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On the Role of Structural Zinc in Bis(Cysteinyl) Protein Sequences
Author(s) -
Meißner Axel,
Haehnel Wolfgang,
Vahrenkamp Heinrich
Publication year - 1997
Publication title -
chemistry – a european journal
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.687
H-Index - 242
eISSN - 1521-3765
pISSN - 0947-6539
DOI - 10.1002/chem.19970030215
Subject(s) - zinc , chemistry , metalloprotein , peptide , nuclear magnetic resonance spectroscopy , cysteine , zinc finger , enzyme , protein structure , biochemistry , combinatorial chemistry , stereochemistry , organic chemistry , transcription factor , gene
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.