Antigen-Antibody Interactions Study by 2d-H-1 Nmr - Molecular Recognition between Decapeptide Analogs of the Acetylcholine-Receptor Alpha-67-76 Fragment and the Anti-Achr Antibodies

dc.contributor.authorCung, M. T.en
dc.contributor.authorMarraud, M.en
dc.contributor.authorTsikaris, V.en
dc.contributor.authorSakarellos, C.en
dc.contributor.authorPapadouli, I.en
dc.contributor.authorTzartos, S. J.en
dc.date.accessioned2015-11-24T16:51:02Z
dc.date.available2015-11-24T16:51:02Z
dc.identifier.issn0021-7689-
dc.identifier.urihttps://olympias.lib.uoi.gr/jspui/handle/123456789/9677
dc.rightsDefault Licence-
dc.subjectmain immunogenic regionen
dc.subjecttwo-dimensional h-1-nmren
dc.subjectmonoclonal-antibodiesen
dc.subjectlocalizationen
dc.subjectresiduesen
dc.titleAntigen-Antibody Interactions Study by 2d-H-1 Nmr - Molecular Recognition between Decapeptide Analogs of the Acetylcholine-Receptor Alpha-67-76 Fragment and the Anti-Achr Antibodiesen
heal.abstractTo investigate the conformational role of the alpha-67-76 decapeptide fragment of the Torpedo acetylcholine receptor (AChR), each residue of the WNPADYGGIK sequence was substituted step by step by alanine. The 2D-NMR conformational study of the peptide analogues in the free state was carried out in DMSO. The COSY and transferred NOESY were applied to study the interactions of a monoclonal antibody (mAb6) directed against the main immunogenic region (MIR) of the AChR and five decapeptide analogues from the MIR.en
heal.accesscampus-
heal.fullTextAvailabilityTRUE-
heal.identifier.secondary<Go to ISI>://A1992HJ07500005-
heal.journalNameJournal De Chimie Physique Et De Physico-Chimie Biologiqueen
heal.journalTypepeer reviewed-
heal.languageFrench-
heal.publicationDate1992-
heal.recordProviderΠανεπιστήμιο Ιωαννίνων. Σχολή Θετικών Επιστημών. Τμήμα Χημείαςel
heal.typejournalArticle-
heal.type.elΆρθρο Περιοδικούel
heal.type.enJournal articleen

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