生物物理
Online ISSN : 1347-4219
Print ISSN : 0582-4052
ISSN-L : 0582-4052
総説
アミノ酸座位間における共進化に基づく残基間コンタクト予測:タンパク質立体構造予測にむけて
宮澤 三造
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ジャーナル フリー

2014 年 54 巻 2 号 p. 091-095

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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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