The physics and chemistry of the calcium-binding proteins

The structures of several calcium-binding proteins are known in considerable detail in both crystalline and solution states. The changes of structure with the binding of calcium, protons, magnesium and hydrophobic molecules are also known. It appears that some calcium-binding structures contain relays of cooperative interaction which run via helices between different parts of these proteins, for example in calmodulin. In others the effect of binding, of for instance calcium, is minimal, as in phospholipase A2. In another group the effect of binding of ions leads to cooperative further binding so that ternary or higher-order complexes are formed, as in the activation of prothrombin. The linking of cellular activities to calcium is thus dependent on several highly developed properties of particular proteins in special environments which have been selected to take advantage of the peculiarities of the calcium ion, namely its particular coordination chemistry and its speed of reaction. The link between calcium, its proteins and activity is not directly to catalysis but is primarily to mechanical properties.