ATP synthase is a membrane-bound biological nanomotor, primarily known for converting ADP and inorganic phosphate to ATP. This enzyme is powered by an electrochemical gradient, established by protons distributed unevenly across the membrane. The protons flow down their electrochemical gradient and activate the two functional domains of ATP synthase: the F0-subcomplex and the F1-subcomplex. F0 is a transmembrane component with subunits that interact directly with the protons. First, the stator-subunit enables protons to enter through its channels and attach to the binding site on another subunit called the rotor. The binding of the incoming protons causes the rotor to spin. When protons complete a 360-degree full rotation, they dissociate from the rotor and exit the membrane through another stator-channel. These dynamic movements within ATP synthase are stabilized by a peripheral stalk that establishes a rigid connection between the F0 and the F1 subcomplexes.