Advertisement

Journal of Biomolecular NMR

, Volume 13, Issue 3, pp 263–274 | Cite as

Alternative E.COSY techniques for the measurement of 3J(C i −1,C i β ) and 3J(H i N ,C i β ) coupling constants in proteins

  • Frank Löhr
  • Heinz Rüterjans
Article

Abstract

Experiments are proposed for the measurement of the vicinal coupling constants between β-carbons and either amide protons of the same or carbonyl carbons of the preceding amino acid residue in 13C/15N-labeled proteins. Both couplings depend on the backbone torsional angle φ. The three-dimensional pulse sequences give rise to E.COSY-like multiplet patterns in which heteronuclear one-bond couplings separate the doublet components corresponding to the two spin states of the respective passive nuclei. Thus, in contrast to previously published pulse schemes which employed the homonuclear 1J(Cα,Cβ) interaction, difficulties due to overlap of spectral regions of active and passive spins are avoided. A major drawback of the novel sequences is their limited sensitivity. Nevertheless, application to Desulfovibrio vulgaris flavodoxin yielded coupling constants for more than 85% of all non-glycine and non-proline residues.

Desulfovibrio vulgaris flavodoxin E.COSY φ-torsion angle three-bond coupling constants 

Preview

Unable to display preview. Download preview PDF.

Unable to display preview. Download preview PDF.

References

  1. Andersson, P., Gsell, B., Wipf, B., Senn, H. and Otting, G. (1998) J. Biomol. NMR, 11, 279–288.Google Scholar
  2. Archer, S.J., Ikura, M., Torchia, D.A. and Bax, A. (1991) J. Magn. Reson., 95, 636–641.Google Scholar
  3. Blümel, M., Schmidt, J.M., Löhr, F. and Rüterjans, H. (1998) Eur. Biophys. J., 27, 321–334.Google Scholar
  4. Brüschweiler, R. and Case, D.A. (1994) J. Am. Chem. Soc., 116, 11199–11200.Google Scholar
  5. Bystrov, V.F. (1976) Prog. NMR Spectrosc., 10, 41–81.Google Scholar
  6. Cowburn, D., Live, D.H., Fischman, A.J. and Agosta, W.C. (1983) J. Am. Chem. Soc., 105, 7435–7442.Google Scholar
  7. Delaglio, F., Torchia, D.A. and Bax, A. (1991) J. Biomol. NMR, 1, 439–446.Google Scholar
  8. Emsley, L. and Bodenhausen, G. (1990) Chem. Phys. Lett., 165, 469–476.Google Scholar
  9. Geen, H. and Freeman, R. (1991) J. Magn. Reson., 93, 93–141.Google Scholar
  10. Goldman, M. (1984) J. Magn. Reson., 60, 437–452.Google Scholar
  11. Griesinger, C., Sørensen, O.W. and Ernst, R.R. (1985) J. Am. Chem. Soc., 107, 6394–6396.Google Scholar
  12. Griesinger, C., Sørensen, O.W. and Ernst, R.R. (1986) J. Chem. Phys., 85, 6837–6852.Google Scholar
  13. Griesinger, C., Sørensen, O.W. and Ernst, R.R. (1987) J. Magn. Reson., 75, 474–492.Google Scholar
  14. Grzesiek, S. and Bax, A. (1993) J. Am. Chem. Soc., 115, 12593–12594.Google Scholar
  15. Hoch, J.C., Dobson, C.M. and Karplus, M. (1985) Biochemistry, 24, 3831–3841.Google Scholar
  16. Hu, S.-J. and Bax, A. (1997) J. Am. Chem. Soc., 119, 6360–6368.Google Scholar
  17. Hu, S.-J. and Bax, A. (1998) J. Biomol. NMR, 11, 199–203.Google Scholar
  18. Jahnke, W., Baur, M., Gemmecker, G. and Kessler, H. (1995) J. Magn. Reson., B106, 86–88.Google Scholar
  19. Karplus, M. (1959) J. Chem. Phys., 30, 11–15.Google Scholar
  20. Karplus, M. (1963) J. Am. Chem. Soc., 85, 2870–2871.Google Scholar
  21. Kay, L.E., Keifer, P. and Saarinen, T. (1992) J. Am. Chem. Soc., 114, 10663–10665.Google Scholar
  22. Kay, L.E., Xu, G.Y. and Yamazaki, T. (1994) J. Magn. Reson., A109, 129–133.Google Scholar
  23. Knauf, M., Löhr, F., Blümel, M., Mayhew, S.G. and Rüterjans, H. (1996) Eur. J. Biochem., 238, 423–434.Google Scholar
  24. Löhr, F. and Rüterjans, H. (1995) J. Biomol. NMR, 5, 25–36.Google Scholar
  25. Löhr, F., Blümel, M., Schmidt, J.M. and Rüterjans, H. (1997) J. Biomol. NMR, 10, 107–118.Google Scholar
  26. Madsen, J.C. and Sørensen, O.W. (1992) J. Magn. Reson., 100, 431–436.Google Scholar
  27. Madsen, J.C., Sørensen, O.W., Sørensen, P. and Poulsen, F.M. (1993) J. Biomol. NMR, 3, 239–244.Google Scholar
  28. Marion, D. and Wüthrich, K. (1983) Biochem. Biophys. Res. Commun., 113, 967–974.Google Scholar
  29. Marion, D., Ikura, M., Tschudin, R. and Bax, A. (1989a) J. Magn. Reson., 85, 393–399.Google Scholar
  30. Marion, D., Ikura, M. and Bax, A. (1989b) J. Magn. Reson., 84, 425–430.Google Scholar
  31. Matsuo, H., Kupčce, Ē., Li, H. and Wagner, G. (1996) J. Magn. Reson., B111, 194–198.Google Scholar
  32. Meissner, A., Duus, J.Ø. and Sørensen, O.W. (1997a) J. Biomol. NMR, 10, 89–94.Google Scholar
  33. Meissner, A., Duus, J.Ø. and Sørensen, O.W. (1997b) J. Magn. Reson., 128, 92–97.Google Scholar
  34. Meissner, A., Schulte-Herbrüggen, T. and Sørensen, O.W. (1998a) J. Am. Chem. Soc., 120, 3803–3804.Google Scholar
  35. Meissner, A., Schulte-Herbrüggen, T. and Sørensen, O.W. (1998b) J. Am. Chem. Soc., 120, 7989–7990.Google Scholar
  36. Palmer III, A.G., Cavanagh, J., Wright, P.E. and Rance, M. (1991) J. Magn. Reson., 93, 151–170.Google Scholar
  37. Schmidt, J.M., Ernst, R.R., Aimoto, S. and Kainosho, M. (1995) J. Biomol. NMR, 6, 95–105.Google Scholar
  38. Schmidt, J.M., Blümel, M., Löhr, F. and Rüterjans, H. (1999) J. Biomol. NMR, in press.Google Scholar
  39. Schmieder, P. and Kessler, H. (1992) Biopolymers, 32, 435–440.Google Scholar
  40. Seip, S., Balbach, J. and Kessler, H. (1994) J. Magn. Reson., B104, 172–179.Google Scholar
  41. Shaka, A.J., Barker, P.B. and Freeman, R. (1985) J. Magn. Reson., 64, 547–552.Google Scholar
  42. Shaka, A.J., Lee, C.J. and Pines, A. (1988) J. Magn. Reson., 77, 274–293.Google Scholar
  43. Stockman, B.J., Richardson, T.E. and Swenson, R.P. (1994) Biochemistry, 33, 15298–15308.Google Scholar
  44. Stonehouse, J., Shaw, G.L., Keeler, J. and Laue, E.D. (1994) J. Magn. Reson., A107, 178–184.Google Scholar
  45. Tjandra, N., Szabo, A. and Bax, A. (1996) J. Am. Chem. Soc., 118, 6986–6991.Google Scholar
  46. Wagner, G. (1990) Prog. NMR Spectrosc., 22, 101–139.Google Scholar
  47. Wang, A.C. and Bax, A. (1995) J. Am. Chem. Soc., 117, 1810–1813.Google Scholar
  48. Wang, A.C. and Bax, A. (1996) J. Am. Chem. Soc., 118, 2483–2494.Google Scholar
  49. Watt W., Tulinsky, A., Swenson, R.P. and Watenpaugh, K.D. (1991) J. Mol. Biol., 218, 195–208.Google Scholar
  50. Wittekind, M. and Mueller, L. (1993) J. Magn. Reson., B101, 201–205.Google Scholar
  51. Zhu, G. and Bax, A. (1990) J. Magn. Reson., 90, 405–410.Google Scholar

Copyright information

© Kluwer Academic Publishers 1999

Authors and Affiliations

  • Frank Löhr
    • 1
  • Heinz Rüterjans
    • 1
  1. 1.Institut für Biophysikalische ChemieJohann Wolfgang Goethe-Universität Frankfurt am MainFrankfurtGermany

Personalised recommendations