The power cycle for actomyosin is shown in the diagram. The binding of ATP induces a conformational change in the lever arm that advances myosin along the actin filament. The binding of a fluorescent ATP analog (mantATP) to actin (A) and to actomyosin (B) was measured in a stop flow experiment. One syringe contained the myosin or a mixture of actin and myosin and the second contained a relative high concentration of mantATP. The concentration of mantATP was varied but was always high relative to the concentration of the proteins. For myosin we have: k= 0.3, k-1= 0.087 kd=0.2 and kd=0.29 for actin-myosin k1=0.45 k-1=0.6 and kd=1.3 Are the results consistent with the scheme for the power stroke shown in the diagram? Why or why not?