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ABSTRACT: Background
Quantitative evaluation of protein structural evolution is important for our understanding of protein biological functions and their evolutionary adaptation, and is useful in guiding protein engineering. However, compared to the models for sequence evolution, the quantitative models for protein structural evolution received less attention. Ancient protein superfamilies are often considered versatile, allowing genetic and functional diversifications during long-term evolution. In this study, we investigated the quantitative impacts of sequence variations on the structural evolution of homologues in 68 ancient protein superfamilies that exist widely in sequenced eukaryotic, bacterial and archaeal genomes.Results
We found that the accumulated structural variations w
SUBMITTER: Zhang Z
PROVIDER: S-EPMC6201574 | biostudies-literature | 2018 Oct
REPOSITORIES: biostudies-literature