Abstract
Image analysis of isolated F-actin filaments shows that the actin helix can be described by a constant rise per subunit but a considerably variable and randomized twist (number of units per turn). The ability of actin subunits to rotate through angles of the order of 10° from their helically ideal positions helps to explain actin's capacity to form many different polymorphic structures.
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References
DeRosier, D. J., Mandelkow, E., Silliman, A., Tilney, L. G. & Kane, R. E. J. molec. Biol. 113, 679–695 (1977).
Hanson, J. Nature 213, 353–356 (1967).
Bourne, G. H. The Structure and Function of Muscle (Academic, New York, 1972).
O'Brien, E. J., Gillis, J. M. & Couch, J. J. molec. Biol. 99, 461–475 (1975).
DeRosier, D. J. & Censullo, R. J. molec. Biol. 146, 77–99 (1981).
Huxley, H. E. & Brown, W. J. molec. Biol. 30, 383–434 (1967).
DeRosier, D. J., Tilney, L. G. & Flicker, P. J. molec. Biol. 137, 375–389 (1980).
Moore, P. B., Huxley, H. E. & DeRosier, D. J. J. molec. Biol. 50, 279–295 (1970).
Wakabayashi, T., Huxley, H. E., Amos, L. A. & Klug, A. J. molec. Biol. 93, 477–497 (1975).
Cohen, C. & Hanson, J. Biochim. biophys. Acta 21, 177–178 (1956).
Oosawa, F. Biophys. Chem. 11, 443–446 (1980).
Takebayashi, T. Morita, Y. & Oosawa, F. Biochim. biophys. Acta 492, 357–363 (1977).
Yanagida, T. & Oosawa, F. J. molec. Biol. 126, 507–524 (1978).
Nagashima, H. & Asakura, S. J. molec. Biol. 136, 169–182 (1980).
Suck, D., Kabsch, W. & Mannherz, H., G. Proc. natn. Acad. Sci. U.S.A. 78, 4319–4323 (1981).
Aebi, U., Fowler, W., Isenberg, G., Pollard, T. & Smith, P. R. J. Cell Biol. 91, 340–351 (1981).
Egelman, E. & DeRosier, D. J. Acta crystallogr. A (in the press).
Yamamoto, K., Yanagida, M., Kawamura, M., Maruyama, K. & Noda, H. J. molec. Biol. 91, 463–469 (1975).
Offer, G., Couch, J., O'Brien, E. & Elliott, A. J. molec. Biol. 151, 663–702 (1981).
Spudich, J. A. & Watt, S., J. biol. Chem. 246, 4866–4871 (1971).
Egelman, E. H., Francis, N. & DeRosier, D. J. J. molec. Biol. (submitted).
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Egelman, E., Francis, N. & DeRosier, D. F-actin is a helix with a random variable twist. Nature 298, 131–135 (1982). https://doi.org/10.1038/298131a0
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DOI: https://doi.org/10.1038/298131a0
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