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Classical Article
. 2004 Jun;123(6):631-41.
doi: 10.1085/jgp.200409091.

The early history of the biochemistry of muscle contraction

Andrew G Szent-Györgyi
Classical Article

The early history of the biochemistry of muscle contraction

Andrew G Szent-Györgyi. J Gen Physiol. 2004 Jun.
No abstract available

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Figures

F<sc>igure</sc> 1.
Figure 1.
Contraction of actomyosin threads (“myosin B”) on addition of ATP. Shown are the same thread A before and B after addition of boiled muscle juice (a source of ATP) (Szent-Györgyi, 1942a).
F<sc>igure</sc> 2.
Figure 2.
The myosin molecule (adapted from Alberts et al., 2002).
F<sc>igure</sc> 3.
Figure 3.
Cross-striated muscle is organized in sarcomeres that extend from one Z-line to the next. The distance between Z-lines is 2–3 μm. The thin filaments contain actin and the thick filaments contain myosin. The thick filaments have bipolar symmetry with a central bare zone in which there are no cross-bridges. The actin fiber symmetry reverses in the Z-line. The area not penetrated by the thin filaments is variable, and is known as the H-zone.
F<sc>igure</sc> 4.
Figure 4.
2-μm long myosin containing thick filaments with cross-bridges and 1-μm long actin containing thin filaments are shown. As the sarcomere shortens, the myosin cross-bridges react with actin and propel the thin filaments toward the center of the sarcomere. Both filament types remain at constant lengths during contraction. The sliding of the filaments explains the constancy of the A-band and the changes of the I-band and the H-zone.
F<sc>igure</sc> 5.
Figure 5.
The cross-bridge cycle. Note that ATP hydrolysis takes place in the detached state. In the actin-bound state contraction is associated with the dissociation of the hydrolysis products; recovery of the resting state structure follows dissociation of myosin from actin by ATP (see Taylor, 2001).
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References

    1. Alberts, B., A. Johnson, J. Lewis, M. Raff, K. Roberts and P. Walter. 2002. Molecular Biology of the Cell. Fourth edition. Garland Publishing. 950 pp.
    1. Asakura, S. 1961. F-actin adenosine triphosphatase activated under sonic vibration. Biochim. Biophys. Acta. 52:65–75. - PubMed
    1. Asakura, S., M. Taniguchi, and F. Oosawa. 1963. Mechano-chemical behaviour of F-actin. J. Mol. Biol. 7:55–69.
    1. Astbury, W.T. 1947. Croonian lecture. On the structure of biological fibers and the problem of muscle. Proc. R. Soc. Lond. B. Biol. Sci. 134:303–328. - PubMed
    1. Bagshaw, C.R. and D.R Trentham. 1974. The characterization of myosin-product complexes and of product-release steps during the magnesium ion-dependent adenosine triphosphatase reaction. Biochem. J. 141:331–349. - PMC - PubMed

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