The interaction between single myosin heads and actin monomers is entropy-driven with a binding constant of 10(5) to 10(6) M-1, but produces very small activation of myosin ATPase.
The simplest interacting unit of actomyosin, viz., single myosin heads (subfragment 1) with actin monomers, has been studied at physiological ionic strength, by isolating the actin molecules from each other on a solid support. The interaction is characterized by a binding constant of 10(5) to 10(6) M-1 in the temperature range 4-30degrees C. It is endothermic with a standard enthalpy of 24 +/- 10 kcal mol-1, and a standard entropy of 110 +/- 40 eu. It is thus, like many protein-protein association processes, entropy-driven. Despite the high affinity of the association, which is comparable in its binding constant to that of subfragment 1 with F-actin, there is only very small activation of myosin ATPase. The ionic-strength dependence of the interaction shows unusual features. Binding of the proteins of the relaxing system to the monomeric actin was also examined: troponin binds both in the presence and absence of calcium ions, but neither tropomyosin nor the tropomyosin-troponin complex was found to bind significantly. Monomeric actin has also been examined as a function of ionic strength by spectroscopic methods; it appears that conformational differences between the G and the F state are the consequence of polymerization, and not of the change in ionic strength required to being the conversion about.
Chantler et al. (Tue,) conducted a other in Actomyosin interaction (in vitro). Actin monomers on a solid support was evaluated on Binding constant and thermodynamic properties. The interaction between single myosin heads and actin monomers is entropy-driven with a binding constant of 10(5) to 10(6) M-1, but produces very small activation of myosin ATPase.
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