Molecular motors are multi-subunit complexes that are indispensable for accomplishing various tasks of the living cells. One such molecular motor is the FOF1 ATP synthase that synthesizes ATP at the expense of the membrane proton gradient. Elucidating the molecular origin of the motor function is challenging despite significant advances in various experimental fields. Currently atomic simulations of whole motor complexes cannot reach to functionally relevant time scales that extend beyond the millisecond regime. Moreover, to reveal the underlying molecular origin of the function, one must model the coupled chemical and conformational events using physically and chemically meaningful multiscaling techniques. In this review, we discuss our approach to model the action of the F1 and FO molecular motors, where emphasis is laid on elucidating the molecular origin of the driving force that leads to directional rotation at the expense of ATP hydrolysis or proton gradients. We have used atomic structures of the motors and used hierarchical multiscaling techniques to generate low dimensional functional free energy surfaces of the complete mechano-chemical process. These free energy surfaces were studied further to calculate important characteristics of the motors, such as, rotational torque, temporal dynamics, occurrence of intermittent dwell states, etc. We also studied the result of mutating various parts of the motor domains and our observations correspond very well with the experimental findings. Overall, our studies have generated a cumulative understanding of the motor action, and especially highlight the crucial role of electrostatics in establishing the mechano-chemical coupling.