DOI QR코드

DOI QR Code

The Structure Change Study on the Actin-Myosin Cross-Bridges in SH of Myosin Head by The Computer Data

컴퓨터 분석에 의한 Myosin Head의 SH가 Actin-Myosin Cross-Bridges에 따른 구조변화 연구

  • Kim, Duck-Sool (Department of Computer Engineering Tongmyong University of Information Technology) ;
  • Ok, Soo-Yol (Department of Computer Engineering Tongmyong University of Information Technology) ;
  • Park, Keun-Ho (Department of Chemical Engineering, Changwon National University)
  • 김덕술 (동명정보대학교 컴퓨터공학과) ;
  • 옥수열 (동명정보대학교 컴퓨터공학과) ;
  • 박근호 (창원대학교 공과대학 화공시스템공학과)
  • Published : 2005.03.31

Abstract

IASL(iodo acetamide) and MSL(maleimide) disordered the orderly helix arrangement of myosin in the rest state of spin level. Especially the effect of IASL was great. Equatorial refiection(10,11) change inferred that myosin head was moved to the vicinity of actin filament by spin level. The intensity change of 143${\AA}$ and 72${\AA}$ could offer information of the mass projection of population of myosin heads along the :filament axis. The slope of intensity profile of the mass projection of 143${\AA}$ and reflection of IASL is appeared and that of MSL is appeared sharply. The decrease of 215${\AA}$ reflection intensity is appeared the periodical characteristic of 143${\AA}$ reflection by spin label. The raise of MSL actin reflection at 51${\AA}$ and 59${\AA}$ in the actin reflection change refers that the shifted myosin head binds a certain actin or changes an actin structure by spin label effect. Because iodo acetamide has a tendency to decease the actin reflection, actin dose not bind myosin head. From this result, we could conclude that LASL and MSL are spin labeled on SH of myosin head and disordered the helix arrangement of actin.

Keywords

References

  1. K. Wakabayashi and Y. Amemiya, 'Handbook on Synchrotron Radiation.', pp. 597, vol. 4. Progress in X-ray Synchrotron Diffraction Studies of Muscle Contraction, North Holland. Amsterdam (1991)
  2. K. Wakabayashi. H. Tanaka, T. Kobayashi. T. Hamanaka, S. Nishizawa, H. Sugi, and T. Mitsui. Dynamic X-ray Diffraction of Skeletal Muscle Contraction Structural Change of Actin Filaments, Adv. Biophys., 27, 3 (1991)
  3. H. E. Huxley, Mechanical Transients and the Origin of Muscular Force, Science, 164, 1365 (1969) https://doi.org/10.1126/science.164.3882.969
  4. H. E. Huxley, A. R. Farqi, and M. Brown, The Low-Angle X-ray Diagram of Vertebrate Striated Muscle and Its Behaviour during Contraction and Rigor, J. Mol. Biol., 30, 383 (1967)
  5. H. E. Huxley, R. M. Simmons, A. R. Farqi, and M. Kress, X-ray Diffraction Studies on Muscle during Shortening and Their Implications Concerning Crossbridge Behaviour, Adv. Exp. Med. Biol., 266, 347 (1988).
  6. H. E. Huxley, A. R. Farqi, M. Kress, J. Bordas, and M. H. J. Koch, Time Resolved X-ray Diffraction Studies of The Myosin Layer-Line Reflections during Muscle Contraction, J. Mol. Biol., 158, 637 (1982)
  7. Y. Amemiya, K. Wakabayashi, T. Hamanaka, T. Wakabayashi, T. Matsushta, and H. Hashizume, Design of a Small-Angle X-ray Diffractometer usmg Synchrotron Radiation at The Photon Factory, Nucl. Instrum. Methods, 208, 471 (1983)
  8. I. Matsubara and N. Yagi, Structural Change m The Thin Filament during Activation Studied by X-ray Diffraction by Highly Stretched Skeletal Muscle, J. Mol. Biol., 208, 359 (1989)
  9. M. A. Bagni, G. Cecchi, F. Coloma, and C. Poggesi, Tension and Stiffness of Frog Muscle fibers at Full Filament Overlap, J. Muscle Res. Cell Motil., 11, 371 (1990)
  10. H. Iwamoto, T. Kobayashi, Y. Amemiya, and K. Wakabayashi, Effect of Stretch and Release on Equatorial X-ray Diffraction During a Twitch Contraction of Frog Skeletal Muscle, Biophys. J., 68, 227 (1995)
  11. M. Kress, H. E. Huxley, A. R. Faruqi, and J. Hendrix, Structural Changes during Activation of Frog Muscle Studies by Time-Resolved X-ray Diffraction, J. Mol. Biol., 188, 325 (1986)
  12. K. Wang, R. McCarter, J. Wright, J. Beverly, and R. Ramirez - Mitchel, Viscoelasticity of the Sarcomere Matrix of Skeletal Muscle Contraction The Actin-Myosin Composite Filament is a Dual-Stage Molecular Spring, Biophys. J., 64, 1161 (1993)
  13. N. Yagi, Effects of N-ethlmaleimide on The Structure of Skinned Frog Skeletal Muscle, J. Muscle Res. Cell Matil., 13, 457 (1992)
  14. N. Yagi and I. Matsubara, 'Structural Changes in The Thin Filament during Activation Studied by X-ray Diffraction by Highly Stretched Skeletal Muscle, J. Mol. Biol., 208, 359 (1989)
  15. K. Wakabayashi, H. Saito, T. Kobayashi, Y. Ueno, and H. Tanaka, Detection of The Spacing Changes of Muscle Thin Filaments during Force Generation by X-ray diffraction, Photon Factory Act. Rep., 10, 352 (1992)
  16. K. Hirose, T. J. M. Murray, C. Franzini-Armstrong, and Y. E. Goldman, Structural Changes in Muscle crossbridge accompanying Force Generation, J. Cell Biol., 127, 763 (1994)
  17. H. Yagi, S. Takemori, and M. Yamaguchi, An X-ray Diffraction Study of Frog Skeletal Muscle during Shortening near The Maximum Velocity, J. Mol. Biol., 231, (1993)