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. 2015 Jul 21;91(7):321–350. doi: 10.2183/pjab.91.321

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© 2015 The Japan Academy

This is an open access article distributed under the terms of the Creative Commons Attribution License, which permits unrestricted use, distribution, and reproduction in any medium, provided the original work is properly cited.

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Figure 6. — Location of ATPase site of myosin and its relation to the actin-binding site as revealed by electron microscopy of negatively stained specimens by assuming the helical symmetry of specimens.⁵⁵⁾ A. The end-on view of the transparent model of actin-tropomyosin-myosin S1-ADP-Vi and avidin. A protrusion on the outer surface of myosin S1 corresponds to avidin. B. The end-on view of actin-tropomyosin-myosin S1 without avidin. C. The schematic illustration of A. D. The discontinuous column-like structures, interpreted as a candidate for tropomyosin in an R-state or an “open” state (right panel of Fig. 15) observed near the grooves of actin double helix. E. The spatial relationship between the actin-binding site, the ATPase site, and reactive thiol (SH1, Cys-707) determined by the developed avidin-biotin system is shown in the left panel.^53–55) In the right panel, two myosin heads are depicted differently. One is more bent than the other. The ATP-induced changes of the angle of the bending region against the main region were shown experimentally.^64–71)