single-molecule maximum likelihood analysis of folding and binding of diffusing molecules.Biophysical journal · 2025Article
- Review
- Fast pressure-jump all-atom simulations and experiments reveal site-specific protein dehydration-folding dynamics.Proceedings of the National Academy of Sciences of the United States of America · 2019Article
- Mapping fast protein folding with multiple-site fluorescent probes.Proceedings of the National Academy of Sciences of the United States of America · 2015Article
- Fast protein folding kinetics.Quarterly reviews of biophysics · 2014Review
- Article
- Microsecond folding experiments and simulations: a match is made.Physical chemistry chemical physics : PCCP · 2013Article
- Single-molecule observation of helix staggering, sliding, and coiled coil misfolding.Proceedings of the National Academy of Sciences of the United States of America · 2012Article
- Making connections between ultrafast protein folding kinetics and molecular dynamics simulations.Proceedings of the National Academy of Sciences of the United States of America · 2011Article
- Folding network of villin headpiece subdomain.Biophysical journal · 2010Article
- Protein folded states are kinetic hubs.Proceedings of the National Academy of Sciences of the United States of America · 2010Article
- A natural missing link between activated and downhill protein folding scenarios.Physical chemistry chemical physics : PCCP · 2010Article
- Probing the folding transition state structure of the villin headpiece subdomain via side chain and backbone mutagenesis.Journal of the American Chemical Society · 2009Article
Corrections and comments
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Authors and funding
6 authors.
Funding
Abstract
We present fluorescence-detected measurements of the temperature-jump relaxation kinetics of the designed three-helix bundle protein alpha(3)D taken under solvent conditions identical to previous infrared-detected kinetics. The fluorescence-detected rate is similar to the IR-detected rate only at the lowest temperature where we could measure it (326 K). The fluorescence-detected rate decreases by a factor of 3 over the 326-344 K temperature range, whereas the IR-detected rate remains nearly constant over the same range. To investigate this probe dependence, we tested an extensive set of physically reasonable one-dimensional (1D) free energy surfaces by Langevin dynamics simulation. The simulations included coordinate- and temperature-dependent roughness, diffusion coefficients, and IR/fluorescence spectroscopic signatures. None of these can reproduce the IR and fluorescence data simultaneously, forcing us to the conclusion that a 1D free energy surface cannot accurately describe the folding of alpha(3)D. This supports the hypothesis that alpha(3)D has a multidimensional free energy surface conducive to downhill folding at 326 K, and that it is already an incipient downhill folder with probe-dependent kinetics near its melting point.
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