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DC Field | Value | Language |
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dc.contributor.author | Galanis, A. S. | en |
dc.contributor.author | Spyroulias, G. A. | en |
dc.contributor.author | Pierattelli, R. | en |
dc.contributor.author | Tzakos, A. | en |
dc.contributor.author | Troganis, A. | en |
dc.contributor.author | Gerothanassis, I. P. | en |
dc.contributor.author | Pairas, G. | en |
dc.contributor.author | Manessi-Zoupa, E. | en |
dc.contributor.author | Cordopatis, P. | en |
dc.date.accessioned | 2015-11-24T16:52:20Z | - |
dc.date.available | 2015-11-24T16:52:20Z | - |
dc.identifier.issn | 0006-3525 | - |
dc.identifier.uri | https://olympias.lib.uoi.gr/jspui/handle/123456789/9868 | - |
dc.rights | Default Licence | - |
dc.subject | angiotensin-i converting enzyme | en |
dc.subject | renin-angiotensin system | en |
dc.subject | zinc binding motifs | en |
dc.subject | nmr | en |
dc.subject | chemical shift index | en |
dc.subject | protein secondary structure | en |
dc.subject | nmr-spectroscopy | en |
dc.subject | thermolysin | en |
dc.subject | resolution | en |
dc.subject | bradykinin | en |
dc.title | Zinc binding in peptide models of angiotensin-I converting enzyme active sites studied through H-1-NMR and chemical shift perturbation mapping | en |
heal.type | journalArticle | - |
heal.type.en | Journal article | en |
heal.type.el | Άρθρο Περιοδικού | el |
heal.identifier.primary | Doi 10.1002/Bip.10362 | - |
heal.identifier.secondary | <Go to ISI>://000183163500007 | - |
heal.identifier.secondary | http://onlinelibrary.wiley.com/store/10.1002/bip.10362/asset/10362_ftp.pdf?v=1&t=hmn3jpj8&s=f97bf82e0c0ed1fe0c2668bb5f8de0564faaaaae | - |
heal.language | en | - |
heal.access | campus | - |
heal.recordProvider | Πανεπιστήμιο Ιωαννίνων. Σχολή Θετικών Επιστημών. Τμήμα Χημείας | el |
heal.publicationDate | 2003 | - |
heal.abstract | We 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.publisher | Wiley-Blackwell | en |
heal.journalName | Biopolymers | en |
heal.journalType | peer reviewed | - |
heal.fullTextAvailability | TRUE | - |
Appears in Collections: | Άρθρα σε επιστημονικά περιοδικά ( Ανοικτά). ΧΗΜ |
Files in This Item:
File | Description | Size | Format | |
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Galanis-2003-Zinc binding in pept.pdf | 1.12 MB | Adobe PDF | View/Open Request a copy |
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