Please use this identifier to cite or link to this item: https://repositorio.unifesp.br/handle/11600/26694
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dc.contributor.authorPertinhez, Thelma A.
dc.contributor.authorKrybus, Regina
dc.contributor.authorCilli, Eduardo Maffud [UNIFESP]
dc.contributor.authorPaiva, Antonio Cechelli de Mattos [UNIFESP]
dc.contributor.authorNakaie, Clovis Ryuichi [UNIFESP]
dc.contributor.authorFranzoni, Lorella
dc.contributor.authorSartor, Giorgio
dc.contributor.authorSpisni, Alberto
dc.contributor.authorSchreier, Shirley
dc.date.accessioned2016-01-24T12:33:10Z
dc.date.available2016-01-24T12:33:10Z
dc.date.issued2002-01-01
dc.identifierhttp://dx.doi.org/10.1002/psc.364
dc.identifier.citationJournal of Peptide Science. W Sussex: John Wiley & Sons Ltd, v. 8, n. 1, p. 23-35, 2002.
dc.identifier.issn1075-2617
dc.identifier.urihttp://repositorio.unifesp.br/handle/11600/26694
dc.description.abstractThe conformation of three synthetic peptides encompassing the proximal and distal half of the third intracellular loop (Ni3 and Ci3) and a portion of the cytoplasmic tail (fCT) of the angiotensin II AT(1A) receptor has been studied using circular dischroism and fluorescence spectroscopies. the results show that the conformation of the peptides is modulated in various ways by the environmental conditions (pH, ionic strength and dielectric constant). Indeed, Ni3 and fCT fold into helical structures that possess distinct stability and polarity due to the diverse forces involved: mainly polar interactions in the first case and a combination of polar and hydrophobic interactions in the second. the presence of these various features also produce distinct intermolecular interactions. Ci3, instead, exists as an ensemble of partially folded states in equilibrium. Since the corresponding regions of the angiotensin II AT(1A) receptor are known to play an important role in the receptor function, due to their ability to undergo conformational changes, these data provide some new clues about their different conformational plasticity. Copyright (C) 2002 European Peptide Society and John Wiley Sons, Ltd.en
dc.format.extent23-35
dc.language.isoeng
dc.publisherWiley-Blackwell
dc.relation.ispartofJournal of Peptide Science
dc.rightsAcesso restrito
dc.subjectangiotensin II AT(1A) receptoren
dc.subjectcircular dichroismen
dc.subjectfluorescenceen
dc.subjectG-proteinen
dc.titleConformational flexibility of three cytoplasmic segments of the angiotensin II AT(1A) receptor: A circular dichroism and fluorescence spectroscopy studyen
dc.typeArtigo
dc.rights.licensehttp://olabout.wiley.com/WileyCDA/Section/id-406071.html
dc.contributor.institutionUniv Parma
dc.contributor.institutionLNLS
dc.contributor.institutionUniversidade de São Paulo (USP)
dc.contributor.institutionUniversidade Federal de São Paulo (UNIFESP)
dc.description.affiliationUniv Parma, Dept Expt Med, Sect Chem & Struct Biochem, I-43100 Parma, Italy
dc.description.affiliationLNLS, Ctr Mol & Struct Biol, BR-13084971 Campinas, Brazil
dc.description.affiliationUniv São Paulo, Dept Biochem, Inst Chem, BR-05599970 São Paulo, Brazil
dc.description.affiliationUniversidade Federal de São Paulo, Dept Biophys, São Paulo, Brazil
dc.description.affiliationUnifespUniversidade Federal de São Paulo, Dept Biophys, São Paulo, Brazil
dc.identifier.doi10.1002/psc.364
dc.description.sourceWeb of Science
dc.identifier.wosWOS:000173575400004
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