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- W2034278689 abstract "Quantitative models and experiments are revealing how the folding free energy surface of a protein is sculpted by sequence and environment. The sometimes conflicting demands of folding, structure and function determine which folding pathways, if any, dominate. Recent advances include experimental estimates of diffusive barrier-crossing times, the observation of ultrafast folders amenable to full-atom simulation, the use of thermodynamic tuning and nonconservative mutations to probe 'hidden' parts of the free energy surface, and a complete microscopic theory of folding." @default.
- W2034278689 created "2016-06-24" @default.
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- W2034278689 date "2002-04-01" @default.
- W2034278689 modified "2023-09-26" @default.
- W2034278689 title "Protein folding: the free energy surface" @default.
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- W2034278689 doi "https://doi.org/10.1016/s0959-440x(02)00304-4" @default.
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