H-1-Nmr Studies on Arginine Tripeptides - Evidence for Guanidinium C-Terminal Carboxylate Interactions

dc.contributor.authorTsikaris, V.en
dc.contributor.authorSakarellos-Daitsiotis, M.en
dc.contributor.authorPanoupomonis, E.en
dc.contributor.authorDetsikas, E.en
dc.contributor.authorSakarellos, C.en
dc.contributor.authorCung, M. T.en
dc.contributor.authorMarraud, M.en
dc.date.accessioned2015-11-24T16:38:35Z
dc.date.available2015-11-24T16:38:35Z
dc.identifier.issn1040-5704-
dc.identifier.urihttps://olympias.lib.uoi.gr/jspui/handle/123456789/8063
dc.rightsDefault Licence-
dc.subjectsequential polypeptidesen
dc.subjectcircular-dichroismen
dc.subjectcrystal-structuresen
dc.subjecthistone modelsen
dc.titleH-1-Nmr Studies on Arginine Tripeptides - Evidence for Guanidinium C-Terminal Carboxylate Interactionsen
heal.abstractGuanidinium-C -terminal carboxylate interactions are involved in the establishment of the secondary structure of various biologically active peptide sequences. The conformational properties of a series of arginine-containing tripeptides, L-Arg-X-Gly (X = L-Ala, Val, Leu), in DMSO solutions at physiological pH, have been studied by means of 1D and 2D H-1-NMR spectroscopy. Measurements of the chemical shifts, NOE effects and temperature coefficients showed that the ArgN(epsilon)H and ArgN(eta)H-2 groups form two hydrogen bonds with the C-terminal carboxylate moiety, whereas the ArgN(alpha)-terminal nitrogen is in the amino state. Our results point out the significant contribution of the C-terminal carboxylate group, at physiological pH, in the stabilization of the Arg side-chain structure in peptides simultaneously containing arginine residues and carboxy terminal sequences.en
heal.accesscampus-
heal.fullTextAvailabilityTRUE-
heal.identifier.secondary<Go to ISI>://A1992HL96700006-
heal.journalNamePeptide Researchen
heal.journalTypepeer reviewed-
heal.languageen-
heal.publicationDate1992-
heal.publisherEaton Publishingen
heal.recordProviderΠανεπιστήμιο Ιωαννίνων. Σχολή Θετικών Επιστημών. Τμήμα Χημείαςel
heal.typejournalArticle-
heal.type.elΆρθρο Περιοδικούel
heal.type.enJournal articleen

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