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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/123456789/9918
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dc.contributor.authorTsikaris, V.en
dc.contributor.authorTroganis, A.en
dc.contributor.authorMoussis, V.en
dc.contributor.authorPanou-Pomonis, E.en
dc.contributor.authorSakarellos-Daitsiotis, M.en
dc.contributor.authorSakarellos, C.en
dc.date.accessioned2015-11-24T16:52:42Z-
dc.date.available2015-11-24T16:52:42Z-
dc.identifier.issn0006-3525-
dc.identifier.urihttps://olympias.lib.uoi.gr/jspui/handle/123456789/9918-
dc.rightsDefault Licence-
dc.subjecto-17 hydrogen bondingen
dc.subjectarginine interactionsen
dc.subjectside-chain-backbone interactionsen
dc.subjectlh-rh modelen
dc.subjecto-17-labeled peptidesen
dc.subjectcarboxylate interactionsen
dc.subjectcrystal-structuresen
dc.subjectaqueous-solutionen
dc.subjectleu-enkephalinen
dc.subjectarginineen
dc.subjectnmren
dc.subjectfibronectinen
dc.subjectsequence-(250-257)en
dc.subjectguanidiniumen
dc.subjectproteinsen
dc.titleArg side-chain-backbone interactions evidenced in model peptides by O-17-NMR spectroscopyen
heal.typejournalArticle-
heal.type.enJournal articleen
heal.type.elΆρθρο Περιοδικούel
heal.identifier.secondary<Go to ISI>://000084994700003-
heal.identifier.secondaryhttp://onlinelibrary.wiley.com/store/10.1002/(SICI)1097-0282(200002)53:2<135::AID-BIP3>3.0.CO;2-5/asset/3_ftp.pdf?v=1&t=h0e0vgqv&s=e7811fbbd4e335f76621af19abf1cd9aef8ef3a6-
heal.languageen-
heal.accesscampus-
heal.recordProviderΠανεπιστήμιο Ιωαννίνων. Σχολή Θετικών Επιστημών. Τμήμα Χημείαςel
heal.publicationDate2000-
heal.abstractThe guanidinium group of arginine possesses a variety of biochemical functions, either by participating in direct interactions in recognition processes, or by stabilizing secondary structures. Three model compounds, selectively O-17 enriched, Ac-Arg-Ala-[O-17]Pro-NH2 (1), Piv-Arg-Pro-[O-17]Gly-NH2 (2) (C-terminal segment of the luteinizing hormone releasing hormone), and Piv-Nle-Pro-[O-17]Gly-NH2 (3), were prepared and studied by O-17-nmr spectroscopy. A direct hydrogen-bonded interaction between the Arg side chain and the carbonyl main chain carboxy-terminus was found, thus confirming the tendency of Arg to participate in proton-acceptor functions. (C) 2000 John Wiley & Sons, Inc.en
heal.publisherWileyen
heal.journalNameBiopolymersen
heal.journalTypepeer reviewed-
heal.fullTextAvailabilityTRUE-
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