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. 1974 Aug;71(8):3265–3269. doi: 10.1073/pnas.71.8.3265

Carbon-13 Magnetic Resonance Evaluation of Polypeptide Secondary Structure and Correlation with Proton Magnetic Resonance Studies

D W Urry 1,2, L W Mitchell 1,2, T Ohnishi 1,2
PMCID: PMC388665  PMID: 4528456

Abstract

With the use of appropriately chosen solvent pairs it is demonstrated that solvent dependence of peptide carbonyl carbon resonances can be correlated with polypeptide secondary structure. Solvent titrations show the peptide carbonyl which is intramolecularly hydrogen bonded to exhibit less chemical shift on going from a dimethylsulfoxide solution to a solution containing a solvent which is a good proton (or deuteron) donor. Effective solvent systems are dimethylsulfoxide paired with water, trifluoroethanol, or methanol. This approach is demonstrated with the pentapeptide of elastin.

Keywords: polypeptide conformation, carbonyl delineation, hydrogen bonding, elastin pentapeptide

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Selected References

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

  1. Brewster A. I., Hruby V. J., Spatola A. F., Bovey F. A. Carbon-13 nuclear magnetic resonance spectroscopy of oxytocin, related oligopeptides, and selected analogs. Biochemistry. 1973 Apr 10;12(8):1643–1649. doi: 10.1021/bi00732a028. [DOI] [PubMed] [Google Scholar]
  2. Deslauriers R., Walter R., Smith I. C. A carbon-13 nuclear magnetic resonance study of oxytocin and its oligopeptides. Biochem Biophys Res Commun. 1972 Aug 21;48(4):854–859. doi: 10.1016/0006-291x(72)90686-9. [DOI] [PubMed] [Google Scholar]
  3. Kopple K. D., Ohnishi M., Go A. Conformations of cyclic peptides. IV. Nuclear magnetic resonance studies of cyclo-pentaglycyl-L-leucyl and cyclo-diglycyl-L-histidyldiglycyl-L-tyrosyl. Biochemistry. 1969 Oct;8(10):4087–4095. doi: 10.1021/bi00838a028. [DOI] [PubMed] [Google Scholar]
  4. Ohnishi M., Urry D. W. Temperature dependence of amide proton chemical shifts: the secondary structures of gramicidin S and valinomycin. Biochem Biophys Res Commun. 1969 Jul 23;36(2):194–202. doi: 10.1016/0006-291x(69)90314-3. [DOI] [PubMed] [Google Scholar]
  5. Pinkerton M., Steinrauf L. K., Dawkins P. The molecular structure and some transport properties of valinomycin. Biochem Biophys Res Commun. 1969 May 22;35(4):512–518. doi: 10.1016/0006-291x(69)90376-3. [DOI] [PubMed] [Google Scholar]
  6. Pitner T. P., Urry D. W. Proton magnetic resonance studies in trifluoroethanol. Solvent mixtures as a means of delineating peptide protons. J Am Chem Soc. 1972 Feb 23;94(4):1399–1400. doi: 10.1021/ja00759a083. [DOI] [PubMed] [Google Scholar]
  7. Rudko A. D., Lovell F. M., Low B. W. Prolactin synthesis in primates. Nat New Biol. 1971 Jul 7;232(27):18–19. [PubMed] [Google Scholar]
  8. Sogn J. A., Craig L. C., Gibbons W. A. The complete assignment of the 13C nuclear magnetic resonance spectrum of the decapeptide gramicidin S-A by selective biosynthetic enrichment studies. J Am Chem Soc. 1974 May 15;96(10):3306–3309. doi: 10.1021/ja00817a046. [DOI] [PubMed] [Google Scholar]
  9. Stern A., Gibbons W. A., Craig L. C. A conformational analysis of gramicidin S-A by nuclear magnetic resonance. Proc Natl Acad Sci U S A. 1968 Oct;61(2):734–741. doi: 10.1073/pnas.61.2.734. [DOI] [PMC free article] [PubMed] [Google Scholar]
  10. Urry D. W., Cunningham W. D., Ohnishi T. Studies on the conformation and interactions of elastin. Proton magnetic resonance of the repeating pentapeptide. Biochemistry. 1974 Jan 29;13(3):609–616. doi: 10.1021/bi00700a032. [DOI] [PubMed] [Google Scholar]
  11. Urry D. W., Ohnishi M., Walter R. Secondary structure of the cyclic moiety of the peptide hormone oxytocin and its deamino analog. Proc Natl Acad Sci U S A. 1970 May;66(1):111–116. doi: 10.1073/pnas.66.1.111. [DOI] [PMC free article] [PubMed] [Google Scholar]
  12. Urry D. W., Walter R. Proposed conformation of oxytocin in solution. Proc Natl Acad Sci U S A. 1971 May;68(5):956–958. doi: 10.1073/pnas.68.5.956. [DOI] [PMC free article] [PubMed] [Google Scholar]
  13. Walter R., Prasad K. U., Deslauriers R., Smith I. C. Conformational studies of oxytocin, lysine vasopressin, arginine vasopressin, and arginine vasotocin by carbon-13 nuclear magnetic resonance spectroscopy. Proc Natl Acad Sci U S A. 1973 Jul;70(7):2086–2090. doi: 10.1073/pnas.70.7.2086. [DOI] [PMC free article] [PubMed] [Google Scholar]

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