On the Role of Structural Zinc in Bis(Cysteinyl) Protein Sequences

✍ Scribed by Dr. Axel Meißner; Prof. Dr. Wolfgang Haehnel; Prof. Dr. Heinrich Vahrenkamp

• Publisher: John Wiley and Sons
• Year: 1997
• Tongue: English
• Weight: 865 KB
• Volume: 3
• Category: Article
• ISSN: 0947-6539
• DOI: 10.1002/chem.19970030215

✦ Synopsis

Besides its functional role in metal or whether the zinc ion provides the pects of this question by synthesizing zinc many hydrolytic metalloenzymes, zinc structurizing power and stability for the complexes of small model peptides and by acts as a structural component by being observed peptide conformations. We have determining their structures in solution by attached to bis(cysteiny1) protein se-addressed the coordination chemistry as-2 D NMR spectroscopy. The peptides quences in some of the same enzymes, and chosen were of the terminally protected in other metalloproteins and zinc fingers, bis(cysteiny1) type: Cys-Cys, Cys-Gly-Keywords and by being an essential constituent in Cys, Cys-Phe-Cys, and Cys-Gly-Ile-Cys.

NMR spectroscopypeptidesmetallothioneins. It is not always obvious The zinc ions fold these peptides into protein structures * structure eluciwhether the zinc-binding proteins are prestructures that can be superimposed on dation * zinc organized for the incorporation of the those of the natural proteins.