SEM Imaging of Single Heavy Meromyosin Molecules on Hydrophilic Silicon Surface

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Abstract

The fine structure of skeletal muscle heavy meromyosin (HMM) with two heads connected to a thin tail was clearly imaged with a high-resolution scanning electron microscope (SEM) by negative staining on a hydrophilic silicon surface. The single molecular image of HMM was analyzed. A structural change in the HMM head on binding of adenosine triphosphate (ATP) was detected. The HMM molecules with head(s) bent at 6-8 nm from the head-tail junction directed toward the end of the tail were found frequently in the presence of ATP. The estimated value for the bending angle was about 20° on average.

Journal

  • bioimages

    bioimages 4 (2), 73-78, 1996

    Bioimaging Society

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Details

  • CRID
    1390007846293106688
  • NII Article ID
    10002037729
  • NII Book ID
    AA11084187
  • DOI
    10.11169/bioimages.4.73
  • ISSN
    09192719
  • Text Lang
    en
  • Data Source
    • JaLC
    • CiNii Articles
  • Abstract License Flag
    Disallowed

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