Abstract
THE conversion of soluble collagen (tropocollagen, procollagen, acid-extract collagen) to gelatin has been shown to involve the separation of the three-chain coiled-coil structure of the collagen molecule into single peptide chains1,2 each having the disordered random-coil configuration. The universal experience with gelatins has been that these disordered chains could not be returned to the complete native collagen structure, although optical rotation, polarized infrared, and wide-angle X-ray diffraction studies of cooled gelatin solutions or gels showed that partial ordering and helical folding of the chains could occur in localized regions3,4. The principal factor ruling against the complete reversibility of the collagen–gelatin transition was the requirement for the proper juxtaposition and recoiling of the three complex peptide chains.
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References
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VEIS, A., COHEN, J. Reversible Transformation of Gelatin to the Collagen Structure. Nature 186, 720–721 (1960). https://doi.org/10.1038/186720a0
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DOI: https://doi.org/10.1038/186720a0
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