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Abstract: In protein folding the term plasticity refers to the number of alternativefolding pathways encountered in response to free energy perturbations such asthose induced by mutation. Here we explore the relation between foldingplasticity and a gross, generic feature of the native geometry, namely, therelative number of local and non-local native contacts. The results from ourstudy, which is based on Monte Carlo simulations of simple lattice proteins,show that folding to a structure that is rich in local contacts is considerablymore plastic than folding to a native geometry characterized by having a verylarge number of long-range contacts i.e., contacts between amino acids thatare separated by more than 12 units of backbone distance. The smaller foldingplasticity of `non-local- native geometries is probably a direct consequence oftheir higher folding cooperativity that renders the folding reaction morerobust against single- and multiple-point mutations.



Autor: P.F.N. Faisca, C. M. Gomes

Fuente: https://arxiv.org/







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