Abstract
THE stability of feather keratin in the solid state is due to cross-Unking of the polypeptide chains by hydrogen bonds, disulphide linkages and electrostatic forces, and under conditions where these bonds are broken solutions of the protein are obtained. The molecular characteristics of the particles in solution are of interest because of their relevance to the interpretation of the data obtained by the diffraction and scatter of X-rays by solid keratin, and the interaction of the particles in solution is relevant to the problem of the manufacture of fibres from the regenerated keratin. I wish to present here data of this sort for soluble feather keratin and in particular to identify the keratin monomer, which it was considered would be a particle in which bonding between the polypeptide chains due to hydrogen bonds, disulphide linkages and electrostatic attraction was absent.
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References
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Huggins, C., Tapley, D. F., and Jensen, E. V., Nature, 167, 592 (1951).
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WOODIN, A. Soluble Feather Keratin. Nature 173, 823–824 (1954). https://doi.org/10.1038/173823a0
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DOI: https://doi.org/10.1038/173823a0
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