Motor proteins constitute an essential part of the cellular machinery. They have been the subject of intensive studies in the past two decades. Yet, when several motors simultaneously carry a single cargo, the effect of motor-motor coupling, such as mutual stalling and jamming, remains unclear. We commence by constructing a general model for single motor motion, which is a product of a derived load-dependent expression and a phenomenological motor specific function. Forming the latter according to recent single molecule measurements for a given load, the model correctly predicts the motor full step-size distribution for all other measured loads. We then use our proposed model to predict transport properties of multimotor complexes, with particular attention to 1-dimensional constructs with variable flexibility, motor density, and number of motors: (i) a chain of motors connected by springs, a recently studied construction of a pair, and (ii) an array of motors all connected by identical springs to a stiff rod, which is essentially a mirror image of standard gliding motility assays. In both systems, and for any number of carrying motors, we find that, while low flexibility results in a strongly damped velocity, increased flexibility renders an almost single motor velocity. Comparing our model based simulations to recent gliding assays we find remarkable qualitative agreement. We also demonstrate consistency with other multimotor motility assays. In all cases, the characteristic spring constant, that controls the crossover behavior between high and low velocity regimes, is found to be the stalling force divided by the mean step size. We conjecture that this characteristic spring constant can serve as a tool for engineering multimotor complexes.
ASJC Scopus subject areas
- Physical and Theoretical Chemistry
- Surfaces, Coatings and Films
- Materials Chemistry