The functional nature of calcium binding units in calmodulin, troponin C and parvalbumin.

Examination of the interaction of major tranquilizers with calmodulin results in the generalization that the functional nature of calcium binding helix-loop-helix regions found in several calcium binding proteins including calmodulin, troponin C and parvalbumin is dependent upon the topography of the hydrophobic and hydrophilic regions on the amphiphilic N-terminal alpha-helix of the helix-loop-helix conformation formed by the binding of the calcium cation to these proteins. The relation of the topography of this amphiphilic alpha-helix to drug binding is delineated at the molecular level and the results obtained are used to describe the interaction of beta-endorphin, dynorphin, alpha-MSH and other peptides with calmodulin. The utility of this hypothesis is further demonstrated by the description of a possible interaction between troponin C, troponin I and troponin T of the troponin complex in skeletal muscle.