Structural and Functional Diversity
  • Michael R. Payne
  • Suzanne E. Rudnick


Tropomyosin (TM) is present throughout evolution both as a major contractile protein in muscle and as an important component of the microfilaments maintaining the cellular cytoarchitecture. Tropomyosin was first isolated by Bailey (1948) and was soon shown to give a complex low-angle X-ray diffraction pattern that is now recognized as an α-helical conformation (Astbury et al, 1948). Crick (1953) interpreted the TM diffraction pattern as two a-helical subunits winding around each other to form a coiled-coil conformation. Optical rotatory dispersion analysis showed an almost fully a-helical molecule, confirming this structure prediction (Szent-Györgyi and Cohen, 1957). Tropomyosin is present in rabbit skeletal muscle as approximately 7% of the total structural protein and is a key component in the actin-linked calcium regulatory mechanism that controls muscle contraction. In vertebrate striated muscle, the thin filament consists of actin, TM, and the three troponin (TN) proteins: TN-T, TN-I, and TN-C. Rabbit skeletal muscle TM migrates on sodium dodecylsulfate (SDS) electrophoretic gels as two polypeptides, a and ß, between 34,000 and 36,000 daltons. Although both a and ß subunits contain the same number of amino acids, ß-TM is slightly more basic and migrates more slowly on SDS gels. Under physiological conditions, the rabbit skeletal TM subunits form a dimer of —68,000 daltons. Each TM molecule has a length of ~400 Å and can interact with seven actin monomers.


Stress Fiber Thin Filament Actin Monomer Rabbit Skeletal Muscle Nonmuscle Cell 
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Copyright information

© Springer Science+Business Media New York 1985

Authors and Affiliations

  • Michael R. Payne
    • 1
  • Suzanne E. Rudnick
    • 2
  1. 1.Department of AnatomyNew York Medical CollegeValhallaUSA
  2. 2.Department of ChemistryManhattan CollegeRiverdaleUSA

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