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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/123456789/9867
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dc.contributor.authorGalanis, A. S.en
dc.contributor.authorSpyroulias, G. A.en
dc.contributor.authorPierattelli, R.en
dc.contributor.authorTzakos, A.en
dc.contributor.authorTroganis, A.en
dc.contributor.authorGerothanassis, I. P.en
dc.contributor.authorPairas, G.en
dc.contributor.authorManessi-Zoupa, E.en
dc.contributor.authorCordopatis, P.en
dc.date.accessioned2015-11-24T16:52:19Z-
dc.date.available2015-11-24T16:52:19Z-
dc.identifier.issn0006-3525-
dc.identifier.urihttps://olympias.lib.uoi.gr/jspui/handle/123456789/9867-
dc.rightsDefault Licence-
dc.subjectAmino Acid Motifsen
dc.subjectAmino Acid Sequenceen
dc.subjectBinding Sitesen
dc.subjectHumansen
dc.subjectIsoenzymes/chemistry/metabolismen
dc.subjectModels, Molecularen
dc.subjectMolecular Sequence Dataen
dc.subjectNuclear Magnetic Resonance, Biomolecular/*methodsen
dc.subjectPeptide Fragments/chemical synthesis/chemistry/metabolismen
dc.subjectPeptide Mappingen
dc.subjectPeptidyl-Dipeptidase A/*chemistry/*metabolismen
dc.subjectProtein Conformationen
dc.subjectProtonsen
dc.subjectSequence Homology, Amino Aciden
dc.subjectSolutionsen
dc.subjectThermolysin/chemistry/metabolismen
dc.subjectZinc/*metabolismen
dc.titleZinc binding in peptide models of angiotensin-I converting enzyme active sites studied through 1H-NMR and chemical shift perturbation mappingen
heal.typejournalArticle-
heal.type.enJournal articleen
heal.type.elΆρθρο Περιοδικούel
heal.identifier.primary10.1002/bip.10362-
heal.identifier.secondaryhttp://www.ncbi.nlm.nih.gov/pubmed/12767125-
heal.identifier.secondaryhttp://onlinelibrary.wiley.com/store/10.1002/bip.10362/asset/10362_ftp.pdf?v=1&t=hncvy7vb&s=fd90fe93933f47e4e52fe39b959ac1a2c1a04828-
heal.languageen-
heal.accesscampus-
heal.recordProviderΠανεπιστήμιο Ιωαννίνων. Σχολή Θετικών Επιστημών. Τμήμα Χημείαςel
heal.publicationDate2003-
heal.abstractWe report the design and synthesis through solid phase 9-flourenylmethoxycarbonyl (Fmoc) chemistry of the two angiotensin-I converting enzyme active sites possessing the general sequence HEMGHX(23)EAIGDX(3). Their zinc-binding properties were monitored in solution through high-resolution (1)H-NMR. The obtained data were analyzed in terms of chemical shift differences. The results indicate that zinc binds to the HEMGH and the EAIGD characteristic motifs, and suggest possible coordination modes of zinc in the native enzyme.en
heal.publisherWileyen
heal.journalNameBiopolymersen
heal.journalTypepeer reviewed-
heal.fullTextAvailabilityTRUE-
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