Abstract
INFRARED spectra in the far-infrared region are very sensitive to the conformational changes of polypeptide backbones1–6. We have measured the infrared spectra of sequential polypeptides in the region from 700 to 200 cm−1 and have found several far-infrared bands characteristic of component amino-acid residues with α-helical and β-form conformations.
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References
Miyazawa, T., Bull. Chem. Soc. Jap., 34, 691 (1961).
Suzuki, S., Iwashita, Y., Shimanouchi, T., & Tsuboi, M., Biopolymers, 4, 337 (1966).
Miyazawa, T., Fukushima, K., Sugano, S., & Masuda, Y., Conformations of Biopolymers (edit. by Ramachandran, G. N.), 557 (Academic Press, New York and London, 1967).
Itoh, K., Nakahara, T., Shimanouchi, T., Oya, M., Uno, K., & Iwakura, Y., Biopolymers, 6, 1759 (1968).
Itoh, K., Shimanouchi, T., & Oya, M., Biopolymers, 7, 649 (1969).
Itoh, K., & Shimanouchi, T., Biopolymers, 9, 383 (1970).
Kovacs, J., Giannotti, R., & Kapoor, A., J. Amer. Chem. Soc., 88, 2281 (1966).
Itoh, K., & Katabuchi, H., Biopolymers (in the press).
Itoh, K., Oya, M., & Shimanouchi, T., Biopolymers (in the press).
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ITOH, K., KATABUCHI, H. & SHIMANOUCHI, T. Far-infrared Bands of Amino-acid Residues with α-Helical and β-Form Conformations. Nature New Biology 239, 42–43 (1972). https://doi.org/10.1038/newbio239042a0
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DOI: https://doi.org/10.1038/newbio239042a0