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• W996172352 abstract "Molecular simulations of large biomolecules typically reveal a complex picture of the freeenergy surface with many kinetically relevant states1–3. Complementary to this, advanced experimental techniques allow probing the equilibrium kinetics of biomolecules directly. This can either be done by perturbation techniques, such as temperature or pressure jump, or by equilibrium experiments in which the measured signal is autocorrelated to obtain kinetic information, as e.g. in fluorescence correlation spectroscopy. These measurements can be described by dynamical fingerprints, i.e. densities of relaxation timescales where each peak corresponds to an exponential relaxation process. In many cases, singleor double-peaked fingerprints are found, suggesting that a twoor three-state model may provide a satisfactory description of the biomolecule studied4, 5. We sketch an approach combining Markov state models (MSM)6, 3 of the simulated dynamics with dynamical fingerprints, which allows addressing the following questions: (i) Is the largest relaxation timescales observed always due to the folding process? (ii) Can a given experiment detect all relaxation processes that are present in the dynamics of the molecule? (iii) Are the processes observed in perturbation experiments the same as those observed in equilibrium experiments? We illustrate our findings using a four-state model of a protein folding equilibrium." @default.
• W996172352 created "2016-06-24" @default.
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• W996172352 date "2012-01-01" @default.
• W996172352 modified "2023-09-26" @default.
• W996172352 title "Resolving the apparent gap in complexity between simulated and measured kinetics of biomolecules" @default.
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