The origin of biological motion can be traced back to the function of
molecular motor proteins. Cytoplasmic dynein and kinesin transport org
anelles within our cells moving along a polymeric filament, the microt
ubule. The motion of the myosin molecules along the actin filaments is
responsible for the contraction of our muscles. Recent experiments ha
ve been able to reveal some important features of the motion of indivi
dual motor proteins, and a new statistical physical description - ofte
n referred to as ''thermal ratchets'' - has been developed for the des
cription of motion of these molecules. In this approach, the motors ar
e considered as Brownian particles moving along one-dimensional period
ic structures due to the effect of nonequilibrium fluctuations. Assumi
ng specific types of interaction between the particles the models can
be made more realistic. We have been able to give analytic solutions f
or our model of kinesin with elastically coupled Brownian heads and fo
r the motion of the myosin filament where the motors are connected thr
ough a rigid backbone. Our theoretical predictions are in a very good
agreement with the various experimental results. In addition, we have
considered the effects arising as a result of interaction among a larg
e number of molecular motors, leading to a number of novel cooperative
transport phenomena. (C) 1998 Elsevier Science B.V. All rights reserv
ed.