Skip to main content
PMC home page
Biophysical Journal logoLink to Biophysical Journal
. 1995 May;68(5):2023–2031. doi: 10.1016/S0006-3495(95)80379-6

Analysis of equatorial x-ray diffraction patterns from muscle fibers: factors that affect the intensities.

S Malinchik 1, L C Yu 1
PMCID: PMC1282105  PMID: 7612844

Abstract

Previously we have shown that cross-bridge attachment to actin and the radial position of the myosin heads surrounding the thick filament backbone affect the equatorial x-ray diffraction intensities in different ways (Yu, 1989). In the present study, other factors frequently encountered experimentally are analyzed by a simple model of the filament lattice. It is shown that the ordering/disordering of filaments, lattice spacing changes, the azimuthal redistributions of cross-bridges, and variations in the ordered/disordered population of cross-bridges surrounding the thick filaments can distinctly affect the equatorial intensities. Consideration of Fourier transforms of individual components of the unit cell can provide qualitative explanations for the equatorial intensity changes. Criteria are suggested that can be used to distinguish the influence of some factors from others.

Full text

PDF
2024

Selected References

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

  1. Brenner B., Yu L. C. Equatorial x-ray diffraction from single skinned rabbit psoas fibers at various degrees of activation. Changes in intensities and lattice spacing. Biophys J. 1985 Nov;48(5):829–834. doi: 10.1016/S0006-3495(85)83841-8. [DOI] [PMC free article] [PubMed] [Google Scholar]
  2. Brenner B., Yu L. C., Podolsky R. J. X-ray diffraction evidence for cross-bridge formation in relaxed muscle fibers at various ionic strengths. Biophys J. 1984 Sep;46(3):299–306. doi: 10.1016/S0006-3495(84)84026-6. [DOI] [PMC free article] [PubMed] [Google Scholar]
  3. Brenner B., Yu L. C. Structural changes in the actomyosin cross-bridges associated with force generation. Proc Natl Acad Sci U S A. 1993 Jun 1;90(11):5252–5256. doi: 10.1073/pnas.90.11.5252. [DOI] [PMC free article] [PubMed] [Google Scholar]
  4. Cecchi G., Griffiths P. J., Bagni M. A., Ashley C. C., Maeda Y. Time-resolved changes in equatorial x-ray diffraction and stiffness during rise of tetanic tension in intact length-clamped single muscle fibers. Biophys J. 1991 Jun;59(6):1273–1283. doi: 10.1016/S0006-3495(91)82342-6. [DOI] [PMC free article] [PubMed] [Google Scholar]
  5. Haselgrove J. C., Stewart M., Huxley H. E. Cross-bridge movement during muscle contraction. Nature. 1976 Jun 17;261(5561):606–608. doi: 10.1038/261606a0. [DOI] [PubMed] [Google Scholar]
  6. Huxley H. E., Kress M., Faruqi A. F., Simmons R. M. X-ray diffraction studies on muscle during rapid shortening and their implications concerning crossbridge behaviour. Adv Exp Med Biol. 1988;226:347–352. [PubMed] [Google Scholar]
  7. Huxley H. E., Simmons R. M., Faruqi A. R., Kress M., Bordas J., Koch M. H. Changes in the X-ray reflections from contracting muscle during rapid mechanical transients and their structural implications. J Mol Biol. 1983 Sep 15;169(2):469–506. doi: 10.1016/s0022-2836(83)80062-x. [DOI] [PubMed] [Google Scholar]
  8. Huxley H. E. Structural difference between resting and rigor muscle; evidence from intensity changes in the lowangle equatorial x-ray diagram. J Mol Biol. 1968 Nov 14;37(3):507–520. doi: 10.1016/0022-2836(68)90118-6. [DOI] [PubMed] [Google Scholar]
  9. Irving M., Lombardi V., Piazzesi G., Ferenczi M. A. Myosin head movements are synchronous with the elementary force-generating process in muscle. Nature. 1992 May 14;357(6374):156–158. doi: 10.1038/357156a0. [DOI] [PubMed] [Google Scholar]
  10. Irving T. C., Millman B. M. Changes in thick filament structure during compression of the filament lattice in relaxed frog sartorius muscle. J Muscle Res Cell Motil. 1989 Oct;10(5):385–394. doi: 10.1007/BF01758435. [DOI] [PubMed] [Google Scholar]
  11. Lowy J., Popp D., Stewart A. A. X-ray studies of order-disorder transitions in the myosin heads of skinned rabbit psoas muscles. Biophys J. 1991 Oct;60(4):812–824. doi: 10.1016/S0006-3495(91)82116-6. [DOI] [PMC free article] [PubMed] [Google Scholar]
  12. Lowy J., Poulsen F. R. Studies of the diffuse x-ray scattering from contracting frog skeletal muscles. Biophys J. 1990 May;57(5):977–985. doi: 10.1016/S0006-3495(90)82617-5. [DOI] [PMC free article] [PubMed] [Google Scholar]
  13. Lowy J., Poulsen F. R. X-ray study of myosin heads in contracting frog skeletal muscle. J Mol Biol. 1987 Apr 20;194(4):595–600. doi: 10.1016/0022-2836(87)90236-1. [DOI] [PubMed] [Google Scholar]
  14. Lymn R. W. Equatorial X-ray reflections and cross arm movement in skeletal muscle. Nature. 1975 Dec 25;258(5537):770–772. doi: 10.1038/258770a0. [DOI] [PubMed] [Google Scholar]
  15. Lymn R. W. Myosin subfragment-1 attachment to actin. Expected effect on equatorial reflections. Biophys J. 1978 Jan;21(1):93–98. doi: 10.1016/S0006-3495(78)85510-6. [DOI] [PMC free article] [PubMed] [Google Scholar]
  16. Miller A., Tregear R. T. Structure of insect fibrillar flight muscle in the presence and absence of ATP. J Mol Biol. 1972 Sep 14;70(1):85–104. doi: 10.1016/0022-2836(72)90165-9. [DOI] [PubMed] [Google Scholar]
  17. Podolsky R. J., St Onge H., Yu L., Lymn R. W. X-ray diffraction of actively shortening muscle. Proc Natl Acad Sci U S A. 1976 Mar;73(3):813–817. doi: 10.1073/pnas.73.3.813. [DOI] [PMC free article] [PubMed] [Google Scholar]
  18. Poole K. J., Rapp G., Maéda Y., Goody R. S. The time course of changes in the equatorial diffraction patterns from different muscle types on photolysis of caged-ATP. Adv Exp Med Biol. 1988;226:391–404. [PubMed] [Google Scholar]
  19. Rayment I., Rypniewski W. R., Schmidt-Bäse K., Smith R., Tomchick D. R., Benning M. M., Winkelmann D. A., Wesenberg G., Holden H. M. Three-dimensional structure of myosin subfragment-1: a molecular motor. Science. 1993 Jul 2;261(5117):50–58. doi: 10.1126/science.8316857. [DOI] [PubMed] [Google Scholar]
  20. Yagi N., Takemori S., Watanabe M. An X-ray diffraction study of frog skeletal muscle during shortening near the maximum velocity. J Mol Biol. 1993 Jun 5;231(3):668–677. doi: 10.1006/jmbi.1993.1318. [DOI] [PubMed] [Google Scholar]
  21. Yu L. C. Analysis of equatorial x-ray diffraction patterns from skeletal muscle. Biophys J. 1989 Mar;55(3):433–440. doi: 10.1016/S0006-3495(89)82837-1. [DOI] [PMC free article] [PubMed] [Google Scholar]
  22. Yu L. C., Brenner B. Structures of actomyosin crossbridges in relaxed and rigor muscle fibers. Biophys J. 1989 Mar;55(3):441–453. doi: 10.1016/S0006-3495(89)82838-3. [DOI] [PMC free article] [PubMed] [Google Scholar]
  23. Yu L. C., Steven A. C., Naylor G. R., Gamble R. C., Podolsky R. J. Distribution of mass in relaxed frog skeletal muscle and its redistribution upon activation. Biophys J. 1985 Mar;47(3):311–321. doi: 10.1016/S0006-3495(85)83921-7. [DOI] [PMC free article] [PubMed] [Google Scholar]
  24. Yu L. P., Hartt J. E., Podolsky R. J. Equatorial x-ray intensities and isometric force levels in frog sartorius muscle. J Mol Biol. 1979 Jul 25;132(1):53–67. doi: 10.1016/0022-2836(79)90495-9. [DOI] [PubMed] [Google Scholar]

Articles from Biophysical Journal are provided here courtesy of The Biophysical Society

RESOURCES