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Curr Opin Struct Biol. 2018 Feb;48:141-148. doi: 10.1016/j.sbi.2018.01.001. Epub 2018 Jan 30.

Evolutionary mechanisms studied through protein fitness landscapes.

Author information

1
Department of Biochemistry and Molecular Pharmacology, University of Massachusetts Medical School, 364 Plantation St, Worcester, MA 01605, United States.
2
Department of Biochemistry and Molecular Pharmacology, University of Massachusetts Medical School, 364 Plantation St, Worcester, MA 01605, United States. Electronic address: Dan.Bolon@umassmed.edu.

Abstract

Biology has, and continues to be, shaped by evolutionary mechanisms. Within the past decade, local fitness landscapes have become experimentally tractable and are providing new perspectives on evolutionary mechanisms. Powered by next-generation sequencing, the impacts of all individual amino acid substitutions on function have been quantified for dozens of proteins. These fitness maps have been utilized to investigate the biophysical underpinnings of existing protein function as well as the appearance and enhancement of new protein functions. This review highlights emerging trends from this rapidly growing area of research, including an expanded understanding of the biophysical mechanisms underlying existing and new protein function, the roles epistasis and adaptation play in shaping evolution, and the prediction of disease-causing alleles in humans.

PMID:
29351890
DOI:
10.1016/j.sbi.2018.01.001

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