Linear Arrangement of Motor Protein on a Mechanically Deposited Fluoropolymer Thin Film.

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  • Suzuki Hitoshi
    Kansai Advanced Research Center, Communications Research Laboratory, 588–2 Iwaoka, Nishi–ku, Kobe 651–24, Japan
  • Oiwa Kazuhiro
    Kansai Advanced Research Center, Communications Research Laboratory, 588–2 Iwaoka, Nishi–ku, Kobe 651–24, Japan
  • Yamada Akira
    Kansai Advanced Research Center, Communications Research Laboratory, 588–2 Iwaoka, Nishi–ku, Kobe 651–24, Japan
  • Sakakibara Hitoshi
    Kansai Advanced Research Center, Communications Research Laboratory, 588–2 Iwaoka, Nishi–ku, Kobe 651–24, Japan
  • Nakayama Haruto
    Kansai Advanced Research Center, Communications Research Laboratory, 588–2 Iwaoka, Nishi–ku, Kobe 651–24, Japan
  • Mashiko Shinro
    Kansai Advanced Research Center, Communications Research Laboratory, 588–2 Iwaoka, Nishi–ku, Kobe 651–24, Japan

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Abstract

Motor protein molecules such as heavy meromyosin (HMM), one of the major components of skeletal muscle, were arranged linearly on a mechanically deposited fluoropolymer thin film substrate in order to regulate the direction of movement generated by the motor protein. The fluoropolymer film consisted of many linear parallel ridges whose heights and widths were 10 to 20 nm and 10 to 100 nm, respectively. The fluoropolymer ridges adsorbed HMM molecules that were applied onto the film. Actin filaments labeled with rhodamine-phalloidin were observed under a fluorescence microscope moving linearly on the HMM-coated ridges. The observation indicates that HMM molecules were aligned on the fluoropolymer ridges while retaining their function. The velocity of actin movement was measured in this system.

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