Abstract
Two recent communications1,2 have described the results of stereochemical model studies of insulin based on the α-helix structure and using the detailed amino-acid residue sequences established by Sanger and his associates3. Both studies were made using identical packing models4 in which the fundamental residue unit (—NH.CH(R).CO—) dimensions are different from those derived by Pauling and Corey5 from experimental studies of amino-acid and peptide structures. The cystine residue bond-lengths and bond-angles recorded by Arndt and Riley2 differ markedly from those found by Yakel and Hughes6 in N.N′-diglycyl-L-cystine. While local deviations in bond-lengths and bond-angles of the residue units and of the hydrogen bonds, brought about by side-chain (R) group interactions, may perhaps be expected along the peptide chain of a native protein, the overall use of dimensions which differ considerably from the experimentally derived values appears to be a purely arbitrary procedure.
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References
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Harfenist, E. J., and Craig, L. C., J. Amer. Chem. Soc., 74, 3087 (1952)
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LOW, B. Experimental Data and Model Structures for the Insulin Molecule. Nature 172, 1146–1147 (1953). https://doi.org/10.1038/1721146a0
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DOI: https://doi.org/10.1038/1721146a0
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