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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/123456789/9868
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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.accessioned2015-11-24T16:52:20Z-
dc.date.available2015-11-24T16:52:20Z-
dc.identifier.issn0006-3525-
dc.identifier.urihttps://olympias.lib.uoi.gr/jspui/handle/123456789/9868-
dc.rightsDefault Licence-
dc.subjectangiotensin-i converting enzymeen
dc.subjectrenin-angiotensin systemen
dc.subjectzinc binding motifsen
dc.subjectnmren
dc.subjectchemical shift indexen
dc.subjectprotein secondary structureen
dc.subjectnmr-spectroscopyen
dc.subjectthermolysinen
dc.subjectresolutionen
dc.subjectbradykininen
dc.titleZinc binding in peptide models of angiotensin-I converting enzyme active sites studied through H-1-NMR and chemical shift perturbation mappingen
heal.typejournalArticle-
heal.type.enJournal articleen
heal.type.elΆρθρο Περιοδικούel
heal.identifier.primaryDoi 10.1002/Bip.10362-
heal.identifier.secondary<Go to ISI>://000183163500007-
heal.identifier.secondaryhttp://onlinelibrary.wiley.com/store/10.1002/bip.10362/asset/10362_ftp.pdf?v=1&t=hmn3jpj8&s=f97bf82e0c0ed1fe0c2668bb5f8de0564faaaaae-
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 H-1-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. (C) 2003 Wiley Periodicals, Inc.en
heal.publisherWiley-Blackwellen
heal.journalNameBiopolymersen
heal.journalTypepeer reviewed-
heal.fullTextAvailabilityTRUE-
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