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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Elliott, A., and Ambrose, E. J., Nature [165, 921 (1950)]. A full account of this work has been communicated to the Royal Society.
Astbury, W. T., Dickinson, S., and Bailey, K., Biochem. J., 29, 2351 (1935).
Sanger, F., Ann. Rep. Chem. Soc., 45, 285 (1948).
Lens, J., J. Biol. Chem., 169, 313 (1947).
Bamford, C. H., Hanby, W. E., and Happey, F., Nature, 164, 138 (1949).
Ambrose, E. J., and Hanby, W. E., Nature, 163, 483 (1949).
Ambrose, E. J., Elliott, A., and Temple, R. B., Nature, 163, 859 (1949).
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ELLIOTT, A., AMBROSE, E. & ROBINSON, C. Chain Configurations in Natured and Denatured Insulin: Evidence from infra-red Spectra. Nature 166, 194 (1950). https://doi.org/10.1038/166194a0
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DOI: https://doi.org/10.1038/166194a0
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