[From sequence variability to structural and functional prediction: modeling of homologous protein families]

Abstract

Thanks to next-generation sequencing, the number of sequenced genomes grows rapidly, providing in particular ample examples for the sequence variability between homologous proteins. This article discusses data-driven probabilistic sequence models, which are able to extract a multitude of information from sequence data alone, including (i) structural features like residue-residue contacts, which are formed in the folded protein, (ii) protein-protein interaction interfaces and (iii) phenotypic effects of amino-acid substitutions in proteins.