85 research outputs found
Mechanism of unidirectional movement of kinesin motors
Kinesin motors have been studied extensively both experimentally and
theoretically. However, the microscopic mechanism of the processive movement of
kinesin is still an open question. In this paper, we propose a hand-over-hand
model for the processivity of kinesin, which is based on chemical, mechanical,
and electrical couplings. In the model the processive movement does not need to
rely on the two heads' coordination in their ATP hydrolysis and mechanical
cycles. Rather, the ATP hydrolyses at the two heads are independent. The much
higher ATPase rate at the trailing head than the leading head makes the motor
walk processively in a natural way, with one ATP being hydrolyzed per step. The
model is consistent with the structural study of kinesin and the measured
pathway of the kinesin ATPase. Using the model the estimated driving force of ~
5.8 pN is in agreements with the experimental results (5~7.5 pN). The
prediction of the moving time in one step (~10 microseconds) is also consistent
with the measured values of 0~50 microseconds. The previous observation of
substeps within the 8-nm step is explained. The shapes of velocity-load (both
positive and negative) curves show resemblance to previous experimental
results.Comment: 22 pages, 6 figure
Model for processive movement of myosin V and myosin VI
Myosin V and myosin VI are two classes of two-headed molecular motors of the
myosin superfamily that move processively along helical actin filaments in
opposite directions. Here we present a hand-over-hand model for their
processive movements. In the model, the moving direction of a dimeric molecular
motor is automatically determined by the relative orientation between its two
heads at free state and its head's binding orientation on track filament. This
determines that myosin V moves toward the barbed end and myosin VI moves toward
the pointed end of actin. During the moving period in one step, one head
remains bound to actin for myosin V whereas two heads are detached for myosin
VI: The moving manner is determined by the length of neck domain. This
naturally explains the similar dynamic behaviors but opposite moving directions
of myosin VI and mutant myosin V (the neck of which is truncated to only
one-sixth of the native length). Because of different moving manners, myosin VI
and mutant myosin V exhibit significantly broader step-size distribution than
native myosin V. However, all three motors give the same mean step size of 36
nm (the pseudo-repeat of actin helix). Using the model we study the dynamics of
myosin V quantitatively, with theoretical results in agreement with previous
experimental ones.Comment: 18 pages, 7 figure
A model for processivity of molecular motors
We propose a two-dimensional model for a complete description of the dynamics
of molecular motors, including both the processive movement along track
filaments and the dissociation from the filaments. The theoretical results on
the distributions of the run length and dwell time at a given ATP
concentration, the dependences of mean run length, mean dwell time and mean
velocity on ATP concentration and load are in good agreement with the previous
experimental results.Comment: 10 pages, 7 figure
Ionic effect on combing of single DNA molecules and observation of their force-induced melting by fluorescence microscopy
Molecular combing is a powerful and simple method for aligning DNA molecules
onto a surface. Using this technique combined with fluorescence microscopy, we
observed that the length of lambda-DNA molecules was extended to about 1.6
times their contour length (unextended length, 16.2 micrometers) by the combing
method on hydrophobic polymethylmetacrylate (PMMA) coated surfaces. The effects
of sodium and magnesium ions and pH of the DNA solution were investigated.
Interestingly, we observed force-induced melting of single DNA molecules.Comment: 12 page
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