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

Nature volume 166, page 194 (29 July 1950) | Download Citation

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Abstract

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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References

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Affiliations

  1. Research Laboratory, Courtaulds, Ltd., Maidenhead, Berks. March 15.

    • A. ELLIOTT
    • , E. J. AMBROSE
    •  & CONMAR ROBINSON

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https://doi.org/10.1038/166194a0

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