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. 1971 Dec;68(12):3088–3091. doi: 10.1073/pnas.68.12.3088

Nuclear Magnetic Resonance Studies of Lysine-Vasopressin: Structural Constraints

P H Von Dreele *, A I Brewster *, F A Bovey *, H A Scheraga *, M F Ferger *, V Du Vigneaud *
PMCID: PMC389596  PMID: 5289251

Abstract

The 220-MHz proton NMR spectra of lysine-vasopressin and some related compounds are examined in deuterated dimethyl sulfoxide to obtain structural information that must be satisfied by any proposed conformation of the molecule. This structural information is in the form of dihedral angles (for rotation about the NH-CαH bonds) from coupling constants, possible hydrogen bonding of the CONH2 and backbone amide groups from the temperature-dependence of the chemical shift, and aromatic ring-aromatic ring interaction from the effect of the magnetically anisotropic groups on the chemical shift.

Keywords: temperature dependence of chemical shifts, coupling constants, magnetically anisotropic groups

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Selected References

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

  1. Bystrov V. F., Portnova S. L., Tsetlin V. I., Ivanov V. T., Ovchinnikov Y. A. Conformational studies of peptide systems. The rotational states of the NH--CH fragment of alanine dipeptides by nuclear magnetic resonance. Tetrahedron. 1969 Feb;25(3):493–515. doi: 10.1016/s0040-4020(01)83261-0. [DOI] [PubMed] [Google Scholar]
  2. CASH W. D., MAHAFFEY L. M., BUCK A. S., NETTLETON D. E., Jr, ROMAS C., DUVIGNEAUD V. SYNTHESIS AND BIOLOGICAL PROPERTIES OF 9-SARCOSINE OXYTOCIN. J Med Pharm Chem. 1962 May;91:413–423. doi: 10.1021/jm01238a001. [DOI] [PubMed] [Google Scholar]
  3. Deslauriers R., Smith I. C. Evidence from proton magnetic resonance data for the stacking of aromatic amino acids in lysine-vasopressin: comparison with oxytocin derivatives and related dipeptides. Biochem Biophys Res Commun. 1970 Jul 13;40(1):179–185. doi: 10.1016/0006-291x(70)91063-6. [DOI] [PubMed] [Google Scholar]
  4. Gillessen D., Du Vigneaud V. The synthesis and pharmacological properties of 4-decarboxamido-8-lysine-vasopressin, 5-decarboxamido-8-lysine-vasopressin, and their 1-deamino analogues. J Biol Chem. 1967 Oct 25;242(20):4806–4812. [PubMed] [Google Scholar]
  5. Hruby V. J., Brewster A. I., Glasel J. A. NMR studies on the conformation of derivatives of the side chain of oxytocin: examples of cis-trans isomerism. Proc Natl Acad Sci U S A. 1971 Feb;68(2):450–453. doi: 10.1073/pnas.68.2.450. [DOI] [PMC free article] [PubMed] [Google Scholar]
  6. Isemura T., Okabayashi H., Sakakibara S. Steric structure of L-proline oligopeptides. I. Infrared absorption spectra of the oligopeptides and poly-L-proline. Biopolymers. 1968;6(3):307–321. doi: 10.1002/bip.1968.360060306. [DOI] [PubMed] [Google Scholar]
  7. Kopple K. D. Conformations of cyclic peptides. V. A proton magnetic resonance study of evolidine, cyclo-ser-phe-leu-pro-val-asn-leu. Biopolymers. 1971;10(7):1139–1152. doi: 10.1002/bip.360100705. [DOI] [PubMed] [Google Scholar]
  8. 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]
  9. Lewis P. N., Momany F. A., Scheraga H. A. Folding of polypeptide chains in proteins: a proposed mechanism for folding. Proc Natl Acad Sci U S A. 1971 Sep;68(9):2293–2297. doi: 10.1073/pnas.68.9.2293. [DOI] [PMC free article] [PubMed] [Google Scholar]
  10. McDonald C. C., Phillips W. D. Proton magnetic resonance spectra of proteins in random-coil configurations. J Am Chem Soc. 1969 Mar 12;91(6):1513–1521. doi: 10.1021/ja01034a039. [DOI] [PubMed] [Google Scholar]
  11. 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]
  12. 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]
  13. 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]
  14. Von Dreele P. H., Brewster A. I., Scheraga H. A., Ferger M. F., Du Vigneaud V. Nuclear magnetic resonance spectrum of lysine-vasopressin and its structural implications. Proc Natl Acad Sci U S A. 1971 May;68(5):1028–1031. doi: 10.1073/pnas.68.5.1028. [DOI] [PMC free article] [PubMed] [Google Scholar]

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