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• W2735539461 startingPage "152707" @default.
• W2735539461 abstract "Recent single-molecule experiments probed transition paths of biomolecular folding and, in particular, measured the time biomolecules spend while crossing their free energy barriers. A surprising finding from these studies is that the transition barriers crossed by transition paths, as inferred from experimentally observed transition path times, are often lower than the independently determined free energy barriers. Here we explore memory effects leading to anomalous diffusion as a possible origin of this discrepancy. Our analysis of several molecular dynamics trajectories shows that the dynamics of common reaction coordinates used to describe protein folding is subdiffusive, at least at sufficiently short times. We capture this effect using a one-dimensional fractional Brownian motion (FBM) model, in which the system undergoes a subdiffusive process in the presence of a potential of mean force, and show that this model yields much broader distributions of transition path times with stretched exponential long-time tails. Without any adjustable parameters, these distributions agree well with the transition path times computed directly from protein trajectories. We further discuss how the FBM model can be tested experimentally." @default.
• W2735539461 created "2017-07-21" @default.
• W2735539461 creator A5030095806 @default.
• W2735539461 creator A5058605984 @default.
• W2735539461 creator A5075489617 @default.
• W2735539461 date "2017-10-21" @default.
• W2735539461 modified "2023-09-24" @default.
• W2735539461 title "Transition path times reveal memory effects and anomalous diffusion in the dynamics of protein folding" @default.
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• W2735539461 doi "https://doi.org/10.1063/1.4993228" @default.
• W2735539461 hasPubMedId "https://pubmed.ncbi.nlm.nih.gov/29055292" @default.
• W2735539461 hasPublicationYear "2017" @default.
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