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Dynamic Light Scattering Study of Muscle F-Actin in Solution

  • Satoru Fujime
  • Shin’ichi Ishiwata
  • Tadakazu Maeda
Part of the NATO Advanced Science Institutes Series book series (NSSA, volume 59)

Abstract

G-actin is globular in shape (Fig. 1a). Its molecular weight is about 42k daltons. G-actin polymerizes into F-actin under physiological salt concentrations (Fig. 1b). Based on observations by electron microscopy, a “pearl-and-necklace” model is proposed for the ultrastructure of F-actin. F-actin is a two-stranded helical polymer. The half pitch of the helix is 35 nm and within this length, there are 13 G-actins. The total length of F-actin varies according to polymerization conditions and, roughly speaking, is longer than 1 pm. As might be supposed from its structure, F-actin is rather stiff. Electron micrographs show the images of gradually curved F-actin. Tropomyosin is a rodlike protein (Fig. lc). When tropomyosin molecules are added to the solution of F-actin, they bind to F-actin and settle in the grooves of F-actin helix forming tropomyosin strands (Fig. ld). Myosin has two heads called subfragment-1 (S-1) and binds to F-actin in the absence of ATP. Partial digestion by some kind of proteases produces heavy meromyosin (HMM) and also S-1 (Fig. le).

Keywords

Correlation Function Power Spectrum Direct Memory Access Heavy Meromyosin Flexibility Parameter 
These keywords were added by machine and not by the authors. This process is experimental and the keywords may be updated as the learning algorithm improves.

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Copyright information

© Plenum Press, New York 1983

Authors and Affiliations

  • Satoru Fujime
    • 1
  • Shin’ichi Ishiwata
    • 1
  • Tadakazu Maeda
    • 1
  1. 1.Mitsubishi-Kasei Institute of Life SciencesTokyo 194Japan

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