major alteration of chain configuration and yet shifts occur in the frequencies of the CO and NH bonds similar to those expected for the change from a-to p-type chain configurations. Further, chain- folding of the type indicated by the model based on the , configuration may well occur in at least part of the insulin molecule Unlike the a-helix, this type offolding would permit very easy formation of S-S links between cysteyl residues placed five residues apart in a polypeptide chain, exactly the interval found by Sanger, Smith & Kitai (1954) in the A chain of insulin.
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George et al. (1957) studied this question.
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