Abstract
BENDIT1 has recently underlined the necessity for refinement of some of the earlier ideas2 on the mechanism of the α–β transformation in wool keratin. The problem of a precise quantitative investigation of the transition is difficult, largely because of the intervention of relaxation and creep, the effects of which on the crystalline phases are unknown. Recently3, a technique for obtaining the desired diffraction data in a short time has been described, and its use, together with standard diffractometric technique, has enabled some interesting preliminary results about the transformation to be obtained.
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References
Bendit, E. G., Nature, 179, 535 (1957).
Astbury, W. T., and Woods, H. J., Phil. Trans. Roy. Soc., A, 232, 333 (1933).
Skertchly, A. R. B., Nature, 180, 802 (1957).
Alexander, P., and Smith, L. F., Proc. Int. Wool. Res. Conf. (C.S.I.R.O., Australia, 1955).
Pauling, L., and Corey, R. B., Nature, 171, 59 (1953).
Woods, H. J., J. Colloid Sci., 1, 407 (1946).
Whewell, C. S., and Woods, H. J., Symposium Fibrous Proteins (Soc. Dyers and Colourists, Bradford, 1946).
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SKERTCHLY, A. The α-β Transformation in Keratin. Nature 181, 639–640 (1958). https://doi.org/10.1038/181639b0
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DOI: https://doi.org/10.1038/181639b0
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