Theoretical Model for the Cooperative Equilibrium Binding of Myosin Subfragment 1 to the Action-Troponin-Tropomyosin Complex
Terrell L. Hill, Evan Eisenberg, Lois Greene
Proceedings of the National Academy of Sciences of the United States of America·1980
Recent experimental data on the equilibrium binding of myosin subfragment 1 (S-1) to regulated actin filaments in the presence and in the absence of Ca2+ are analyzed by using a linear Ising model. In the model, each tropomyosin-troponin unit (including seven sites on the actin filament) can be in one of two possible states, which have different intrinsic free energies and different binding constants for S-1. Bound S-1 molecules do not interact with each other. There are nearest-neighbor (pair) interactions between these units that depend on the state of each member of the pair and on the number of Ca2+ bound to one member of the pair. There are two sources of positive cooperativity in this system: the fact that seven actin sites change state together as part of a single unit; and the existence of attractive nearest-neighbor interactions between units. Parameters in the model are evaluated by fitting the data, both in the presence and in the absence of Ca2+. Several extensions of this model are discussed.