Natural and modified wool fibers were subjected to breaking-twist-angle measurements in selected alkaline media and temperatures. The results are in accord with the crosslinking at temperatures characteristic of lanthionine and of lysinoalanine formation and with generalized degradation at highest pH conditions. Modifications of wool that inhibit crosslinkage formation are also discussed. This paper demonstrates the potential ability of breaking-twist-angle measure ments for characterizing crosslinking behavior in protein networks.
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Ellison et al. (1978) studied this question.
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