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Zinc binding in peptide models of angiotensin‐I converting enzyme active sites studied through 1 H‐NMR and chemical shift perturbation mapping
Author(s) -
Galanis Athanassios S.,
Spyroulias Georgios A.,
Pierattelli Roberta,
Tzakos Andreas,
Troganis Anastassios,
Gerothanassis Ioannis P.,
Pairas George,
ManessiZoupa Evy,
Cordopatis Paul
Publication year - 2003
Publication title -
biopolymers
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.556
H-Index - 125
eISSN - 1097-0282
pISSN - 0006-3525
DOI - 10.1002/bip.10362
Subject(s) - chemistry , zinc , active site , enzyme , peptide , binding site , nuclear magnetic resonance spectroscopy , stereochemistry , crystallography , biochemistry , organic chemistry
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 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. © 2003 Wiley Periodicals, Inc. Biopolymers 69: 244–252, 2003