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- W2329492246 abstract "A simple model is presented that describes general features of protein folding, in good agreement with experimental results and detailed all-atom simulations. Starting from microscopic physics, and with no free parameters, this model predicts that protein folding occurs remarkably quickly because native-like states are kinetic hubs. A hub-like network arises naturally out of microscopic physical concerns, specifically the kinetic longevity of native contacts during a search of globular conformations. The model predicts folding times scaling as τf ∼ eξN in the number of residues, but because the model shows ξ is small, the folding times are much faster than Levinthal’s approximation. Importantly, the folding time scale is found to be small due to the topology and structure of the network. We show explicitly how our model agrees with generic experimental features of the folding process, including the scaling of τf with N, two-state thermodynamics, a sharp peak in CV, and native-state fluctuations." @default.
- W2329492246 created "2016-06-24" @default.
- W2329492246 creator A5017550931 @default.
- W2329492246 creator A5032418986 @default.
- W2329492246 date "2012-04-11" @default.
- W2329492246 modified "2023-09-24" @default.
- W2329492246 title "A Simple Model Predicts Experimental Folding Rates and a Hub-Like Topology" @default.
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- W2329492246 doi "https://doi.org/10.1021/jp212332c" @default.
- W2329492246 hasPubMedCentralId "https://www.ncbi.nlm.nih.gov/pmc/articles/3376171" @default.
- W2329492246 hasPubMedId "https://pubmed.ncbi.nlm.nih.gov/22452581" @default.
- W2329492246 hasPublicationYear "2012" @default.
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