Abstract
X-RAY studies of the fibrous proteins indicate that they fall almost exclusively into one or other of two main configurational groups, the keratin-myosin group and the collagen group1. The interpretation of the structure and properties of the former group is now well advanced and has frequently been reported on in NATURE and elsewhere, but the structure of the latter, in spite of many investigations, has hitherto remained unexplained. It was suggested several years ago that the amino-acid residues in gelatin (which also gives the typical collagen diffraction pattern) are somehow grouped in threes with probably every third a glycine residue and every ninth a hydroxyproline residue, that the strong meridian arc of spacing about 2.86 A. is associated with the average length of a residue in the direction of the fibre axis, and that such an average length could very well arise from an alternate cis- and trans- configuration2; but further progress was not possible for lack of experimental data. More recent chemical and X-ray evidence points now to a solution that is both simple and convincing.
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ASTBURY, W., BELL, F. Molecular Structure of the Collagen Fibres. Nature 145, 421–422 (1940). https://doi.org/10.1038/145421a0
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DOI: https://doi.org/10.1038/145421a0
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