The observation of the actin-myosin sliding motion in in vitro motility assay system has contributed to the clarification of the driving force of motor proteins. Those studies have suggested that molecular friction in addition to hydrodynamical friction plays an important role in the sliding motion. However, it has not yet been discussed how the molecular friction takes part in the sliding motion due to a few motors or a single motor protein. This study, at first, has experimentally estimated the molecular friction in a Characean motility assay system using chemically modified Chara myosins. Next, we have constructed a Langevin equation for the sliding motion on the basis of the molecular level picture proposed by Tawada and Sekimoto. It has been found from the model that the molecular friction affects the sliding motion even when a small number of myosins interact with the actin filament. Last, we have discussed the molecular friction due to a small number of motor proteins quantitatively.
|ジャーナル||Journal of the Physical Society of Japan|
|出版ステータス||Published - 1999 3月|
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