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Biophys J, February 2000, p. 541-556, Vol. 78, No. 2

*Department of Chemistry, University of New Mexico, Albuquerque,
New Mexico 87131; and
Departments of Physics and Cellular
and Molecular Biology, University of California, Berkeley, California
94720 USA,
Physical Biosciences Division, Lawrence
Berkeley National Laboratory, Berkeley, California 94720, USA
A theory of molecular motors is presented that explains
how the energy released in single chemical reactions can generate mechanical motion and force. In the simplest case the fluctuating movements of a motor enzyme are well described by a diffusion process
on a two-dimensional potential energy surface, where one dimension is a
chemical reaction coordinate and the other is the spatial displacement
of the motor. The coupling between chemistry and motion results from
the shape of the surface, and motor velocities and forces result from
diffusion currents on this surface. This microscopic description is
shown to possess an equivalent kinetic mechanism in which the rate
constants depend on externally applied forces. By using this
equivalence we explore the characteristic properties of several broad
classes of motor mechanisms and give general expressions for motor
velocity versus load force for any member of each class. We show that
in some cases simple plots of 1/velocity vs. 1/concentration can
distinguish between classes of motor mechanisms and may be used to
determine the step at which movement occurs.
Biophys J, February 2000, p. 541-556, Vol. 78, No. 2
© 2000 by the Biophysical Society 0006-3495/00/02/541/16 $2.00
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