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• W2020060224 abstract "In protein folding the term plasticity refers to the number of alternative folding pathways encountered in response to free energy perturbations such as those induced by mutation. Here we explore the relation between folding plasticity and a gross, generic feature of the native geometry, namely, the relative number of local and non-local native contacts. The results from our study, which is based on Monte Carlo simulations of simple lattice proteins, show that folding to a structure that is rich in local contacts is considerably more plastic than folding to a native geometry characterized by having a very large number of long-range contacts (i.e., contacts between amino acids that are separated by more than 12 units of backbone distance). The smaller folding plasticity of native geometries is probably a direct consequence of their higher folding cooperativity that renders the folding reaction more robust against single- and multiple-point mutations." @default.
• W2020060224 created "2016-06-24" @default.
• W2020060224 creator A5015402015 @default.
• W2020060224 creator A5052906833 @default.
• W2020060224 date "2008-12-01" @default.
• W2020060224 modified "2023-10-15" @default.
• W2020060224 title "On the relation between native geometry and conformational plasticity" @default.
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• W2020060224 doi "https://doi.org/10.1016/j.bpc.2008.09.006" @default.
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