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- W2161836601 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." @default.
- W2161836601 created "2016-06-24" @default.
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- W2161836601 date "2010-06-08" @default.
- W2161836601 modified "2023-10-11" @default.
- W2161836601 title "Probing static disorder in Arrhenius kinetics by single-molecule force spectroscopy" @default.
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- W2161836601 doi "https://doi.org/10.1073/pnas.1006517107" @default.
- W2161836601 hasPubMedCentralId "https://www.ncbi.nlm.nih.gov/pmc/articles/2895103" @default.
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- W2161836601 hasPublicationYear "2010" @default.
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