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• W2017486784 abstract "An open question of great interest in biophysics is whether variations in structure cause protein folds to differ in the number of amino acid sequences that can fold to them stably, i.e., in their designability. Recently, we have shown that a novel quantitative measure of a fold's tertiary topology, called its contact trace, strongly correlates with the fold's designability. Here, we investigate the relationship between a fold's contact trace and its relative frequency of usage in mesophilic vs. thermophilic eubacteria. We observe that thermophilic organisms exhibit a bias toward using folds of higher contact trace when compared with mesophiles. We establish this difference both for the distributions of folds at the whole-proteome level and also through more focused structural comparisons of orthologous proteins. Our findings suggest that thermophilic adaptation in bacterial genomes occurs in part through natural selection of more designable folds, pointing to designability as a key component of protein fitness." @default.
• W2017486784 created "2016-06-24" @default.
• W2017486784 creator A5022792589 @default.
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• W2017486784 date "2003-07-03" @default.
• W2017486784 modified "2023-10-12" @default.
• W2017486784 title "Natural selection of more designable folds: A mechanism for thermophilic adaptation" @default.
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• W2017486784 doi "https://doi.org/10.1073/pnas.1530713100" @default.
• W2017486784 hasPubMedCentralId "https://www.ncbi.nlm.nih.gov/pmc/articles/166380" @default.
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