Abstract
Opening the Arg-Glu salt bridge in myosin, which presumably succeeds the myosin-catalyzed hydrolysis of adenosine triphosphate, was modeled computationally on the basis of the structures corresponding to the enzyme-substrate and enzyme-product complexes found in the quantum mechanics-molecular mechanics simulations. According to the calculations of the potential of mean force, opening the bridge is considerably facilitated upon termination of the chemical reaction, but does not promote egress of inorganic phosphate by the back-door mechanism.
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