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Updated: May 8, 2026

Structure and Coordination Determination of Peptide-metal Complexes Using 1D and 2D 1H NMR
Published on: December 16, 2013
On the role of structural zinc in bis(cysteinyl) protein sequences
A Meißner1, W Haehnel, H Vahrenkamp
1Institut für Anorganische und Analytische Chemie der Universität Freiburg Albertstr. 21, D-79104 Freiburg (Germany), Fax: Int. code +(761)203-6001.
Abstract:
Besides its functional role in many hydrolytic metalloenzymes, zinc acts as a structural component by being attached to bis(cysteinyl) protein sequences in some of the same enzymes, and in other metalloproteins and zinc fingers, and by being an essential constituent in metallothioneins. It is not always obvious whether the zinc-binding proteins are pre-organized for the incorporation of the metal or whether the zinc ion provides the structurizing power and stability for the observed peptide conformations. We have addressed the coordination chemistry aspects of this question by synthesizing zinc complexes of small model peptides and by determining their structures in solution by 2D NMR spectroscopy. The peptides chosen were of the terminally protected bis(cysteinyl) type: Cys-Cys, Cys-Gly-Cys, Cys-Phe-Cys, and Cys-Gly-Ile-Cys. The zinc ions fold these peptides into structures that can be superimposed on those of the natural proteins.
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