Hostname: page-component-78c5997874-m6dg7 Total loading time: 0 Render date: 2024-11-17T15:23:32.023Z Has data issue: false hasContentIssue false
  • English
  • Français

Recent X-ray diffraction studies of muscle

Published online by Cambridge University Press:  17 March 2009

Jean Hanson
Jean Hanson
Affiliation:
Medical Research Council Biophysics Research Unit, King's College, London
Get access Rights & Permissions [Opens in a new window]

Extract

An intact living muscle has such a regular structure that it diffracts light or X-rays, thereby providing patterns that contain uniquely valuable information. Interpretation of these patterns is not straightforward, but is helped by light microscopy and electron microscopy, which can often provide similar though less reliable information. At all levels of complexity, from that of the fibrils to that of the molecules, structure in a muscle is orderly. No other natural cell assembly is so suited to study by the diffraction method, and the results obtained in recent years are an outstanding example of how this method can elucidate a biological problem. In contrast to protein crystallography, where the system studied is artificial, muscle can be examined in its natural state, during normal activity. The levels of structure explored as yet in muscle are above that of the atoms in the molecules. Such structure is more commonly investigated by electron microscopy, and the application of the diffraction method to living muscle has provided a valuable check on the preparative artifacts that worry the microscopist. The great complexity of a muscle, as compared with a protein crystal, and the fact that the system is only semi-crystalline, giving a much less detailed diffraction pattern, make the problems of interpretation especially difficult. But a great deal of useful information is available about other properties of muscle and its constituents, and the flourishing state of muscle biology at present is a major factor contributing to the successful application of the diffraction method.

Type
Research Article
Information
Quarterly Reviews of Biophysics , Volume 1 , Issue 2 , June 1968 , pp. 177 - 216
Copyright
Copyright © Cambridge University Press 1968

Access options

Get access to the full version of this content by using one of the access options below. (Log in options will check for institutional or personal access. Content may require purchase if you do not have access.)

References

REFERENCES

Asakura, S., Taniguchi, M. & Oosawa, F. (1963). Mechano-chemical behaviour of F-actin. J. molec. Biol. 7, 55–69.Google Scholar
Astbury, W. T. (1949). X-ray and electron microscope studies, and their cytological significance, of the recently-discovered muscle proteins, tropomyosin and actin. Expl Cell Res. (suppl. I), pp. 234–46.Google Scholar
Burge, R. E. (1963).Equatorial X-ray diffraction by fibrous proteins. J. molec. Biol. 7, 213–24.CrossRefGoogle ScholarPubMed
Carlsen, F., Knappeis, G G. & Buchthal, F. (1961). Ultrastructure of the resting and contracted striated muscle fiber at different degrees of stretch. J. biophys. biochem. Cytol. II, 95–117.CrossRefGoogle Scholar
Cohen, C. & Hanson, J. (1956). An X-ray diffraction study of F-actin. Biochim. Biophys. Acta 21, 177–8.CrossRefGoogle Scholar
Cohen, C. & Longley, W. (1966). Tropomyosin paracrystals formed by divalent cations. Science, N.Y., 152, 794–6.Google Scholar
Davies, R. (1963). A molecular theory of contraction. Nature, Lond. 199, 1068–74.CrossRefGoogle ScholarPubMed
Ebashi, S. & Kodama, A. (1965). A new protein factor promoting aggregation of tropomyosin. J. Biochem., Tokyo 58, 107–8.Google Scholar
Ebashi, S. & Kodama, A. (1966). Native tropomyosin-like action of troponin on trypsin-treated myosin B. J. Biochem., Tokyo 60, 733–4.Google Scholar
Elliott, A. (1965). The use of toroidal reflecting surfaces in X-ray diffraction cameras. J. scient. Instrum. 42, 312–16.Google Scholar
Elliott, A. & Lowy, J. (1967). Unpublished results reported to meeting of British Biophysical Society, December 1967.Google Scholar
Elliott, G. F. (1964). X-ray diffraction studies on striated and smooth muscles. Proc. R. Soc. B 160, 467–72.Google ScholarPubMed
Elliott, G. F. (1967 a). Variations of the contractile apparatus in smooth and striated muscles. X-ray diffraction studies at rest and in contraction. J. gen. Physiol. 50, no. 6, part 2, pp. 171–84.CrossRefGoogle ScholarPubMed
Elliott, G. F. (1967 b). Unpublished results reported to meeting of British Biophysical Society, December 1967.Google Scholar
Elliott, G. F. & Lowy, J. (1961). Low-angle X-ray refiexions from living molluscan muscles. J. molec. Biol. 3, 41–6.CrossRefGoogle ScholarPubMed
Elliott, G. F. & Lowy, J. (1967). Unpublished results reported to meeting of British Biophysical Society, December 1967.Google Scholar
Elliott, G. F., Lowy, J. & Millman, B. M. (1965), X-ray diffraction from living striated muscle during contraction. Nature, Lond. 206, 1357–8.CrossRefGoogle ScholarPubMed
Elliott, G. F., Lowy, J. & Millman, B. M. (1967). Low-angle X-ray diffraction studies of living striated muscle during contraction. J. molec. Biol. 3, 31–45.CrossRefGoogle Scholar
Elliott, G. F., Lowy, J. & Worthington, C. R. (1963). An X-ray diffraction and light-diffraction study of the filament lattice of striated muscle in the living state and in rigor. J. molec. Biol. 6, 295–305.CrossRefGoogle Scholar
Elliott, G. F. & Worthington, C. R. (1959). Low-angle X-ray diffraction patterns of smooth and striated muscles. J. Physiol., Lond. 149, 32–3 P.Google Scholar
Elliott, G. F. & Worthington, C. R. (1963). A small-angle optically focusing X-ray diffraction camera in biological research. J. Ultrastruct. Res. 9, 166–76.Google Scholar
Gorden, A. M., Huxley, A. F. & Julian, F. J. (1966). The variation in isometric tension with sarcomere length in vertebrate muscle fibres. J. Physiol., Lond. 184, 170–92.Google Scholar
Hanson, J. (1967 a). Axial period of actin filaments; electron microscope studies. Nature, Lond. 213, 353–6.CrossRefGoogle Scholar
Hanson, J. (1967 b). Unpublished results reported to meeting of British Biophysical Society, December 1967.Google Scholar
Hanson, J. & Huxley, H. E. (1953). Structural basis of the cross-striations in muscle. Nature, Lond. 172, 530–2.CrossRefGoogle ScholarPubMed
Hanson, J. & Huxley, H. E. (1955). The structural basis of contraction in striated muscle. Symp. Soc. exp. Blot. 9, 228–64.Google Scholar
Hanson, J. & Lowy, J. (1961). The structure of the muscle fibres in the translucent part of the adductor of the oyster Crassostrea angulata. Proc. R. Soc. B, 154, 173–96.Google Scholar
Hanson, J. & Lowy, J. (1963). The structure of F-actin and of the actin filaments isolated from muscle. J. molec. Biol. 6, 46–60.Google Scholar
Hanson, J. & Lowy, J. (1964). The structure of actin filaments and the origin of the axial periodicity in the I-substance of vertebrate striated muscle. Proc. R. Soc. B 160, 449–58.Google Scholar
Hanson, J., Lowy, J., Huxley, H. E., Bailey, K., Kay, C. M. & Rüegg, J. C. (1957). Structure of molluscan tropomyosin. Nature, Lond. 180, 1134–5.CrossRefGoogle ScholarPubMed
Huxley, H. E. (1953 a). X-ray analysis and the problem of muscle. Proc. R. Soc. B 141, 59–62.Google ScholarPubMed
Huxley, H. E. (1953 b). Electron microscope studies of the organisation of the filaments in striated muscle. Biochim. biophys. Ada 12, 387–94.Google Scholar
Huxley, H. E. (1957). The double array of filaments in cross-striated muscle. J. biophys. biochem. Cytol. 3, 631–48.CrossRefGoogle ScholarPubMed
Huxley, H. E. (1960). Muscle cells. Chapter 7, pp. 365–481, in The Cell, vol. IV. Ed. Brachet, J., and Mirsky, A., New York and London: Academic Press.Google Scholar
Huxley, H. E. (1963). Electron microscope studies on the structure of natural and synthetic protein filaments from striated muscle. J. molec. Biol. 7, 281–308.CrossRefGoogle ScholarPubMed
Huxley, H. E. (1966). The fine structure of striated muscle and its functional significance. Harvey Lect. (series 60), pp. 85–118.Google Scholar
Huxley, H. E. (1967). Recent X-ray diffraction and electron microscope studies of striated muscle. J. gen. Physiol 50, no. 6, part 2, pp. 71–81.Google Scholar
Huxley, H. E. & Brown, W. (1967). The low-angle X-ray diagram of vertebrate striated muscle and its behaviour during contraction and rigor. J. molec. Biol. 30, 383–434.CrossRefGoogle ScholarPubMed
Huxley, H. E., Brown, W. & Holmes, K. C. (1965). Constancy of axial spacings in frog sartorius muscle during contraction. Nature, Lond. 206, 1358.Google Scholar
Huxley, H. E. & Hanson, J. (1956). Preliminary observations on the structure of insect flight muscle. In Electron Microscopy, pp. 202–4. Ed. Sjöstrand, F. S. and Rhodin, J.. Stockholm: Almqvist and Wiksell.Google Scholar
Huxley, H. E., Holmes, K. C. & Brown, W. (1966). The design requirements of vertebrate striated muscle. In Principles of Biomolecular Organization, pp. 259–69. Ed. Wolstenholme, G. E. W. and O'Connor, M.. London: Churchill.Google Scholar
Knappeis, G. G. & Carlsen, F. (1962). The ultrastructure of the Z disc in skeletal muscle. J. Cell Biol. 13, 323–35.Google Scholar
Lowey, S., Goldstein, L., Cohen, C. & Luck, S. M. (1967). Proteolytic degradation of myosin and the meromyosins by a water-insoluble polyanionic derivative of trypsin. J. molec. Biol. 23, 287–304.Google Scholar
Lowy, J., Millman, B. M. & Hanson, J. (1964). Structure and function in smooth tonic muscles of lamellibranch molluscs. Proc. R. Soc. B 160, 525–36.Google Scholar
Lowy, J. & Vibert, P. (1967 a). Structure and organisation of actin in a molluscan smooth muscle. Nature, Lond. 215, 1254–5.Google Scholar
Lowy, J. & Vibert, P. (1967 b). Unpublished results reported to meeting of British Biophysical Society, December 1967.Google Scholar
Millman, B. M. & Elliott, G. F. (1965). X-ray diffraction from contracting molluscan muscle. Nature, Lond. 206, 824–5.Google Scholar
Millman, B. M., Elliott, G. F. & Lowy, J. (1967). Axial period of actin filaments: X-ray diffraction studies. Nature, Lond. 213, 356–8.CrossRefGoogle Scholar
Ohutsuki, I., Masaki, T., Nonomura, T. & Ebashi, S. (1967). Periodic distribution of troponin along the thin filament. J. Biochem., Tokyo 61, 817–19.CrossRefGoogle Scholar
Page, S. & Huxley, H. E. (1963). Filament lengths in striated muscle. J. Cell Biol. 19, 269–90.CrossRefGoogle ScholarPubMed
Pepe, F. A. (1967). The myosin filament. J. molec. Biol. 27, 203–36.CrossRefGoogle Scholar
Perry, S. V. (1967). The structure and interactions of myosin. Progr. Biophys. Molec. Biol. 17, 325–81.CrossRefGoogle ScholarPubMed
Podolsky, R. (1964). The maximum sarcomere length for contraction of isolated myofibrils. J. Physiol., Lond. 170, 110–23.Google Scholar
Pringle, J. W. S. (1967). Evidence from insect fibrillar muscle about the elementary contractile process. J. gen. Physiol. 50, no. 6, part 2, pp. 139–6.CrossRefGoogle ScholarPubMed
Reedy, M. K. (1967). Cross-bridges and periods in insect flight muscle. Am. Zool. 7, 465–81.Google Scholar
Reedy, M. K., Holmes, K. C. & Tregear, R. T. (1965). Induced changes in orientation of the cross-bridges of glycerinated insect flight muscle. Nature, Lond., 207, 1276–80.CrossRefGoogle ScholarPubMed
Rome, E. (1967 a). Light- and X-ray diffraction studies of the filament lattice of glycerol-extracted rabbit psoas muscle. J. molec. Biol. 27, 591–602.CrossRefGoogle ScholarPubMed
Rome, E. (1967 b). Light and X-ray diffraction studies of the filament lattice of striated muscle. Ph.D. Thesis, University of London.CrossRefGoogle Scholar
Rome, E. (1968). In preparation.Google Scholar
Rowe, A. (1967). Unpublished results reported to meeting of British Biophysical Society, December 1967.Google Scholar
RÜegg, J. C. (1964). Tropomyosin-paramyosin system and ‘prolonged contraction’ in a molluscan smooth muscle. Proc. R. Soc. B 160, 536–42.Google Scholar
Selby, C. C. & Bear, R. S. (1956). The structure of actin-rich filaments of muscles according to X-ray diffraction. J. biophys. biochem. Cytol. 2, 71–8.CrossRefGoogle ScholarPubMed
Slayter, H. S. & Lowey, S. (1967). Substructure of the myosin molecule as visualized by electron microscopy. Proc. natn. Acad. Sci. 58, 1611–18.Google Scholar
Spencer, M. & Worthington, C. R. (1960). A hypothesis of contraction in striated muscle. Nature, Lond. 187, 388–91.Google Scholar
Szent-Györgyi, A. G., Cohen, C. & Philpott, D. E. (1960). Light meromyosin fraction I: a helical molecule from myosin. J. molec. Biol. 2, 133–42.Google Scholar
Szent-Györgyi, A. G. & Huxley, H. E. (1966). Unpublished results reported in Budapest Conference on Muscular Contraction.Google Scholar
Takahashi, K. & Yasui, T. (1966). Morphological changes of the lateral projections of myosin filament. J. Biochem., Tokyo 60, 231–2.Google Scholar
Worthington, C. R. (1959). Large axial spacings in striated muscle. J. molec. Biol. I, 398–401.CrossRefGoogle Scholar
Worthington, C. R. (1960). Discrete low-angle X-ray diffraction from air-dried mitochondria. J. molec. Biol. 2, 327–9.Google Scholar
Worthington, C. R. (1961). X-ray diffraction studies on the large-scale molecular structure of insect muscle. J. molec. Biol. 3, 618–33.Google Scholar