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
. 1973 Oct;70(10):2732–2736. doi: 10.1073/pnas.70.10.2732

Theory of Muscular Contraction Extended to Groups of Actin Sites

Terrell L Hill 1
PMCID: PMC427097  PMID: 4517930

Abstract

It was shown in an earlier paper how to connect, in principle, the biochemical states of a cross-bridge with the mechanics of muscular contraction, by the methods of statistical mechanics. The treatment applies to cross-bridges that are able to interact with only one actin site at a time. The present paper shows that it is a straightforward matter to extend the theory to groups of actin sites (three, five, etc.), say 55 Å apart, as suggested by the work of Moore, H. E. Huxley, and DeRosier. The possibility of the cross-bridge attachment slipping between sites is included. This provides an alternative molecular interpretation of the model introduced by A. F. Huxley and Simmons. A second possible interpretation is also suggested: their discrete stable angles correspond to different biochemical (attached) states. The Huxley-Simmons analysis of an example is rederived and extended somewhat (x averaging), from the point of view of the present theory. Their qualitative conclusions are left unchanged by the x averaging, but significant quantitative effects are possible. Possible consequences of fast slipping in isotonic contraction are discussed in a preliminary way.

Keywords: statistical mechanics, sliding filament model, biochemical state diagram, Huxley-Simmons analysis

Full text

PDF
2732

Selected References

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

  1. Hill T. L. On the sliding-filament model of muscular contraction, II. Proc Natl Acad Sci U S A. 1968 Sep;61(1):98–105. doi: 10.1073/pnas.61.1.98. [DOI] [PMC free article] [PubMed] [Google Scholar]
  2. Hill T. L. Sliding filament model of muscular contraction. V. Isometric force and interfilament spacing. J Theor Biol. 1970 Dec;29(3):395–410. doi: 10.1016/0022-5193(70)90105-0. [DOI] [PubMed] [Google Scholar]
  3. Hill T. L., White G. M. On the sliding-filament model of muscular contraction, IV. Calculation of force-velocity curves. Proc Natl Acad Sci U S A. 1968 Nov;61(3):889–896. doi: 10.1073/pnas.61.3.889. [DOI] [PMC free article] [PubMed] [Google Scholar]
  4. 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]
  5. Lymn R. W., Taylor E. W. Mechanism of adenosine triphosphate hydrolysis by actomyosin. Biochemistry. 1971 Dec 7;10(25):4617–4624. doi: 10.1021/bi00801a004. [DOI] [PubMed] [Google Scholar]
  6. Moore P. B., Huxley H. E., DeRosier D. J. Three-dimensional reconstruction of F-actin, thin filaments and decorated thin filaments. J Mol Biol. 1970 Jun 14;50(2):279–295. doi: 10.1016/0022-2836(70)90192-0. [DOI] [PubMed] [Google Scholar]
  7. Podolsky R. J., Nolan A. C., Zaveler S. A. Cross-bridge properties derived from muscle isotonic velocity transients. Proc Natl Acad Sci U S A. 1969 Oct;64(2):504–511. doi: 10.1073/pnas.64.2.504. [DOI] [PMC free article] [PubMed] [Google Scholar]
  8. Trentham D. R., Bardsley R. G., Eccleston J. F., Weeds A. G. Elementary processes of the magnesium ion-dependent adenosine triphosphatase activity of heavy meromyosin. A transient kinetic approach to the study of kinases and adenosine triphosphatases and a colorimetric inorganic phosphate assay in situ. Biochem J. 1972 Feb;126(3):635–644. doi: 10.1042/bj1260635. [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