Reaction free energy surfaces in myosin-actin-ATP systems.
If we select for consideration any reaction M1 in equilibrium M2 in the myosin-ATPase cycle, the question arises as to the relations between the rate constants for (1) M1 equilibrium M2, (2) AM1 in equilibrium AM2 (A = actin), (3) A + M1 in equilibrium AM1, and (4) A + M2 equilibrium AM2, with actin and myosin either (a) in solution or (b) in the myofilament structure. It is shown here, by means of examples, that a single so-called potential of mean force, W, and structural free energy, Am, suffice to determine the reaction free energy surfaces for all of these transitions (W for the solution case, W + Am for the structured case). In fact, Am is the same for all reactions in the myosin-ATPase cycle. Of course, though indispensable as the starting point and adequate for qualitative understanding, the reaction free energy surface does not provide (without additional theory) the actual values of the rate constants or of the corresponding basic free energy changes in the myosin states involved. These rate constants and free energies are discussed, in a preliminary way, in two other papers.
D000199:Actins / Q000378:metabolism; D000251:Adenosine Triphosphatases / Q000378:metabolism; D000255:Adenosine Triphosphate; D001665:Binding Sites; D046911:Macromolecular Substances; D009218:Myosins / Q000378:metabolism; D011485:Protein Binding; D011487:Protein Conformation; D013816:Thermodynamics
D000199:Actins; D046911:Macromolecular Substances; D000255:Adenosine Triphosphate; D000251:Adenosine Triphosphatases; D009218:Myosins