Motion of Molecular Motor Ratcheted by Internal Uctuations and Protein Friction

We investigate theoretically a novel mechanism of transducing chemical energy into a directed force. A hypothetical motor protein is considered such that conformational changes induced by nucleotide binding and/or hydrolysis lead to asymmetric internal velocity uctu-ations. We demonstrate that these uctuations result in unidirectional motion if rectiied by protein friction. The motor protein force-velocity relationship and other characteristics are computed based on analogy with known molecular motors.