Please use this identifier to cite or link to this item: https://olympias.lib.uoi.gr/jspui/handle/123456789/10134
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dc.contributor.authorV.Tsikarisen
dc.contributor.authorM.Sakarellos-Daitsiotisen
dc.contributor.authorE.Panou-Pomonisen
dc.contributor.authorE.Detsikasen
dc.contributor.authorC. Sakarellosen
dc.contributor.authorM.T. Cungen
dc.contributor.authorM. Marrauden
dc.date.accessioned2015-11-24T16:54:14Z-
dc.date.available2015-11-24T16:54:14Z-
dc.identifier.urihttps://olympias.lib.uoi.gr/jspui/handle/123456789/10134-
dc.rightsDefault Licence-
dc.title1H-NMR studies on arginine tripeptides: evidence for guanidinium-C-terminal carboxylate interactionsen
heal.typejournalArticle-
heal.type.enJournal articleen
heal.type.elΆρθρο Περιοδικούel
heal.identifier.secondaryhttp://www.ncbi.nlm.nih.gov/pubmed/1581638-
heal.languageen-
heal.accesscampus-
heal.recordProviderΠανεπιστήμιο Ιωαννίνων. Σχολή Θετικών Επιστημών. Τμήμα Χημείαςel
heal.publicationDate1992-
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 1H-NMR spectroscopy. Measurements of the chemical shifts, NOE effects and temperature coefficients showed that the ArgN epsilon H and ArgN eta H2 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.journalNamePeptide Researchen
heal.journalTypepeer reviewed-
heal.fullTextAvailabilityTRUE-
Appears in Collections:Άρθρα σε επιστημονικά περιοδικά ( Ανοικτά)

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