摘要
We describe a very coarse-grained molecular model for the simulation of myosin V on an actin filament. The molecular representation is hierarchical with the finest level representing secondary structure elements (end-points) which are grouped into domains which are then grouped into molecules. Each level moves with a Brownian-like motion both in translation and rotation. Molecular integrity is maintained by steric exclusion and inter-domain restraints. A molecular description is developed for a myosin dimer on a actin filament with binding interactions also specified between domains to simulate both loose and tight binding. The stability of the model was tested in the pre- and post-power-stroke conformations with simulations in both states being used to test the preferred binding site of the myosin on the filament. The effects of the myosin twofold symmetry and the restriction of an attached cargo were also tested. These results provide the basis for the development of a dynamic model of processive motion.
- 出版日期2010-9
- 单位河北医科大学