Abstract
THE complete structure of myoglobin in the crystalline state has been revealed through the work of Kendrew et al.1–3. One unresolved question of some interest is how much the conformation is altered when the molecule is transferred from the crystal to a dilute solution. Some pertinent information was obtained by Gurd et al.4 by comparison of the reactivity of histidine residues of sperm whale myoglobin in the crystalline state and in solution. A second possible line of attack involves a comparison of the molecular dimensions deduced crystallographically with those measured for the molecule in solution.
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References
Kendrew, J. C., Bodo, G., Dintzis, H. M., Parrish, R. G., Wyckoff, H. W., and Phillips, D. C., Nature, 181, 662 (1958).
Bodo, G., Dintzis, H. M., Kendrew, J. C., and Wyckoff, H. W., Proc. Roy. Soc., A, 253, 70 (1959).
Kendrew, J. C., Dickerson, R. E., Strondberg, B. E., Hart, R. G., Davies, D. R., Phillips, D. C., and Shore, V. C., Nature, 185, 422 (1960).
Gurd, F. R. N., Banaszak, L. J., Eylar, P. A., Andrews, P. A., and Burgner, J. M., paper presented at the 144th meeting of the American Chemical Society, Abst. of Papers, 5H (Los Angeles, California, April 1–5, 1963).
Guinier, A., and Fournet, G., Small Angle Scattering of X-rays (John Wiley and Sons, 1955).
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KRIGBAUM, W., BRIERRE, R. Molecular Conformation of Myoglobin in Dilute Solution. Nature 206, 396–397 (1965). https://doi.org/10.1038/206396a0
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DOI: https://doi.org/10.1038/206396a0
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