Please use this identifier to cite or link to this item: https://olympias.lib.uoi.gr/jspui/handle/123456789/19732
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dc.contributor.authorCung, M. T.en
dc.contributor.authorMarraud, M.en
dc.contributor.authorHadjidakis, I.en
dc.contributor.authorBairaktari, E.en
dc.contributor.authorSakarellos, C.en
dc.contributor.authorKokla, A.en
dc.contributor.authorTzartos, S.en
dc.date.accessioned2015-11-24T19:01:51Z-
dc.date.available2015-11-24T19:01:51Z-
dc.identifier.issn0006-3525-
dc.identifier.urihttps://olympias.lib.uoi.gr/jspui/handle/123456789/19732-
dc.rightsDefault Licence-
dc.subjectAmino Acid Sequenceen
dc.subject*Epitopesen
dc.subjectHydrogenen
dc.subjectMagnetic Resonance Spectroscopy/methodsen
dc.subjectMolecular Sequence Dataen
dc.subject*Oligopeptides/chemical synthesisen
dc.subjectProtein Conformationen
dc.subject*Receptors, Cholinergic/immunologyen
dc.titleTwo-dimensional 1H-NMR study of synthetic peptides containing the main immunogenic region of the Torpedo acetylcholine receptoren
heal.typejournalArticle-
heal.type.enJournal articleen
heal.type.elΆρθρο Περιοδικούel
heal.identifier.primary10.1002/bip.360280141-
heal.identifier.secondaryhttp://www.ncbi.nlm.nih.gov/pubmed/2470436-
heal.identifier.secondaryhttp://onlinelibrary.wiley.com/store/10.1002/bip.360280141/asset/360280141_ftp.pdf?v=1&t=h0aky8f7&s=f72ebd3b4ed3bdc13fe067ce61fb31af2d8e93d4-
heal.languageen-
heal.accesscampus-
heal.recordProviderΠανεπιστήμιο Ιωαννίνων. Σχολή Επιστημών Υγείας. Τμήμα Ιατρικήςel
heal.publicationDate1989-
heal.abstractA comparative 1H-NMR spectral study of a synthetic decapeptide containing the main immunogenic region of the Torpedo acetylcholine receptor (AChR; WNPADYGGIK, representing the alpha 67-76 fragment of Torpedo AChR) with four analogous peptides (WNP3-D5YGGIK, WNPAA5YGGIK, WNPADYGGA9K, and WNPD4DYGGV9K) has been carried out in dimethyl sulfoxide. One- and two-dimensional nmr experiments [correlated spectroscopy (COSY), relayed COSY, and phase-sensitive nuclear Overhauser enhancement spectroscopy (NOESY)] were performed to obtain complete assignments of the proton resonances. The presence of strong and multiple short- and long-range NOEs, and especially a strong long-range NOE between the two Asn2-C alpha H and Gly7-C alpha H protons, argues in favor of a rigid folded structure in all five cases. Temperature dependence measurements indicate the existence of three intramolecular interactions involving the Asp3, Gly8, and Lys10 amide protons.en
heal.journalNameBiopolymersen
heal.journalTypepeer-reviewed-
heal.fullTextAvailabilityTRUE-
Appears in Collections:Άρθρα σε επιστημονικά περιοδικά ( Ανοικτά) - ΙΑΤ

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