NMR Approaches to the Characterization of the Interaction of Metal Ions with Proteins

  • Thomas C. Williams
  • Judith G. Shelling
  • Brian D. Sykes
Part of the NATO ASI Series book series (NSSA, volume 107)


A general interest of our laboratory is the structure, function and biological role of calcium-binding proteins. Calcium ions are very important in the regulation of a wide variety of biological processes. One such process is contractility. The contraction of mammalian skeletal and cardiac muscle is regulated by the level of calcium ions present and the interaction of calcium ions with several proteins. This occurs in the following fashion. The nerve impulse releases calcium ions from the sarcoplasmic reticulum membrane which surrounds the muscle fibers. The increased intracellular calcium level then results in the interaction of calcium with the calcium-specific sites of the thin filament protein, troponin-C. This turns on the muscle. The calcium then migrates to parvalbumin, a soluble protein whose affinity for calcium ions is very high. Since this turns the contraction off, parvalbumin is referred to as a soluble relaxing factor. Eventually, the calcium is pumped back into the sarcoplasmic reticulum by the SR Ca+2 ATPase where it is bound in high concentration to the protein calsequestrin. This process thus involves the interaction of calcium with at least five proteins or membrane channels with varying affinities for calcium.


Stability Constant Fractional Change Sarcoplasmic Reticulum Membrane Spectroscopic Change Doublet Resonance 
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Copyright information

© Plenum Press, New York 1986

Authors and Affiliations

  • Thomas C. Williams
    • 1
  • Judith G. Shelling
    • 1
  • Brian D. Sykes
    • 1
  1. 1.MRC Group in Protein Structure and Function and the Department of BiochemistryUniversity of AlbertaEdmontonCanada

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