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• W2767568106 abstract "Protein function arises from a poorly defined pattern of cooperative energetic interactions between amino acid residues. Strategies for deducing this pattern have been proposed, but lack of benchmark data has limited experimental verification. Here, we extend deep-mutation technologies to enable measurement of many thousands of pairwise amino acid couplings in members of a protein family. The data show that despite great evolutionary divergence, homologous proteins conserve a sparse, spatially distributed network of cooperative interactions between amino acids that underlies function. This pattern is quantitatively captured in the coevolution of amino acid positions, especially as indicated by the statistical coupling analysis (SCA), providing experimental confirmation of the key tenets of this method. This work establishes a clear link between physical constraints on protein function and sequence analysis, enabling a general practical approach for understanding the structural basis for protein function." @default.
• W2767568106 created "2017-11-17" @default.
• W2767568106 creator A5041945711 @default.
• W2767568106 creator A5050583390 @default.
• W2767568106 date "2017-11-07" @default.
• W2767568106 modified "2023-09-25" @default.
• W2767568106 title "Inferring amino acid interactions underlying protein function" @default.
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• W2767568106 doi "https://doi.org/10.1101/215368" @default.
• W2767568106 hasPublicationYear "2017" @default.
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