Multiscale dynamic modeling of processive motor proteins

This paper examines dynamic behavior of a single scale biological system, nanoscale processive motor proteins, which has multiscale features because of interactions with surrounding environment. A new multiscale mechanical modeling approach has been introduced that addresses these interactions, including contact and impact with substrate and fluidic viscosity, during motor proteins processivity. The idea leads to retaining mass properties which are critical to the treatment of contact and impact required for motor protein processivity. In addition, the model supports the intriguing possibility that the effective viscous friction forces are quite small. In order to accomplish this, minimal form of the first and the second order models using embedded constraints are developed. A comparison between a widely-accepted overdamped and the proposed underdamped dynamic behavior is presented. The resulting motion predicted by the spatial model of motor proteins are obtained using a simplified model of Myosin V.