ArticleProceedings of the National Academy of Sciences of the United States of America2007
Distinguishing between cooperative and unimodal downhill protein folding.
Article in Proceedings of the National Academy of Sciences of the United States of America, 2007. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 38 papers.
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38 citing papers in PubMed.
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- Two-Dimensional Fluorescence Lifetime Correlation Spectroscopy: Concepts and Applications.Molecules (Basel, Switzerland) · 2018Review
- Simultaneous Determination of Two Subdomain Folding Rates Using the "Transfer-Quench" Method.Biophysical journal · 2017Article
- Probing the Action of Chemical Denaturant on an Intrinsically Disordered Protein by Simulation and Experiment.Journal of the American Chemical Society · 2016Article
- Random coil negative control reproduces the discrepancy between scattering and FRET measurements of denatured protein dimensions.Proceedings of the National Academy of Sciences of the United States of America · 2015Article
- Single-Molecule Analysis of CytochromeThe journal of physical chemistry letters · 2013Article
- Microsecond dynamics of an unfolded protein by a line confocal tracking of single molecule fluorescence.Scientific reports · 2013Article
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- Small-angle X-ray scattering and single-molecule FRET spectroscopy produce highly divergent views of the low-denaturant unfolded state.Journal of molecular biology · 2012Article
- Conformational properties of the unfolded state of Im7 in nondenaturing conditions.Journal of molecular biology · 2012Article
- Protein folding at single-molecule resolution.Biochimica et biophysica acta · 2011Review
- The human peripheral subunit-binding domain folds rapidly while overcoming repulsive Coulomb forces.Protein science : a publication of the Protein Society · 2010Article
- Multicolor single-molecule FRET to explore protein folding and binding.Molecular bioSystems · 2010Review
- Evidence, from simulations, of a single state with residual native structure at the thermal denaturation midpoint of a small globular protein.Journal of the American Chemical Society · 2010Article
- Single-molecule studies of the Im7 folding landscape.Journal of molecular biology · 2010Article
- Capillarity theory for the fly-casting mechanism.Proceedings of the National Academy of Sciences of the United States of America · 2010Article
- Multiple conformations of full-length p53 detected with single-molecule fluorescence resonance energy transfer.Proceedings of the National Academy of Sciences of the United States of America · 2009Article
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5 authors.
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Abstract
Conventional cooperative protein folding invokes discrete ensembles of native and denatured state structures in separate free-energy wells. Unimodal noncooperative ("downhill") folding, however, proposes an ensemble of states occupying a single free-energy well for proteins folding at >/=4 x 10(4) s(-1) at 298 K. It is difficult to falsify unimodal mechanisms for such fast folding proteins by standard equilibrium experiments because both cooperative and unimodal mechanisms can present the same time-averaged structural, spectroscopic, and thermodynamic properties when the time scale used for observation is longer than for equilibration. However, kinetics can provide the necessary evidence. Chevron plots with strongly sloping linear refolding arms are very difficult to explain by downhill folding and are a signature for cooperative folding via a transition state ensemble. The folding kinetics of the peripheral subunit binding domain POB and its mutants fit to strongly sloping chevrons at observed rate constants of >6 x 10(4) s(-1) in denaturant solution, extrapolating to 2 x 10(5) s(-1) in water. Protein A, which folds at 10(5) s(-1) at 298 K, also has a well-defined chevron. Single-molecule fluorescence energy transfer experiments on labeled Protein A in the presence of denaturant demonstrated directly bimodal distributions of native and denatured states.
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