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X-Ray Interpretation of the Molecular Structure of Gelatine

Abstract

IN a recent communication1 it was shown how X-ray studies indicate that the average dimensions associated with an amino-acid residue in an extended protein chain are of the order of 3½, 4½ and 9½ A., the first being the length in the direction of the main-chain, the second the thickness of the main-chain, and the third the lateral extension of the side-chains: it was shown also how these three quantities account for the observed average density of proteins and the weight per unit area of mono-molecular protein films. More recently2 the arguments have been applied with some precision to the case of -keratin, for which the dimensions in question are found by X-rays to be 3.38, 4.65, and 9.8 A., respectively, while the density3 is 1.30 and the weighted mean residue weight about 115 (so far as can be estimated from available chemical analyses4). We can thus set out the following relation: which is a reasonably strict demonstration of the point we wished to make, namely, that the dimensions 3.38, 4.65, and 9.8 A. in -keratin are on the average those of one amino-acid residue.

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References

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ASTBURY, W., ATKIN, W. X-Ray Interpretation of the Molecular Structure of Gelatine. Nature 132, 348 (1933). https://doi.org/10.1038/132348a0

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