Abstract
IN a communication from this laboratory1, the belief has been put forward that the polypeptide chains in poly-L-alanine fibres form right-handed rather than left-handed helices; this view is based on the X-ray diffraction pattern. If it is correct, it is to be expected that the same sense of helix will be the stable form in other L-polypeptides. Now the contribution to the optical rotation of an α-polypeptide from the helix alone is considerable; according to Fitts and Kirkwood2, a right-handed helix of polyglycine should have a specific rotation of about + 130°. In a later communication3 they have concluded from the change in specific rotation on destruction of the α-helix (in poly-γ-benzyl-L-glutamate and in poly-L-glutamic acid) that in these polymers the helices are right-handed.
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References
Elliott, A., and Malcolm, B. R., Nature [178, 912 (1956)].
Fitts, D. D., and Kirkwood, J. G., Proc. U.S. Nat. Acad. Sci., 42, 33 (1956).
Fitts, D. D., and Kirkwood, J. G., J. Amer. Chem. Soc., 78, 2650 (1956).
Doty, P., Holtzer, A. M., Bradbury, J. H., and Blout, E. R., J. Amer. Chem. Soc., 76, 4493 (1954). Doty, P., Bradbury, J. H., and Holtzer, A. M., ibid., 78, 947 (1956). Doty, P., and Yang, J. T., ibid., 78, 498 (1956).
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ELLIOTT, A., HANBY, W. & MALCOLM, B. Optical Rotation of the α-Helix in Synthetic Polypeptides. Nature 178, 1170 (1956). https://doi.org/10.1038/1781170a0
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DOI: https://doi.org/10.1038/1781170a0
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