Zinc binding in peptide models of angiotensin-I converting enzyme active sites studied through H-1-NMR and chemical shift perturbation mapping

 
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2003 (EN)
Zinc binding in peptide models of angiotensin-I converting enzyme active sites studied through H-1-NMR and chemical shift perturbation mapping (EN)

Galanis, A. S. (EN)

Πανεπιστήμιο Ιωαννίνων. Σχολή Θετικών Επιστημών. Τμήμα Χημείας (EL)
Galanis, A. S. (EN)

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)

angiotensin-i converting enzyme (EN)

Πανεπιστήμιο Ιωαννίνων (EL)
University of Ioannina (EN)

Biopolymers (EN)

English

2003

<Go to ISI>://000183163500007

Wiley-Blackwell (EN)



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