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Short Pseudo-repeat in Paramyosin

Abstract

PARAMYOSIN, a fibrous protein which has so far only been found in the muscles of invertebrates, gives an X-ray pattern with sharp 1.5 and 5.1 Å meridional and diffuse 10 Å near-equatorial reflexions and so is classified with α-keratin, myosin and fibrinogen as an α-fibrous protein. The X-ray patterns of these proteins differ, however, in the low-angle region where the pattern may be indexed on a repeat of 198 Å for α-keratin1, 420 Å for striated muscle2, 226 Å for fibrinogen3 and 725 Å for paramyosin4. The only one of these low-angle patterns which is clearly understood is that of paramyosin which may be interpreted in terms of either the two-dimensional net shown in Fig. 1(a) or a helix5. Electron micrographs have shown a two-dimensional pattern of spots6 similar to the lattice in Fig. 1(a) where the axial repeat is 725 Å, and this is reduced to 145 Å in axial projection (Fig. 1(b)). This communication reports a pseudo-repeat of 29 Å in axial projection which shows up when the paramyosin is treated with silver.

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References

  1. MacArthur, I., Nature, 152, 38 (1943).

    Article  ADS  CAS  Google Scholar 

  2. Huxley, H. E., Proc. Roy. Soc., B, 141, 59 (1953).

    ADS  CAS  Google Scholar 

  3. Stryer, L., Cohen, C., and Langridge, R., Nature, 197, 793 (1963).

    Article  ADS  CAS  Google Scholar 

  4. Bear, R. S. J., Amer. Chem. Soc., 67, 1625 (1945).

    Article  CAS  Google Scholar 

  5. Bear, R. S., and Selby, C. C. J., Biophys. Biochem. Cytol., 2, 55 (1956).

    Article  CAS  Google Scholar 

  6. Schmitt, F. O., Bear, R. S., Hall, C. E., and Jakus, M. A., Ann. N.Y. Acad. Sci., 47, 799 (1947).

    Article  ADS  CAS  Google Scholar 

  7. Robertson, J. M., J. Chem. Soc., 1195 (1936).

  8. Robertson, J. M., and Woodward, I., J. Chem. Soc., 219 (1937).

  9. Kendrew, J. C., Dickerson, R. E., Strandberg, B. E., Hart, R. G., Davies, D. R., Phillips, D. C., and Shore, V. C., Nature, 185, 422 (1960).

    Article  ADS  CAS  Google Scholar 

  10. Bear, R. S., Adv. Protein Chem., 7, 69 (1952).

    Article  CAS  Google Scholar 

  11. Fraser, R. D. B., and MacRae, T. P., Nature, 179, 732 (1957).

    Article  ADS  CAS  Google Scholar 

  12. Fraser, R. D. B., and MacRae, T. P., J. Mol. Biol., 1, 387 (1959).

    Article  CAS  Google Scholar 

  13. Hodge, A. J., Proc. U.S. Nat. Acad. Sci., 38, 850 (1952).

    Article  ADS  CAS  Google Scholar 

  14. Cohen, C., and Holmes, K. C., J. Mol. Biol., 6, 423 (1963).

    Article  CAS  Google Scholar 

  15. Cohen, C., and Szent-Györgyi, A. G. J., Amer. Chem. Soc., 79, 248 (1957).

    Article  CAS  Google Scholar 

  16. Petruska, J. A., and Hodge, A. J., Proc. U.S. Nat. Acad. Sci., 51, 871 (1964).

    Article  ADS  CAS  Google Scholar 

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MILLER, A. Short Pseudo-repeat in Paramyosin. Nature 207, 524–525 (1965). https://doi.org/10.1038/207524a0

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