Fumiko Takagi

Macoto Kikuchi3
Tsuyoshi Hondou1
Ken Sekimoto1
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We investigated the structural relaxation of myosin motor domain from the pre-power stroke state to the near-rigor state using molecular dynamics simulation of a coarse-grained protein model. To describe the structural change, we propose a " dual G¯ o-model, " a variant of the G¯ o-like model that has two reference structures. The nucleotide dissociation(More)
Molecular motors such as kinesin regulate affinity to a rail protein during the ATP hydrolysis cycle. The regulation mechanism, however, is yet to be determined. To understand this mechanism, we investigated the structural fluctuations of the motor head of the single-headed kinesin called KIF1A in different nucleotide states using molecular dynamics(More)
How molecular motors like Kinesin regulates the affinity to the rail protein in the process of ATP hydrolysis (ATP → ADP·Pi → ADP + Pi) remains to be uncovered. To understand the regulation mechanism, we investigate the structural fluctuation of KIF1A in different nucleotide states that are realized in the ATP hydrolysis process by molecular dynamics(More)
When a small dynamical system that is initially in contact with a heat bath is detached from this heat bath and then caused to undergo a quasi-static adiabatic process, the resulting statistical distribution of the system's energy differs from that of an equilibrium ensemble. Subsequent contact of the system with another heat bath is inevitably(More)
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