Thermoanalytical investigations of extended and annealed keratins |
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Authors: | M Spei R Holzem |
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Institution: | (1) Present address: Lehrstuhl für Makromolekulare Chemie der RWTH Aachen, Aachen, FRG |
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Abstract: | DSC investigations have been used to characterize the microfibril-matrix complex of keratin consisting of helical low-sulfur microfibrils in a nonhelical high-sulfur matrix. The corresponding DSC curves display one or two endothermic peaks in the temperature range 230°–255°C. The first peak is a microfibrillar peak and the second one a matrix peak (cystine decomposition peak). DSC investigations of extended keratins have shown that the microfibrillar peak is a helix peak. DSC investigations of annealed keratins confirm our earlier assumption that the helix peak is no helix melting peak but an irreversible helix unfolding, superimposed by various decomposition reactions. The matrix peak of the above described keratin samples is less reproducible than the corresponding helix peak and cannot be used for further characterization studies of keratins.Dedicated to Professor E. G. Klesper on the occasion of his 60th birthday. |
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Keywords: | -keratins" target="_blank">gif" alt="agr" align="BASELINE" BORDER="0">-keratins DSC-investigations microfibril-matrix complex helix peak matrix peak |
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