Inverse statistical physics of protein sequences: a key issues review

In the course of evolution, proteins undergo important changes in their amino acid sequences, while their three-dimensional folded structure and their biological function remain remarkably conserved. Thanks to modern sequencing techniques, sequence data accumulate at unprecedented pace. This provide...

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Vydáno v:Reports on progress in physics Ročník 81; číslo 3; s. 032601
Hlavní autoři: Cocco, Simona, Feinauer, Christoph, Figliuzzi, Matteo, Monasson, Rémi, Weigt, Martin
Médium: Journal Article
Jazyk:angličtina
Vydáno: England 01.03.2018
ISSN:1361-6633, 1361-6633
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Shrnutí:In the course of evolution, proteins undergo important changes in their amino acid sequences, while their three-dimensional folded structure and their biological function remain remarkably conserved. Thanks to modern sequencing techniques, sequence data accumulate at unprecedented pace. This provides large sets of so-called homologous, i.e. evolutionarily related protein sequences, to which methods of inverse statistical physics can be applied. Using sequence data as the basis for the inference of Boltzmann distributions from samples of microscopic configurations or observables, it is possible to extract information about evolutionary constraints and thus protein function and structure. Here we give an overview over some biologically important questions, and how statistical-mechanics inspired modeling approaches can help to answer them. Finally, we discuss some open questions, which we expect to be addressed over the next years.
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ISSN:1361-6633
1361-6633
DOI:10.1088/1361-6633/aa9965