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Near Infra- Red Spectra of Proteins and Related Substances

Abstract

IN addition to the extended configuration of a polypeptide chain, we have proposed a bent or folded configuration, and tried to explain the experimental data of proteins by the various combinations of these two basic configurations1. The experimental proof for the existence of the bent configuration of the molecule of acetylglycine anilide (I) afforded evidence in support of our view2. The same results have since been obtained for acetylglycine N-methyl amide, acetylleucine anilide and acetylleucine N-methyl amide: namely, in very dilute carbon tetrachloride solutions, these substances exhibit two characteristic absorption peaks, one at 3,450 cm.−1 arising from the NH-group in the free state, and the other at 3,330 3,360 cm.−1 from that involved in the intramolecular hydrogen bonding. (These experiments were carried out with Sugita, Kato and Kondo of this Laboratory and the details will be published elsewhere.)

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References

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MIZTJSHIMA, SI., SHIMANOUCHI, T. & TSUBOI, M. Near Infra- Red Spectra of Proteins and Related Substances. Nature 166, 406–407 (1950). https://doi.org/10.1038/166406a0

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