Use este identificador para citar ou linkar para este item: http://www.alice.cnptia.embrapa.br/alice/handle/doc/876510
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dc.contributor.authorLEITE, V.pt_BR
dc.contributor.authorSILVA, R.pt_BR
dc.contributor.authorYAMAGISHI, M.pt_BR
dc.contributor.authorCHAHINE, J.pt_BR
dc.date.accessioned2011-07-26T01:04:04Z-
dc.date.available2011-07-26T01:04:04Z-
dc.date.created2011-02-09pt_BR
dc.date.issued2010pt_BR
dc.identifier.citationIn: ANNUAL SYMPOSIUM OF THE PROTEIN SOCIETY, 24., 2010, California. [Abstracts...]. [S.l.: s.n.], 2010.pt_BR
dc.identifier.urihttp://www.alice.cnptia.embrapa.br/alice/handle/doc/876510pt_BR
dc.descriptionEffect of mutations on the stability of proteins is a crucial issue in protein evolution. Such effects depend strongly on the overall hydrophobic protein character. In a recent work we suggested two scenarios for folding with distinct protein evolution consequences [1]. Under low hydrophobic conditions, proteins collapse concomitantly with the formation of their native state, and are less robust to mutations. This feature implies higher homology among proteins of different species. On the other limit, at high hydrophobicity, proteins collapse before folding, and this case they are more susceptible to mutations, suggesting lower homology among proteins of different species. In this work we investigate this conjecture studying the homology of four proteins for 41 different species, correlating it with their average hydrophobicity. The proteins studied were lysozyme, cytochrome-c, myoglobin and histone H3, and we used eighteen different hydrophobic scales. Along with the homology calculation, a comparison of structural similarity (rmsd) was also carried out. The results confirm the above suggestion, indicating that proteins at low hydrophobicity display low variations on sequences and conformations. On the other hand, at high hydrophobicity, proteins exhibit high variability on sequences and conformations.pt_BR
dc.language.isoengeng
dc.rightsopenAccesseng
dc.subjectEvolução de proteínapt_BR
dc.subjectHidrofobicidade em proteínaspt_BR
dc.titleRole of hydrophobicity in protein evolution.pt_BR
dc.typeResumo em anais e proceedingspt_BR
dc.date.updated2020-01-24T11:11:11Zpt_BR
dc.subject.nalthesaurusProteinspt_BR
riaa.ainfo.id876510pt_BR
riaa.ainfo.lastupdate2020-01-24 -02:00:00pt_BR
dc.contributor.institutionVITOR LEITE, IBILCE/UNESP; RICARDO SILVA, IBILCE/UNESP; MICHEL YAMAGISHI, CNPTIA; JORGE CHAHINE, IBILCE/UNESP.pt_BR
Aparece nas coleções:Resumo em anais de congresso (CNPTIA)

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