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. 1981 Dec;36(3):509–517. doi: 10.1016/S0006-3495(81)84749-2

Determination of beta-turn conformation by laser Raman spectroscopy.

H Ishizaki, P Balaram, R Nagaraj, Y V Venkatachalapathi, A T Tu
PMCID: PMC1327643  PMID: 7326322

Abstract

To correlate the Raman frequencies of the amide I and III bands to beta-turn structures, three peptides shown to contain beta-turn structure by x-ray diffraction and NMR were examined. The compounds examined were tertiary (formula: see text). The amide I band of these compounds is seen at 1,668, 1,665, and 1,677 cm-1, and the amide III band appears at 1,267, 1,265, and 1,286 cm-1, respectively. Thus, it is concluded that the amide I band for type III beta-turn structure appears in the range between 1,665 and 1,677 cm-1 and the amide III band between 1,265 and 1,286 cm-1.

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Selected References

These references are in PubMed. This may not be the complete list of references from this article.

  1. Ballardin A., Fischman A. J., Gibbons W. A., Roy J., Schwartz I. L., Smith C. W., Walter R., Wyssbrod H. R. Conformational studies on [Pro3, Gly4]-oxytocin in dimethyl sulfoxide by 1H nuclear magnetic resonance spectroscopy: evidence for a type II beta turn in the cyclic moiety. Biochemistry. 1978 Oct 17;17(21):4443–4454. doi: 10.1021/bi00614a014. [DOI] [PubMed] [Google Scholar]
  2. Bandekar J., Krimm S. Vibrational analysis of peptides, polypeptides, and proteins. VI. Assignment of beta-turn modes in insulin and other proteins. Biopolymers. 1980 Jan;19(1):31–36. doi: 10.1002/bip.1980.360190103. [DOI] [PubMed] [Google Scholar]
  3. Bandekar J., Krimm S. Vibrational analysis of peptides, polypeptides, and proteins: Characteristic amide bands of beta-turns. Proc Natl Acad Sci U S A. 1979 Feb;76(2):774–777. doi: 10.1073/pnas.76.2.774. [DOI] [PMC free article] [PubMed] [Google Scholar]
  4. Chou P. Y., Fasman G. D. Beta-turns in proteins. J Mol Biol. 1977 Sep 15;115(2):135–175. doi: 10.1016/0022-2836(77)90094-8. [DOI] [PubMed] [Google Scholar]
  5. Han S. L., Stimson E. R., Maxfield F. R., Scheraga H. A. Conformational study of [Leu5]-enkephalin by laser Raman spectroscopy. Int J Pept Protein Res. 1980 Sep;16(3):173–181. [PubMed] [Google Scholar]
  6. Hruby V. J., Deb K. K., Fox J., Bjarnason J., Tu A. T. Conformational studies of peptide hormones using laser Raman and circular dichroism spectroscopy. A comparative study of oxytocin agonists and antagonists. J Biol Chem. 1978 Sep 10;253(17):6060–6067. [PubMed] [Google Scholar]
  7. Hseu T. H., Chang H. Laser Raman studies on the conformation of Pro-Leu-Gly-NH2. Biochim Biophys Acta. 1980 Aug 21;624(2):340–345. doi: 10.1016/0005-2795(80)90075-6. [DOI] [PubMed] [Google Scholar]
  8. Krimm S., Bandekar J. Vibrational analysis of peptides, polypeptides, and proteins. V. Normal vibrations of beta-turns. Biopolymers. 1980 Jan;19(1):1–29. doi: 10.1002/bip.1980.360190102. [DOI] [PubMed] [Google Scholar]
  9. Lippert J. L., Tyminski D., Desmeules P. J. Determination of the secondary structure of proteins by laser Raman spectroscopy. J Am Chem Soc. 1976 Oct 27;98(22):7075–7080. doi: 10.1021/ja00438a057. [DOI] [PubMed] [Google Scholar]
  10. Mueller P., Rudin D. O. Action potentials induced in biomolecular lipid membranes. Nature. 1968 Feb 24;217(5130):713–719. doi: 10.1038/217713a0. [DOI] [PubMed] [Google Scholar]
  11. Nikiforovich G. V., Leonova V. I., Galaktionov S. G., Chipens G. I. Theoretical conformational analysis of oxytocin molecule. Int J Pept Protein Res. 1979 Apr;13(4):363–373. doi: 10.1111/j.1399-3011.1979.tb01894.x. [DOI] [PubMed] [Google Scholar]
  12. Pezolet M., Pigeon-Gosselin M., Coulombe L. Laser Raman investigation of the conformation of human immunoglobulin G. Biochim Biophys Acta. 1976 Dec 22;453(2):502–512. doi: 10.1016/0005-2795(76)90146-x. [DOI] [PubMed] [Google Scholar]
  13. Rao C. P., Nagaraj R., Rao C. N., Balaram P. Infrared spectroscopy as a probe for the development of secondary structure in the amino-terminal segment of alamethicin. FEBS Lett. 1979 Apr 15;100(2):244–248. doi: 10.1016/0014-5793(79)80343-9. [DOI] [PubMed] [Google Scholar]
  14. Rao C. P., Nagaraj R., Rao C. N., Balaram P. Infrared studies on the conformation of synthetic alamethicin fragments and model peptides containing alpha-aminoisobutyric acid. Biochemistry. 1980 Feb 5;19(3):425–431. doi: 10.1021/bi00544a004. [DOI] [PubMed] [Google Scholar]
  15. Shamala N., Nagaraj R., Balaram P. The crystal and molecular structure of the amino terminal tetrapeptide of alamethicin. A novel 310 helical conformation. Biochem Biophys Res Commun. 1977 Nov 7;79(1):292–298. doi: 10.1016/0006-291x(77)90094-8. [DOI] [PubMed] [Google Scholar]
  16. Spiro T. G., Gaber B. P. Laser Raman scattering as a probe of protein structure. Annu Rev Biochem. 1977;46:553–572. doi: 10.1146/annurev.bi.46.070177.003005. [DOI] [PubMed] [Google Scholar]
  17. Tu A. T., Bjarnason J. B., Hruby V. J. Conformation of oxytocin studied by laser Raman spectroscopy. Biochim Biophys Acta. 1978 Apr 26;533(2):530–533. doi: 10.1016/0005-2795(78)90399-9. [DOI] [PubMed] [Google Scholar]
  18. Tu A. T., Lee J., Deb K. K., Hruby V. J. Laser Raman spectroscopy and circular dichroism studies of the peptide hormones mesotocin, vasotocin, lysine vasopressin, and arginine vasopressin. Conformational analysis. J Biol Chem. 1979 May 10;254(9):3272–3278. [PubMed] [Google Scholar]
  19. Venkatachalapathi Y. V., Balaram P. An incipient 3(10) helix in Piv-Pro-Pro-Ala-NHMe as a model for peptide folding. Nature. 1979 Sep 6;281(5726):83–84. doi: 10.1038/281083a0. [DOI] [PubMed] [Google Scholar]
  20. Williams R. W., Dunker A. K., Peticolas W. L. A NEW METHOD FOR DETERMINING PROTEIN SECONDARY STRUCTURE BY LASER RAMAN SPECTROSCOPY APPLIED TO fd PHAGE. Biophys J. 1980 Oct;32(1):232–234. doi: 10.1016/S0006-3495(80)84944-7. [DOI] [PMC free article] [PubMed] [Google Scholar]
  21. Yu N. T. Raman spectroscopy: a conformational probe in biochemistry. CRC Crit Rev Biochem. 1977;4(3):229–280. doi: 10.3109/10409237709102559. [DOI] [PubMed] [Google Scholar]

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