Evidence for Structural Changes in Crossbridges During Force Generation

  • B. Brenner
  • L. C. Yu
Part of the Advances in Experimental Medicine and Biology book series (AEMB, volume 332)


During muscle contraction, it is generally thought that myosin heads undergo large scale conformational changes, such as an oar-like rotation between 90° and 45° while attached to actin. However, evidence for conformational changes of the attached crossbridges associated with force generation has been ambiguous. In this study, we compared the conformations of attached crossbridges in (i) the pre-force generating state, (ii) force generating state, (ii) rigor state.

High resolution equatorial X-ray diffraction patterns have been obtained from single chemically skinned rabbit psoas fibers under relaxed, fully Ca2+-activated and rigor conditions. The experimental condition was chosen (ionic strength = 50 mM and temperature = 5°C) such that there are large fractions (80–100%) of crossbridges attached in all the three states, and the attached crossbridges in the relaxed muscle represent the pre-force generating state.

Upon activation, changes in the two innermost intensities I10 and I11 did not follow the familiar reciprocal changes. Instead, there was almost no change in I11 while I10 decreased by 30%. Similarly, greater changes were found in I10 as the fiber goes into rigor from the activated state. Changes were also found in the higher order reflections suggesting that the structure of the force generating crossbridges is not a mixture of those found in the weakly bound and rigor crossbridges. Therefore, our data provides evidence that the average conformation of the force generating crossbridges is different from the weakly attached and from rigor crossbridges.


Thin Filament Myosin Head Thick Filament Rigor Condition Cross Bridge 
These keywords were added by machine and not by the authors. This process is experimental and the keywords may be updated as the learning algorithm improves.


Unable to display preview. Download preview PDF.

Unable to display preview. Download preview PDF.


  1. 1.
    Pringle, J.W.S. Prog. Biophys. Biophys. Chem. 17, 1–60 (1967).CrossRefGoogle Scholar
  2. 2.
    Huxley, H.E. Science 164, 1356–1366 (1969).PubMedCrossRefGoogle Scholar
  3. 3.
    Huxley, A.F. & Simmons, R.M. Nature 233, 533–538 (1971).PubMedCrossRefGoogle Scholar
  4. 4.
    Reedy, M.K., Holmes, K.C. & Tregear, R.T. Nature 207, 1276–1280 (1965).PubMedCrossRefGoogle Scholar
  5. 5.
    Brenner, B. Biophys. J. 41, 99–102 (1983).PubMedCrossRefGoogle Scholar
  6. 6.
    Yu, L.C. & Brenner, B. Biophys. J. 55, 441–453 (1989).PubMedCrossRefGoogle Scholar
  7. 7.
    Brenner, B., Schoenberg, M., Chalovich, J.M., Greene, L.E. & Eisenberg, E. Proc. Natl. Acad. Sci. USA 79, 7288–7291 (1982).PubMedCrossRefGoogle Scholar
  8. 8.
    Brenner, B., Yu, L.C. & Podolsky, R.J. Biophys. J. 46, 299–306 (1984).PubMedCrossRefGoogle Scholar
  9. 9.
    Brenner, B., Yu, L.C. & Chalovich, J.M. Proc. Natl. Acad. Sci. USA 88, 5739–5743 (1991).PubMedCrossRefGoogle Scholar
  10. 10.
    Kraft, Th., Chalovich, J.M., Yu, L.C. & Brenner, B. Biophys. J. 59, 375a (1991).CrossRefGoogle Scholar
  11. 11.
    Chalovich, J.M., Chock, P.B. & Eisenberg, E. J. Biol. Chem. 256, 575–578 (1981).PubMedGoogle Scholar
  12. 12.
    Chalovich, J.M. & Eisenberg, E. J. Biol. Chem 257, 2431–2437 (1982).Google Scholar
  13. 13.
    Brenner, B., Chalovich, J.M., Greene, L.E., Eisenberg, E. & Schoenberg, M. Biophys. J. 50, 685–691 (1986).PubMedCrossRefGoogle Scholar
  14. 14.
    Brenner, B., Yu, L.C, Greene, L.E., Eisenberg, E. & Schoenberg, M. Biophys. J. 50, 1101–1108 (1986).PubMedCrossRefGoogle Scholar
  15. 15.
    Schoenberg, M. Biophys. J. 54, 135 (1988).PubMedCrossRefGoogle Scholar
  16. 16.
    Lovell, S.J. & Harrington, W.F. J. Mol. Biol. 149, 659–674 (1981).PubMedCrossRefGoogle Scholar
  17. 17.
    Cooke, R. & Franks, K. Biochemistry 19, 2265–2269 (1980).PubMedCrossRefGoogle Scholar
  18. 18.
    Lymn, R.W. Biophys. J. 21, 93–98 (1978).PubMedCrossRefGoogle Scholar
  19. 19.
    Yu, L C. Biophys. J. 55, 433–440 (1989).PubMedCrossRefGoogle Scholar
  20. 20.
    Brenner, B. & Yu, L.C. J. Physiol. (Lond.) 441, 703–718 (1991).Google Scholar
  21. 21.
    Yu, L C., Steven, A.C., Naylor, G.R.S., Gamble, R.C. & Podolsky, R.J. Biophys. J. 47, 311–321 (1985).PubMedCrossRefGoogle Scholar
  22. 22.
    Harford, J.J. & Squire, J.M. in Molecular mechanisms in musclular contraction (ed Squire, J.M.) 287–320 (Macmillan Press, London, 1989).Google Scholar

Copyright information

© Springer Science+Business Media New York 1993

Authors and Affiliations

  • B. Brenner
    • 1
  • L. C. Yu
    • 2
  1. 1.Department of General PhysiologyUniversity of UlmGermany
  2. 2.National Institutes of HealthBethesdaUSA

Personalised recommendations