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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DOI: https://doi.org/10.1038/220371b0
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