Kinesins are biomolecular motors which move on cylindrical nano-tubes called microtubules  . A normal microtubule consists of more than one protofilament on which the equispaced motor binding sites form a periodic array. The collective movement of the kinesins on a microtubule is, therefore, analogous to vehicular traffic on multi-lane highways where each protofilament is the analogue of a single lane. We extend a recent model of the traffic of single-headed kinesin KIF1A [{\it Phys. Rev. E {\bf 75}, 041905 (2007)}] by incorporating processes which correspond to shifting of the motor proteins from one protofilament to another. On the basis of analytical treatment of our model, we predict the effects of lane changing on the flux of the KIF1A motors . Our quantitative predictions can be tested, in principle, by carrying out {\it in-vitro} experiments with fluorescently labelled KIF1A molecules.
KIF1A kinesins are single-headed motor proteins which move on cylindrical nano-tubes called microtubules (MT) . A normal MT consists of 13 protofilaments on which the equispaced motor binding sites form a periodic array. The collective movement of the kinesins on a MT is, therefore, analogous to vehicular traffic on multi-lane highways where each protofilament is the analogue of a single lane. Does lane-changing increase or decrease the motor flux per lane? We address this fundamental question here by appropriately extending a recent model [{\it Phys. Rev. E {\bf 75}, 041905 (2007)}] . By carrying out analytical calculations and computer simulations of this extended model, we predict that the flux per lane can increase or decrease with the increasing rate of lane changing , depending on the concentrations of motors and the rate of hydrolysis of ATP, the ``fuel'' molecules. Our predictions can be tested, in principle, by carrying out {\it in-vitro} experiments with fluorescently labelled KIF1A molecules.
R
Kinesins are biomolecular motors
KIF1A kinesins are single-headed motor proteins
A
(MT)
R
microtubule consists of more than one protofilament
MT consists of 13 protofilaments
R
microtubule
MT
R
We extend
Does lane-changing increase or decrease the motor flux per lane? We address this fundamental question here by appropriately extending
D
of the traffic of single-headed kinesin KIF1A
R
by incorporating processes which correspond to shifting of the motor proteins from one protofilament to another. On the basis of analytical treatment of our
. By carrying out analytical calculations and computer simulations of this extended
R
the effects
that the flux per lane can increase or decrease with the increasing rate
R
on the flux of the KIF1A motors . Our quantitative
, depending on the concentrations of motors and the rate of hydrolysis of ATP, the ``fuel'' molecules. Our