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Chain Configurations in Natured and Denatured Insulin: Evidence from infra-red Spectra

Naturevolume 166page194 (1950) | Download Citation



THE range of techniques available for studying the denaturing and renaturing of proteins has recently been increased by the observation1 that a change from the extended (β) chain configuration of a synthetic polypeptide to the folded (α) form is accompanied by an increase in the frequency of the infra-red absorption band characteristic of the C = O peptide link. There is already evidence2 that some denaturing processes in proteins are accompanied by an unfolding of polypeptide chains, producing the extended β-form, and it seemed of interest to see if evidence on this point could be obtained from infra-red spectra.

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    Elliott, A., and Ambrose, E. J., Nature [165, 921 (1950)]. A full account of this work has been communicated to the Royal Society.

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    Astbury, W. T., Dickinson, S., and Bailey, K., Biochem. J., 29, 2351 (1935).

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    Sanger, F., Ann. Rep. Chem. Soc., 45, 285 (1948).

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    Bamford, C. H., Hanby, W. E., and Happey, F., Nature, 164, 138 (1949).

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    Ambrose, E. J., and Hanby, W. E., Nature, 163, 483 (1949).

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    Ambrose, E. J., Elliott, A., and Temple, R. B., Nature, 163, 859 (1949).

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  1. Research Laboratory, Courtaulds, Ltd., Maidenhead, Berks

    • A. ELLIOTT
    • , E. J. AMBROSE


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