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- W2967372260 abstract "In order to preserve structure and function, proteins tend to preferentially conserve amino acids at particular sites along the sequence. Because mutations can affect structure and function, the question arises whether the preference of a protein site for a particular amino acid varies between protein homologs, and to what extent that variation depends on sequence divergence. Answering these questions can help in the development of models of sequence evolution, as well as provide insights on the dependence of the fitness effects of mutations on the genetic background of sequences, a phenomenon known as epistasis. Here, I comment on recent computational work providing a systematic analysis of the extent to which the amino acid preferences of proteins depend on the background mutations of protein homologs." @default.
- W2967372260 created "2019-08-22" @default.
- W2967372260 creator A5075863884 @default.
- W2967372260 date "2019-01-01" @default.
- W2967372260 modified "2023-10-14" @default.
- W2967372260 title "Gene Families, Epistasis and the Amino Acid Preferences of Protein Homologs" @default.
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- W2967372260 doi "https://doi.org/10.1177/1176934319870485" @default.
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