Abstract
IN recent communications1 to this and other journals, the hypothesis has been developed of a lactam-lactim interchange (I) to account for the linear folding of polypeptide chains in keratin and myosin and what appears to be a similar, generalized, intramolecular folding in the globular proteins. We wish to point out that in certain respects the argument is unchanged if, instead of a lactam-lactim, a keto-enol interchange (II) is postulated.
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References
Frank, F. C., and Astbury, W. T., J. Text. Inst., 27, P282 (1936) ; Chem. Weekbl., 33, 778 (1936). Wrinch, D. M., NATURE, 137, 411 (1936); 138, 241 (1936) ; Proc. Roy. Soc., A (in the press). Frank, F. C., NATURE, 138, 242 (1936).
Jordan Lloyd, D., Biol. Rev., 7, 254 (1932) ; Jordan Lloyd, D., and Marriott, R. H., Trans. Far. Soc., 29, 1228 (1933). Mirsky, A. and Pauling, L., Proc. Nat. Acad. Sci., 22, 439 (1936). Wrinch, D. M., and Jordan Lloyd, D., NATURE, 138, 758 (1936).
Huggins, M. L., NATURE, 139, 550 (1937).
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ASTBURY, W., WRINCH, D. Intramolecular Folding of Proteins by Keto-Enol Interchange. Nature 139, 798 (1937). https://doi.org/10.1038/139798a0
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DOI: https://doi.org/10.1038/139798a0
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