NMR Studies of Calcium and Magnesium in Biological Systems

  • Sture Forsén
  • Thomas Andersson
  • Torbjörn Drakenberg
  • Eva Thulin
  • Tadeusz Wieloch


The NMR spectroscopic technique has developed to a state where studies of 25Mg2+ and 43Ca2+ in the millimolar concentration range are feasible. This development has in turn opened new possibilities in the study of calcium and magnesium binding proteins. In the article three proteins are chosen as examples: troponin C, calmodulin and phospholipase A2. The type of information that can be obtained is: (i) binding constants in the range 1 to 104 M-1; (ii) the competition of different cations for the calcium or magnesium binding site; (iii) the effects of other ligands (drugs etc.) on the protein; (iv) pKa values for the groups involved in the Mg2+ or Ca2+ binding; (v) the dynamics of the binding site (correlation time). 43Ca NMR studies of proteins with calcium binding constants exceeding 105 M-1 are generally not possible. In such situations the use of 113Cd or 111Cd NMR is often a powerful alternative. The Cd isotopes have both spin I = 1/2 and NMR signals from the individual ions when bound to the protein may be obtained. The chemical shift of cadmium is very sensitive to the nature of the ligands. Additional information may be obtained from competition experiments, chemical modifications, pH variations etc.


Line Width Binding Constant Calcium Binding Protein 43Ca Signal Magnesium Binding 
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Copyright information

© Plenum Press, New York 1981

Authors and Affiliations

  • Sture Forsén
    • 1
  • Thomas Andersson
    • 1
  • Torbjörn Drakenberg
    • 1
  • Eva Thulin
    • 1
  • Tadeusz Wieloch
    • 1
  1. 1.Physical Chemistry 2 and Physical Chemistry 3 Chemical CentreLund UniversityLund 7Sweden

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