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• W1963768262 abstract "Recent protein design experiments have demonstrated that proteins can migrate between folds through the accumulation of substitution mutations without visiting disordered or nonfunctional points in sequence space. To explore the biophysical mechanism underlying such transitions we use a three-letter continuous protein model with seven atoms per amino acid to provide realistic sequence-structure and sequence-function mappings through explicit simulation of the folding and interaction of model sequences. We start from two 16-amino-acid sequences folding into an α-helix and a β-hairpin, respectively, each of which has a preferred binding partner with 35 amino acids. We identify a mutational pathway between the two folds, which features a sharp fold switch. By contrast, we find that the transition in function is smooth. Moreover, the switch in preferred binding partner does not coincide with the fold switch. Discovery of new folds in evolution might therefore be facilitated by following fitness slopes in sequence space underpinned by binding-induced conformational switching." @default.
• W1963768262 created "2016-06-24" @default.
• W1963768262 creator A5011206268 @default.
• W1963768262 creator A5017147820 @default.
• W1963768262 date "2014-09-01" @default.
• W1963768262 modified "2023-10-16" @default.
• W1963768262 title "Smooth Functional Transition along a Mutational Pathway with an Abrupt Protein Fold Switch" @default.
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• W1963768262 doi "https://doi.org/10.1016/j.bpj.2014.07.020" @default.
• W1963768262 hasPubMedCentralId "https://www.ncbi.nlm.nih.gov/pmc/articles/4156676" @default.
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• W1963768262 hasPublicationYear "2014" @default.
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