Tropomyosin View Full Text


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Chapter Info

DATE

1985

AUTHORS

Michael R. Payne , Suzanne E. Rudnick

ABSTRACT

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. More... »

PAGES

141-184

References to SciGraph publications

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  • Book

    TITLE

    Cell and Muscle Motility

    ISBN

    978-1-4757-4725-6
    978-1-4757-4723-2

    Identifiers

    URI

    http://scigraph.springernature.com/pub.10.1007/978-1-4757-4723-2_6

    DOI

    http://dx.doi.org/10.1007/978-1-4757-4723-2_6

    DIMENSIONS

    https://app.dimensions.ai/details/publication/pub.1001226873


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