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