Use este identificador para citar ou linkar para este item: http://www.alice.cnptia.embrapa.br/alice/handle/doc/24589
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dc.contributor.authorHIGA, R. H.eng
dc.contributor.authorTOZZI, C. L.eng
dc.date.accessioned2020-01-16T00:34:49Z-
dc.date.available2020-01-16T00:34:49Z-
dc.date.created2009-02-16
dc.date.issued2008
dc.identifier.citationGenetics and Molecular Research, v. 7, n. 3, p. 898-909, 2008.eng
dc.identifier.urihttp://www.alice.cnptia.embrapa.br/alice/handle/doc/24589-
dc.descriptionComputational methods for predicting protein-protein interaction sites based on structural data are characterized by an accuracy between 70 and 80%. Some experimental studies indicate that only a fraction of the residues, forming clusters in the center of the interaction site, are energetically important for binding. In addition, the analysis of amino acid composition has shown that residues located in the center of the interaction site can be better discriminated from the residues in other parts of the protein surface. In the present study, we implement a simple method to predict interaction site residues exploiting this fact and show that it achieves a very competitive performance compared to other methods using the same dataset and criteria for performance evaluation (success rate of 82.1%).eng
dc.language.isoengeng
dc.rightsopenAccesseng
dc.subjectPrevisão de sítios de interaçãoeng
dc.subjectPrevisão de sítios de ligaçãoeng
dc.subjectSítios de interaçãoeng
dc.subjectSítios de ligaçãoeng
dc.subjectEstrutura da proteínaeng
dc.titleA simple and efficient method for predicting protein-protein interaction sites.eng
dc.typeArtigo de periódicoeng
dc.date.updated2020-01-16T00:34:49Z
dc.subject.thesagroGenéticaeng
dc.subject.thesagroProteínaeng
riaa.ainfo.id24589eng
riaa.ainfo.lastupdate2020-01-15
dc.contributor.institutionROBERTO HIROSHI HIGA, CNPTIA; CLESIO LUIS TOZZI, UNICAMP.eng
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