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• W2158843259 abstract "Abstract This is our second type of model for protein folding where the configurational parameters and the effective potential energy function are chosen in such a way that all conformations are described and the canonical partition function can be evaluated analytically. Structure is described in terms of distances between pairs of sequentially contiguous blocks of eight residues, and all possible conformations are grouped into 71 subsets in terms of bounds on these distances. The energy is taken to be a sum of pairwise interactions between such blocks. The 210 energy parameters were adjusted so that the native folds of 32 small proteins are favored in free energy over the denatured state. We then found 146 proteins having negligible sequence similarity to any of the training proteins, yet the free energy of the respective correct native states were favored over the denatured state. © 2004 Wiley Periodicals, Inc. Biopolymers, 2004" @default.
• W2158843259 created "2016-06-24" @default.
• W2158843259 creator A5009393979 @default.
• W2158843259 date "2004-08-31" @default.
• W2158843259 modified "2023-10-14" @default.
• W2158843259 title "Statistical mechanics of protein folding by cluster distance geometry" @default.
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• W2158843259 doi "https://doi.org/10.1002/bip.20118" @default.
• W2158843259 hasPubMedId "https://pubmed.ncbi.nlm.nih.gov/15378485" @default.
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