ArticleProceedings of the National Academy of Sciences of the United States of America2010
Probing static disorder in Arrhenius kinetics by single-molecule force spectroscopy.
Article in Proceedings of the National Academy of Sciences of the United States of America, 2010. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 20 papers.
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Who cites it
20 citing papers in PubMed.
- Identical sequences, different behaviors: Protein diversity captured at the single-molecule level.Biophysical journal · 2024Article
- Electro-detachment of kinesin motor domain from microtubule in silico.Computational and structural biotechnology journal · 2023Article
- Non-ergodicity of a globular protein extending beyond its functional timescale.Chemical science · 2022Article
- Direct observation of chaperone-modulated talin mechanics with single-molecule resolution.Communications biology · 2022Article
- Nonexponential kinetics captured in sequential unfolding of polyproteins over a range of loads.Current research in structural biology · 2022Article
- Protein nanomechanics in biological context.Biophysical reviews · 2021Review
- Mechanical Unfolding of Single Polyubiquitin Molecules Reveals Evidence of Dynamic Disorder.ACS omega · 2020Article
- Evidence of disorder in biological molecules from single molecule pulling experiments.Physical review letters · 2014Article
- Article
- The Janus-faced role of external forces in mechanochemical disulfide bond cleavage.Nature chemistry · 2013Article
- On the mechanism of recombination hotspot scanning during double-stranded DNA break resection.Proceedings of the National Academy of Sciences of the United States of America · 2013Article
- Force dependency of biochemical reactions measured by single-molecule force-clamp spectroscopy.Nature protocols · 2013Article
- Force-clamp analysis techniques give highest rank to stretched exponential unfolding kinetics in ubiquitin.Biophysical journal · 2012Article
- Dynamic prestress in a globular protein.PLoS computational biology · 2012Article
- Mechanical unfolding studies of protein molecules.Biophysics (Nagoya-shi, Japan) · 2012Review
- A conditional gating mechanism assures the integrity of the molecular force-sensor titin kinase.Biophysical journal · 2011Article
- Direct quantification of the attempt frequency determining the mechanical unfolding of ubiquitin protein.The Journal of biological chemistry · 2011Article
- Contrasting the individual reactive pathways in protein unfolding and disulfide bond reduction observed within a single protein.Journal of the American Chemical Society · 2011Article
- Water's role in the force-induced unfolding of ubiquitin.Proceedings of the National Academy of Sciences of the United States of America · 2010Article
- First passage time distribution in stochastic processes with moving and static absorbing boundaries with application to biological rupture experiments.The Journal of chemical physics · 2010Article
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Authors and funding
9 authors.
Funding
Abstract
The widely used Arrhenius equation describes the kinetics of simple two-state reactions, with the implicit assumption of a single transition state with a well-defined activation energy barrier DeltaE, as the rate-limiting step. However, it has become increasingly clear that the saddle point of the free-energy surface in most reactions is populated by ensembles of conformations, leading to nonexponential kinetics. Here we present a theory that generalizes the Arrhenius equation to include static disorder of conformational degrees of freedom as a function of an external perturbation to fully account for a diverse set of transition states. The effect of a perturbation on static disorder is best examined at the single-molecule level. Here we use force-clamp spectroscopy to study the nonexponential kinetics of single ubiquitin proteins unfolding under force. We find that the measured variance in DeltaE shows both force-dependent and independent components, where the force-dependent component scales with F(2), in excellent agreement with our theory. Our study illustrates a novel adaptation of the classical Arrhenius equation that accounts for the microscopic origins of nonexponential kinetics, which are essential in understanding the rapidly growing body of single-molecule data.
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