An Investigation of the Cross-bridge Cycle Using ATP Analogues and Low-angle X-ray Diffraction from Glycerinated Fibres of Insect Flight Muscle

  • K. C. Holmes
  • R. S. Goody
  • H. G. Mannherz
  • J. Barrington Leigh
  • G. Rosenbaum
Conference paper
Part of the 26. Colloquium der Gesellschaft für Biologische Chemie 10.–12. April 1975 in Mosbach/Baden book series (MOSBACH, volume 26)

Abstract

The interdigitating filament arrays of muscle contain as their major components the proteins actin and myosin. Globular actin molecules aggregate to form the “thin” filaments. Myosin molecules consist of fully α-helical tails and enzymatically active heads. The molecules spontaneously aggregate to form bipolar filaments (the “thick” filaments) with the heads protruding to form the “cross-bridges”. Two heads may constitute one cross-bridge. The interaction between actin and myosin is mediated by the cross-bridges. By limited proteolytic digestion the enzymatically active fragments of myosin S1 (single heads) and HMM (two heads with a length of tail) may be prepared. The heads (S1) are joined to the tails by a more flexible part of the tail known as the S2 region. (For details and references see Huxley, this volume.)

Keywords

Hydrolysis Quartz Glycerol Catalysis Hexagonal 

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References

  1. Bagshaw, C.R., Eccleston, J.F., Eckstein, F., Goody, R.S., Gutfreund, H., Trentham, D.R.: Biochem. J. 141 , 351–364 (1974).PubMedGoogle Scholar
  2. Bagshaw, C.R., Trentham, D.R.: Biochem. J. 133, 331–349 (1973).Google Scholar
  3. Barringtonteigh, J., Holmes, K.C., Mannherz, H.G., Rosenbaum, G., Eckstein, F., Goody, R.: Cold Spring Harbor Symp. Quant. Biol. 37, 443–447 (1972).Google Scholar
  4. Caspar, D.L.D., Holmes, K.C.: J. Mol. Biol. 46, 99–133 (1969).PubMedCrossRefGoogle Scholar
  5. Goody, R.S., Eckstein, F.: J. Amer. Chem. Soc. 93, 6252 (1971).CrossRefGoogle Scholar
  6. Goody, R.S., Holmes, K.C., Mannherz, H.G., Barrington Leigh, J., Rosenbaum, G.: Biophys. J., in press (1975).Google Scholar
  7. Huxley, A.F., Simmons, R.M.: Nature 233, 533–538 (1971).PubMedCrossRefGoogle Scholar
  8. Huxley, H.E.: Science 164, 1356–1366 (1969).PubMedCrossRefGoogle Scholar
  9. Jewell, B.R., Pringle, J.W.S., Rüegg, J.C.: J. Physiol. 173, 6–8 (1964) .Google Scholar
  10. Kuhn, H.J.: Sep. Experientia 29, 1086–1088 (1973).CrossRefGoogle Scholar
  11. Lienhard, G.E., Secemski, I.I.: J. Biol. Chem. 248, 1121–1122 (1973).PubMedGoogle Scholar
  12. Lymn, R.W., Taylor, E.W.: Biochemistry 9, 2975–2983 (1970).PubMedCrossRefGoogle Scholar
  13. Lymn, R.W., Taylor, E.W.: Biochemistry 10, 4617–4624 (1971).PubMedCrossRefGoogle Scholar
  14. Mannherz, H.G., Barrington Leigh, J., Holmes, K.C., Rosenbaum, G. : Nature New Biology (Lond.) 241, 226–229 (1973).Google Scholar
  15. Marston, S.B., Tregear, R.T.: Nature New Biology (Lond.) 235, 23–24 (1972).Google Scholar
  16. Miller, A., Tregear, R.T.: Nature (Lond.) 226, 1060–1061 (1970).CrossRefGoogle Scholar
  17. Miller, A., Tregear, R.T.: J. Mol. Biol. 70, 85–104 (1972).PubMedCrossRefGoogle Scholar
  18. Reedy, M.K.: J. Mol. Biol. 31, 155–176 (1968).PubMedCrossRefGoogle Scholar
  19. Reedy, M.K., Holmes, K.C., Tregear, R.T.: Nature (Lond.) 207, 1276–1280 (1965) .CrossRefGoogle Scholar
  20. Squire, J.M.: J. Mol. Biol. 72, 125–138 (1972).PubMedCrossRefGoogle Scholar
  21. Szent-Györgyi, A.: Biol. Bull. 96, 140 (1949).PubMedCrossRefGoogle Scholar
  22. Taylor, E.W., Lymn, R.W., Moll, G. : Biochemistry 9, 2284–2991 (1970).Google Scholar
  23. Weber, A., Murray, J.M.: Physiol. Rev. 53, 612–673 (1973).PubMedGoogle Scholar
  24. Yount, R.G., Babcock, D., Ballantyre, W., Ojala, D.: Biochemistry 10, 2484–2489 (1971) .PubMedCrossRefGoogle Scholar

Copyright information

© Springer-Verlag Berlin · Heidelberg 1976

Authors and Affiliations

  • K. C. Holmes
  • R. S. Goody
  • H. G. Mannherz
  • J. Barrington Leigh
  • G. Rosenbaum

There are no affiliations available

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