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• W2041505869 abstract "Protein folding is inherently a heterogeneous process because of the very large number of microscopic pathways that connect the myriad unfolded conformations to the unique conformation of the native structure. In a first step towards the long-range goal of describing the distribution of pathways experimentally, Förster resonance energy transfer (FRET) has been measured on single, freely diffusing molecules. Here we use this method to determine properties of the free-energy surface for folding that have not been obtained from ensemble experiments. We show that single-molecule FRET measurements of a small cold-shock protein expose equilibrium collapse of the unfolded polypeptide and allow us to calculate limits on the polypeptide reconfiguration time. From these results, limits on the height of the free-energy barrier to folding are obtained that are consistent with a simple statistical mechanical model, but not with the barriers derived from simulations using molecular dynamics. Unlike the activation energy, the free-energy barrier includes the activation entropy and thus has been elusive to experimental determination for any kinetic process in solution." @default.
• W2041505869 created "2016-06-24" @default.
• W2041505869 creator A5055791638 @default.
• W2041505869 creator A5066892009 @default.
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• W2041505869 date "2002-10-17" @default.
• W2041505869 modified "2023-10-10" @default.
• W2041505869 title "Probing the free-energy surface for protein folding with single-molecule fluorescence spectroscopy" @default.
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• W2041505869 doi "https://doi.org/10.1038/nature01060" @default.
• W2041505869 hasPubMedId "https://pubmed.ncbi.nlm.nih.gov/12384704" @default.
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