Publications by authors named "Hidetaka Tobita"

When the size of a polymerization locus is smaller than a few hundred nanometers, such as in miniemulsion polymerization, each locus may contain no more than one key-component molecule, and the concentration may become much larger than the corresponding bulk polymerization, leading to a significantly different rate of polymerization. By focusing attention on the component having the lowest concentration within the species involved in the polymerization rate expression, a simple formula can predict the particle diameter below which the polymerization rate changes significantly from the bulk polymerization. The key component in the conventional free-radical polymerization is the active radical and the polymerization rate becomes larger than the corresponding bulk polymerization when the particle size is smaller than the predicted diameter.

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It is essential to know the detailed structure of the thin filament to understand the regulation mechanism of striated muscle contraction. Fluorescence resonance energy transfer (FRET) was used to construct an atomic model of the actin-tropomyosin (Tm)-troponin (Tn) core domain complex. We generated single-cysteine mutants in the 167-195 region of Tm and in TnC, TnI, and the β-TnT 25-kDa fragment, and each was attached with an energy donor probe.

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Fluorescence resonance energy transfer (FRET) was used to construct an atomic model of the actin-tropomyosin (Tm) complex on a reconstituted thin filament. We generated five single-cysteine mutants in the 146-174 region of rabbit skeletal muscle α-Tm. An energy donor probe was attached to a single-cysteine Tm residue, while an energy acceptor probe was located in actin Gln41, actin Cys374, or the actin nucleotide binding site.

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