Α-β intramolecular transformation of myosin

ABSTRACT SHORTLY after the discovery and investigation by the methods of X-ray analysis1of the long-range elastic, intramolecular transformation which takes place when the fibre-substance

(keratin) of hair is stretched, the possibility emerged that the elastic mechanism of muscle is similar at least in principle to that of hair2. There is a remarkable likeness between the

X-ray photograph of washed and dried muscle and that of unstretched hair (α-keratin), and there are, moreover, certain striking analogies between their respective elastic properties.

Recently, the X-ray and elastic comparison between muscle and hair has been set out in detail3, and once more the suggestion was made that the normal molecular configuration of the muscle

protein myosin—first shown by Boehm and Weber4 to give, when oriented, an X-ray photograph resembling* that of muscle itself—is that of a folded polypeptide chain system like that of

α-keratin, which it should be possible, by extension under appropriate conditions, to transform into a fully-ex tended system like that of β-keratin (stretched hair). The present writers

tried to bring about this transformation two years ago by experiments on the sartorius muscle of the frog, but without success2. ARTICLE PDF REFERENCES * W. T. Astbury and A. Street, _Phil.

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W. A. Sisson, _Roy. Soc._—in press. * W. T. Astbury and H. J. Woods, _Phil. Trans. Roy. Soc._, A, 232, 333; 1933. H. J. Woods, _NATURE_, 132, 709; 1933. Article  ADS  Google Scholar  * E. C.

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University of Leeds, W. T. ASTBURY & SYLVIA DICKINSON Authors * W. T. ASTBURY View author publications You can also search for this author inPubMed Google Scholar * SYLVIA DICKINSON

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DICKINSON, S. α-β Intramolecular Transformation of Myosin. _Nature_ 135, 95 (1935). https://doi.org/10.1038/135095a0 Download citation * Issue Date: 19 January 1935 * DOI:

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