Evidence for Order in the Structure of α-Elastin

  • An Erratum to this article was published on 28 December 1968

Abstract

THE structure of elastin, the insoluble constituent protein of elastic fibres occurring in the intercellular spaces of connective tissues, has been investigated and different models have been proposed. While a fibril structure is supported by electron microscope results1–3, the rubber-like properties of the water swollen elastin have been interpreted as evidence for a cross-linked network of randomly coiled chains4–6. According to Partridge7,8, elastin should be composed of globular protein molecules arranged in a tetrahedral packing, but Ramachandran9,10 has suggested a collagen-like triple helical structure on the basis of X-ray analysis and of amino-acid composition.

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MAMMI, M., GOTTE, L. & PEZZIN, G. Evidence for Order in the Structure of α-Elastin. Nature 220, 371–373 (1968). https://doi.org/10.1038/220371b0

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