Seibutsu Butsuri
Online ISSN : 1347-4219
Print ISSN : 0582-4052
ISSN-L : 0582-4052
Review
Prediction of Residue-Contacts Based on Coevolution between Amino Acid Sites: Toward the Prediction of Protein Structure
Sanzo MIYAZAWA
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JOURNAL FREE ACCESS
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2014 Volume 54 Issue 2 Pages 091-095

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Abstract

Residue-residue interactions that fold a protein into a unique three-dimensional structure and make it play a specific function put structural and functional constraints in varying degrees on each residue site. Coevolution between closely-located sites caused by such selective constraints is recorded in amino acid orders of homologous sequences and also in the evolutionary trace of amino acid substitutions. A challenge for predicting residue contacts through coevolving site pairs is to extract direct dependences between sites by removing phylogenetic correlations and indirect dependences through other residues within a protein or even through other molecules. Recent attempts, particularly by detecting co-substitutions, are reviewed.

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© 2014 by THE BIOPHYSICAL SOCIETY OF JAPAN
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