The stochastic driving force that is exerted by a single molecular motor (e
.g., a kinesin, or myosin protein molecule) moving on a periodic molecular
track (such;Is a microtubule, actin filament, etc.) is discussed from a gen
eral theoretical viewpoint open to experimental test. An elementary but fun
damental "barometric" relation for the driving force is introduced that (i)
applies to a range of kinetic and stochastic models of catalytic motor pro
teins, (ii) is consistent with more elaborate expressions that entail furth
er; explicit assumptions for the representation of externally applied loads
and, (iii) sufficiently close to thermal equilibrium, satisfies an Einstei
n;type relation in terms of the observable velocity and dispersion, or diff
usion coefficient, of the (load-free) motor protein on its track. Even in t
he simplest two-state kinetic models, the predicted velocity-vs.-load plots
(that are observationally accessible) exhibit a variety of contrasting sha
pes that can include nonmonotonic behavior. Previously suggested bounds on
the driving force are shown to be inapplicable in general by considering di
screte jump models which feature waiting-time distributions. Some compariso
ns with experiment are sketched. (C) 1999 Elsevier Science B.V. All rights
reserved.