Reito Wada

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Urea and trimethylamine N-oxide (TMAO) are known to denature and stabilize proteins, respectively. We examined two actin-binding processes, namely, end-to-end annealing of actin filaments (F-form) and the polymerization of actin monomers (G-form) into filaments, in the presence of urea, TMAO, and both solutes. Fluorescence microscopy for direct observation(More)
The motility of actin filaments interacting with heavy meromyosin molecules was directly observed on indium tin oxide-coated glass (ITO-glass), over which a surface current flowed. Because the increase in surface current applied to ITO-glass increases the temperature, we focused on the temperature-dependence of the sliding velocity and the effect of the(More)
ATP-driven motor proteins, which function in cell motility and organelle transport, have potential applications as bio-inspired micro-devices; however, their control remains unsatisfactory. Here, we show rapid-velocity control of actin filaments interacting with myosin motors using voltage applied to Pt electrodes in an in vitro motility system, by which(More)
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