New Evidence on the structure of Some Proteins from Measurements with Polarized Infra-red Radiation

Abstract

CURRENT views on the structure of keratin, myosin and related proteins are based on chemical analyses and on X-ray diffraction data. The X-ray evidence (Astbury and Street1 ) shows that these proteins may exist in either of two forms, α and β, each of which shows a characteristic X-ray diffraction photograph. The most intense meridian reflexion corresponds to a chain spacing in the α-form Of about 5·1 A., while in the β-form the chain spacing is about 3·3 A. Since it is possible, after suitable softening treatment, to change a natural protein in the α-form to the β-form by stretching or squeezing, it is generally assumed that the poly-pentide chains in the α-form are folded in some way, whereas the β-form corresponds to the extended chain. Astbury2 has proposed a particular form of folding for α-keratin ; Huggins3, Wrinch4, and Wrinch and Jordan Lloyd5 have suggested a number of other possibilities. In an interesting recent paper by Astbury, Dalgleish, Darmon and Sutherland6 the properties of some synthetic polypeptides and natural proteins have been discussed, both from the point of view of X-ray diffraction and infra-red absorption.

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AMBROSE, E., ELLIOTT, A. & TEMPLE, R. New Evidence on the structure of Some Proteins from Measurements with Polarized Infra-red Radiation. Nature 163, 859–862 (1949). https://doi.org/10.1038/163859a0

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