We investigate theoretically a novel mechanism of transducing chemical
energy into a directed force. A hypothetical motor protein is conside
red such that conformational changes induced by nucleotide binding and
/or hydrolysis lead to asymmetric internal velocity fluctuations. We d
emonstrate that these fluctuations result in unidirectional motion if
rectified by protein friction. The motor protein force-velocity relati
onship and other characteristics are computed based on analogy with kn
own molecular motors. (C) 1998 Elsevier Science B.V.