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• W2019475286 abstract "The prediction of the three-dimensional structures of the native states of proteins from the sequences of their amino acids is one of the most important challenges in molecular biology. An essential task for solving this problem within coarse-grained models is the deduction of effective interaction potentials between the amino acids. Over the years, several techniques have been developed to extract potentials that are able to discriminate satisfactorily between the native and nonnative folds of a preassigned protein sequence. In general, when these potentials are used in actual dynamical folding simulations, they lead to a drift of the native structure outside the quasinative basin. In this article, we present and validate an approach to overcome this difficulty. By exploiting several numerical and analytical tools, we set up a rigorous iterative scheme to extract potentials satisfying a prerequisite of any viable potential: the stabilization of proteins within their native basin (less than 3-4 A RMSD). The scheme is flexible and is demonstrated to be applicable to a variety of parameterizations of the energy function, and it provides in each case the optimal potentials." @default.
• W2019475286 created "2016-06-24" @default.
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• W2019475286 date "2001-01-01" @default.
• W2019475286 modified "2023-10-17" @default.
• W2019475286 title "Learning effective amino acid interactions through iterative stochastic techniques" @default.
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• W2019475286 doi "https://doi.org/10.1002/1097-0134(20010215)42:3<422::aid-prot120>3.0.co;2-2" @default.
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