Skip to main content
Proceedings of the National Academy of Sciences of the United States of America logoLink to Proceedings of the National Academy of Sciences of the United States of America
. 1979 Oct;76(10):5066–5070. doi: 10.1073/pnas.76.10.5066

On the origin of the contractile force in skeletal muscle.

W F Harrington
PMCID: PMC413080  PMID: 291923

Abstract

Analysis of the early tension responses after abrupt step changes in the length of isometrically contracting skeletal muscle shows that the magnitude of the recovery tension (T2) and the time dependence of this process at various step displacements give a good correlation with the behavior expected for a helix-coil transition in the subfragment-2 (S-2) region of myosin. The "instantaneous" tension response (to T1) after the step change in length appears to have its origin in compliance within the coil region of S-2, which is formed through helix melting at the moment of force generation.

Full text

PDF
5066

Selected References

These references are in PubMed. This may not be the complete list of references from this article.

  1. Barden J. A., Mason P. Muscle crossbridge stroke and activity revealed by optical diffraction. Science. 1978 Mar 17;199(4334):1212–1213. doi: 10.1126/science.415364. [DOI] [PubMed] [Google Scholar]
  2. Blangé T., Karemaker J. M., Kramer A. E. Tension transients after quick release in rat and frog skeletal muscles. Nature. 1972 Jun 2;237(5353):281–283. doi: 10.1038/237281a0. [DOI] [PubMed] [Google Scholar]
  3. Chiao Y. C., Harrington W. F. Cross-bridge movement in glycerinated rabbit psoas muscle fibers. Biochemistry. 1979 Mar 20;18(6):959–963. doi: 10.1021/bi00573a004. [DOI] [PubMed] [Google Scholar]
  4. Ford L. E., Huxley A. F., Simmons R. M. Tension responses to sudden length change in stimulated frog muscle fibres near slack length. J Physiol. 1977 Jul;269(2):441–515. doi: 10.1113/jphysiol.1977.sp011911. [DOI] [PMC free article] [PubMed] [Google Scholar]
  5. Harrington W. F. A mechanochemical mechanism for muscle contraction. Proc Natl Acad Sci U S A. 1971 Mar;68(3):685–689. doi: 10.1073/pnas.68.3.685. [DOI] [PMC free article] [PubMed] [Google Scholar]
  6. Huxley A. F. Muscular contraction. J Physiol. 1974 Nov;243(1):1–43. [PMC free article] [PubMed] [Google Scholar]
  7. Huxley A. F., Simmons R. M. Proposed mechanism of force generation in striated muscle. Nature. 1971 Oct 22;233(5321):533–538. doi: 10.1038/233533a0. [DOI] [PubMed] [Google Scholar]
  8. Mason P. Dynamic stiffness and crossbridge action in muscle. Biophys Struct Mech. 1977 Dec 27;4(1):15–25. doi: 10.1007/BF00538837. [DOI] [PubMed] [Google Scholar]
  9. Morimoto K., Harrington W. F. Substructure of the thick filament of vertebrate striated muscle. J Mol Biol. 1974 Feb 15;83(1):83–97. doi: 10.1016/0022-2836(74)90425-2. [DOI] [PubMed] [Google Scholar]
  10. Squire J. M. General model of myosin filament structure. II. Myosin filaments and cross-bridge interactions in vertebrate striated and insect flight muscles. J Mol Biol. 1972 Dec 14;72(1):125–138. doi: 10.1016/0022-2836(72)90074-5. [DOI] [PubMed] [Google Scholar]
  11. Sutoh K., Harrington W. F. Cross-linking of myosin thick filaments under activating and rigor conditions. A study of the radial disposition of cross-bridges. Biochemistry. 1977 May 31;16(11):2441–2449. doi: 10.1021/bi00630a020. [DOI] [PubMed] [Google Scholar]
  12. Sutoh K., Sutoh K., Karr T., Harrington W. F. Isolation and physico-chemical properties of a high molecular weight subfragment-2 of myosin. J Mol Biol. 1978 Nov 25;126(1):1–22. doi: 10.1016/0022-2836(78)90276-0. [DOI] [PubMed] [Google Scholar]
  13. Tregear R. T., Squire J. M. Myosin content and filament structure in smooth and striated muscle. J Mol Biol. 1973 Jun 25;77(2):279–290. doi: 10.1016/0022-2836(73)90336-7. [DOI] [PubMed] [Google Scholar]
  14. Tsong T. Y., Karr T., Harrington W. F. Rapid helix--coil transitions in the S-2 region of myosin. Proc Natl Acad Sci U S A. 1979 Mar;76(3):1109–1113. doi: 10.1073/pnas.76.3.1109. [DOI] [PMC free article] [PubMed] [Google Scholar]

Articles from Proceedings of the National Academy of Sciences of the United States of America are provided here courtesy of National Academy of Sciences

RESOURCES