Investigating metal-binding in proteins by nuclear magnetic resonance |
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Authors: | M Ringkjøbing Jensen M A S Hass D F Hansen J J Led |
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Institution: | 1.Department of Chemistry,University of Copenhagen,Copenhagen ?,Denmark;2.Department of Medical Genetics and Microbiology,University of Toronto,Toronto,Canada |
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Abstract: | Metal ions play a key role for the function of many proteins. The interaction of the metal ion with the protein and its involvement
in the function of the protein vary widely. In some proteins, the metal ion is bound tightly to the ligand residues and may
be the key player in the function of the protein, as in the case of blue copper proteins. In other proteins, the metal ion
is bound only temporarily and loosely to the protein, as in the case of some metalloenzymes and other proteins where the metal
ion acts as a cofactor necessary for the function of the protein. Such proteins are often known as metal ion-activated proteins.
The review focuses on recent nuclear magnetic resonance (NMR) studies of a series of metal-dependent proteins and the characterization
of the metal-binding sites. In particular, we focus on NMR techniques for studying metal binding to proteins such as chemical
shift mapping, paramagnetic NMR and changes in backbone dynamics upon metal binding.
Received 12 October 2006; received after revision 30 November 2006; accepted 5 February 2007 |
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Keywords: | NMR chemical shift mapping backbone dynamics paramagnetic NMR calmodulin zinc finger plastocyanin prion protein |
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