Abstract
Ideally, direct NMR spectroscopic studies of the structure and dynamics of a metal binding site would utilize the ion that is naturally bound to the protein. For calcium-binding proteins, the NMR active isotope 43Ca is a quadrupolar (I = 7/2) nucleus that produces broad peaks when bound to a protein (1–4) Although much useful information can be gleaned from studies of this nucleus (3,4), it is impossible to resolve the signals for individual calcium-binding sites in a protein with multiple-binding sites. However, isomorphous replacement of the calcium ion with an ion with more favorable NMR properties often allows the resolution of NMR signals for individual sites and provides valuable insight into the coordination of the ion within the binding site from the observed shifts. 113Cd, and to a lesser extent, 207Pb, are two such I = 1/2 metal nuclei that have been successfully used to characterize the Ca2+-binding properties of a variety of metalloproteins (5–8)
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Clarke, T.E., Vogel, H.J. (2002). Cadmium-113 and Lead-207 NMR Spectroscopic Studies of Calcium-Binding Proteins. In: Vogel, H.J. (eds) Calcium-Binding Protein Protocols: Volume 2: Methods and Techniques. Methods in Molecular Biology™, vol 173. Springer, Totowa, NJ. https://doi.org/10.1385/1-59259-184-1:205
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DOI: https://doi.org/10.1385/1-59259-184-1:205
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