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  5. Άρθρα σε επιστημονικά περιοδικά ( Ανοικτά). ΧΗΜ
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Please use this identifier to cite or link to this item: https://olympias.lib.uoi.gr/jspui/handle/123456789/8908
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dc.contributor.authorMylonas, M.en
dc.contributor.authorPlakatouras, J. C.en
dc.contributor.authorHadjiliadis, N.en
dc.contributor.authorKrezel, A.en
dc.contributor.authorBal, W.en
dc.date.accessioned2015-11-24T16:45:18Z-
dc.date.available2015-11-24T16:45:18Z-
dc.identifier.issn0020-1693-
dc.identifier.urihttps://olympias.lib.uoi.gr/jspui/handle/123456789/8908-
dc.rightsDefault Licence-
dc.subjectcu(ii)en
dc.subjecthistone h2aen
dc.subjecthexapeptidesen
dc.subjecthistidineen
dc.subjectpotentiometryen
dc.subjectspectroscopic studiesen
dc.subjectmetal-binding sequenceen
dc.subjectcopper(ii) complexesen
dc.subjectimidazole nitrogensen
dc.subjectl-histidineen
dc.subjectnickel(ii)en
dc.subjectstabilityen
dc.subjectpeptidesen
dc.subjectni(ii)en
dc.subjectaminoen
dc.subjecth3en
dc.titlePotentiometric and spectroscopic studies of the interaction of Cu(II) ions with the hexapeptides AcThrAlaSeHisHisLysNH(2), AcThrGluAlaHisHisLysNH(2), AcThrGluSerAlaHisLysNH(2) and AcThrGluSerHisAlaLysNH(2), models of C-terminal tail of histone H2Aen
heal.typejournalArticle-
heal.type.enJournal articleen
heal.type.elΆρθρο Περιοδικούel
heal.identifier.secondary<Go to ISI>://000179281100009-
heal.languageen-
heal.accesscampus-
heal.recordProviderΠανεπιστήμιο Ιωαννίνων. Σχολή Θετικών Επιστημών. Τμήμα Χημείαςel
heal.publicationDate2002-
heal.abstractThe hexapeptides AcThrAlaSerHisHisLysNH(2), AcThrGluAlaHisHisLysNH(2), AcThrGluSerAlaHisLysNH(2) and AcThrGluSerHisAlaLysNH(2) which represent modifications of the 120-125 sequence of histone H2A were synthesized and their interactions with Cu(II) ions were studied with potentiometric and spectroscopic (UV-Vis, EPR and CD spectroscopy) studies. All peptides coordinate Cu(II) efficiently. At physiological pH, AcThrAlaSerHisHisLysNH(2) forms dimeric species while the rest of the peptides form monomers. The dimer is formed when Cu(II) ions coordinate equatorially through the imidazole nitrogen of the His-4 residue and the amide nitrogens of the Ser-3 and His-4 residues, plus the imidazole nitrogen of the His-5 residue of a second peptide molecule after deprotonation. At higher pH peptides AcThrAlaSerHisHisLysNH(2) and AcThrGluAlaHisHisLysNH(2) are using the second histidine residue for coordination at the apical position while Cu(II) ions coordinate equatorially with the imidazole nitrogen of His-5 or His-4 and three amido nitrogens with the peptides AcThrGluSerAlaHisLysNH(2) and AcThrGluSerHisAlaLysNH(2) (C) 2002 Elsevier Science B.V. All rights reserved.en
heal.publisherElsevieren
heal.journalNameInorganica Chimica Actaen
heal.journalTypepeer reviewed-
heal.fullTextAvailabilityTRUE-
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