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dc.contributor.authorLiu, Jen-Weien_US
dc.contributor.authorLin, Jau-Jien_US
dc.contributor.authorCheng, Chih-Wenen_US
dc.contributor.authorLin, Yu-Fengen_US
dc.contributor.authorHwang, Jenn-Kangen_US
dc.contributor.authorHuang, Tsun-Tsaoen_US
dc.date.accessioned2018-08-21T05:54:26Z-
dc.date.available2018-08-21T05:54:26Z-
dc.date.issued2017-09-01en_US
dc.identifier.issn0887-3585en_US
dc.identifier.urihttp://dx.doi.org/10.1002/prot.25329en_US
dc.identifier.urihttp://hdl.handle.net/11536/145945-
dc.description.abstractResidues that are crucial to protein function or structure are usually evolutionarily conserved. To identify the important residues in protein, sequence conservation is estimated, and current methods rely upon the unbiased collection of homologous sequences. Surprisingly, our previous studies have shown that the sequence conservation is closely correlated with the weighted contact number (WCN), a measure of packing density for residue's structural environment, calculated only based on the C-alpha positions of a protein structure. Moreover, studies have shown that sequence conservation is correlated with environment-related structural properties calculated based on different protein substructures, such as a protein's all atoms, backbone atoms, side-chain atoms, or side-chain centroid. To know whether the C-alpha atomic positions are adequate to show the relationship between residue environment and sequence conservation or not, here we compared C-alpha atoms with other substructures in their contributions to the sequence conservation. Our results show that C-alpha positions are substantially equivalent to the other substructures in calculations of various measures of residue environment. As a result, the overlapping contributions between C-alpha atoms and the other substructures are high. yielding similar structure-conservation relationship. Take the WCN as an example, the average overlapping contribution to sequence conservation is 87% between C-alpha, and all-atom substructures. These results indicate that only C-alpha atoms of a protein structure could reflect sequence conservation at the residue level.en_US
dc.language.isoen_USen_US
dc.subjectcontact numberen_US
dc.subjectresidue conservationen_US
dc.subjectresidue structural environmenten_US
dc.subjectstructure-evolution relationshipen_US
dc.subjectVoronoi volumeen_US
dc.subjectweighted contact numberen_US
dc.titleOn the relationship between residue structural environment and sequence conservation in proteinsen_US
dc.typeArticleen_US
dc.identifier.doi10.1002/prot.25329en_US
dc.identifier.journalPROTEINS-STRUCTURE FUNCTION AND BIOINFORMATICSen_US
dc.citation.volume85en_US
dc.citation.spage1713en_US
dc.citation.epage1723en_US
dc.contributor.department生物科技學院zh_TW
dc.contributor.department生物資訊及系統生物研究所zh_TW
dc.contributor.departmentCollege of Biological Science and Technologyen_US
dc.contributor.departmentInstitude of Bioinformatics and Systems Biologyen_US
dc.identifier.wosnumberWOS:000408033200010en_US
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