Advertisement

Journal of Biomolecular NMR

, Volume 12, Issue 3, pp 417–421 | Cite as

Effects of sample preparation conditions on biomolecular solid-state NMR lineshapes

  • David L. Jakeman
  • Dan J. Mitchell
  • Wendy A. Shuttleworth
  • Jeremy N.S. Evans
Article

Abstract

Sample preparation conditions with the 46 kDa enzyme complex of 5-enolpyruvyl-shikimate-3-phosphate (EPSP) synthase, shikimate-3-phosphate (S3P) and glyphosate (GLP) have been examined in an attempt to reduce linewidths in solid-state NMR spectra. The linewidths of 13P resonances associated with enzyme bound S3P and GLP in the lyophilized ternary complex have been reduced to 150 ± 12 Hz and 125 ± 7 Hz respectively, by a variety of methods involving additives and freezing techniques.

EPSP synthase fast freezing narrowing linewidths 13P NMR solid-state NMR trehalose 

Preview

Unable to display preview. Download preview PDF.

Unable to display preview. Download preview PDF.

References

  1. Appleyard, R.J. and Evans, J.N.S. (1993) J. Magn. Reson. Series B, 102, 245–252.Google Scholar
  2. Appleyard, R.J., Shuttleworth, W.A. and Evans, J.N. S. (1994) Biochemistry, 33, 6812–6821.Google Scholar
  3. Barlow, P.N., Appleyard, R.J., Wilson, B.J.O. and Evans, J.N.S. (1989) Biochemistry, 28, 7985–7991 and correction p. 10093.Google Scholar
  4. Bondinell, W.E., Vrek, J., Knowles, P.F., Sprecher, M. and Sprinson, D.B. (1971) J. Biol. Chem., 246, 6191–6196.Google Scholar
  5. Bradford, M.M. (1976) Anal. Biochem., 72, 248–254.Google Scholar
  6. Butler, S.L. and Falke, J.J. (1996) Biochemistry, 35, 10595–10600.Google Scholar
  7. Carpenter, J.F., Pikal, M.J., Chang, B.S. and Randolph, T.W. (1997) Pharm. Res., 14, 969–975.Google Scholar
  8. Chen, P.S., Toribara, T.Y. and Warner, H. (1956) Anal. Chem., 28, 1756–1758.Google Scholar
  9. Christensen, A.M. and Schaefer, J. (1993) Biochemistry, 32, 2868–2873.Google Scholar
  10. Clegg, J.S. (1965) Comp. Biochem. Physiol., 14, 135–143.Google Scholar
  11. Crowe, L.M., Reid, D.S. and Crowe, J.H. (1996) Biophys. J., 71, 2087–2093.Google Scholar
  12. Evans, J.N.S. (1992) In Pulsed Magnetic Resonance: NMR, ESR and Optics (A Recognition of E.L. Hahn) Oxford University Press, Oxford and New York.Google Scholar
  13. Evans, J.N.S. (1995) In Encyclopedia of NMR, John Wiley & Sons.Google Scholar
  14. Evans, J.N.S. (1996) Biomolecular NMR Spectroscopy, Oxford University Press, Oxford and New York.Google Scholar
  15. Evans, J.N.S., Appleyard, R.J. and Shuttleworth, W. (1992) Bull. Magn. Reson., 14, 81–85.Google Scholar
  16. Evans, J.N.S., Appleyard, R.J. and Shuttleworth, W.A. (1993) J. Am. Chem. Soc., 115, 1588–1590.Google Scholar
  17. Glaubitz, C. and Watts, A. (1998) J. Magn. Reson., 130, 305–316.Google Scholar
  18. Gregory, R.B., Gangoda, M., Gilpin, R.K. and Su, W. (1993a) Biopolymers, 33, 1871–1876.Google Scholar
  19. Gregory, R.B., Gangoda, M., Gilpin, R.K. and Su, W. (1993b) Biopolymers, 33, 513–519.Google Scholar
  20. Griffiths, J.M. and Griffin, R.G. (1993) Anal. Chim. Acta, 283, 1081–1101.Google Scholar
  21. Lazo, N.D., Hu, W. and Cross, T.A. (1992) J. Chem. Soc., Chem. Commun., 1529–1531.Google Scholar
  22. Lazo, N.D., Hu, W., Lee, K.-C. and Cross, T.A. (1993) Biochem. Biophys. Res. Commun., 197, 904–909.Google Scholar
  23. Lee, C.W., Das Gupta, S.K., Mattai, J., Shipley, G.G., Abdel-Mageed, O.H., Makriyannis, A. and Griffin, R.G. (1989) Biochemistry, 28, 5000–5009.Google Scholar
  24. Lee, C.W., Waugh, J.S. and Griffin, R.G. (1986) Biochemistry, 25, 3737–3742.Google Scholar
  25. Lin, T.Y. and Timasheff, S.N. (1996) Protein Sci., 5, 372–381.Google Scholar
  26. McDowell, L.M., Klug, C.A., Beusen, D.D. and Schaefer, J. (1996a) Biochemistry, 35, 5395–5403.Google Scholar
  27. McDowell, L.M. and Schaefer, J. (1996) Curr. Opin. Struct. Biol., 6, 624–629.Google Scholar
  28. McDowell, L.M., Schmidt, A., Cohen, E.R., Studelska, D.R. and Schaefer, J. (1996b) J. Mol. Biol., 256, 160–171.Google Scholar
  29. Millican, R.C. (1963) Anal. Biochem., 6, 181.Google Scholar
  30. Opella, S.J. (1997) Nat. Struct. Biol., 4, 845–848.Google Scholar
  31. Shuttleworth, W.A., Hough, C.D., Bertrand, K.P. and Evans, J.N.S. (1992) Protein Eng., 5, 461–466.Google Scholar
  32. Sikorski, J.A. and Gruys, K.J. (1997) Acc. Chem. Res., 30, 2–8.Google Scholar
  33. Smith, S.O. and Peersen, O.B. (1992) Annu. Rev. Biophys. Biomol. Struct., 21, 25–47.Google Scholar
  34. Tjandra, N. and Bax, A. (1997) Science, 278, 1697–1697.Google Scholar
  35. Tomita, Y., Oconnor, E.J. and McDermott, A. (1994) J. Am. Chem. Soc., 116, 8766–8771.Google Scholar
  36. Tycko, R. (1996) J. Biomol. NMR, 8, 239–251.Google Scholar
  37. Van Veldhoven, P.P. and Mannaerts, G.P. (1987) Anal. Biochem., 161, 45–48.Google Scholar
  38. Xie, G. and Timasheff, S.N. (1997a) Protein Sci., 6, 211–221.Google Scholar
  39. Xie, G. and Timasheff, S.N. (1997b) Biophys. Chem., 64, 25–43.Google Scholar

Copyright information

© Kluwer Academic Publishers 1998

Authors and Affiliations

  • David L. Jakeman
    • 1
  • Dan J. Mitchell
    • 1
  • Wendy A. Shuttleworth
    • 1
  • Jeremy N.S. Evans
    • 1
  1. 1.Department of Biochemistry and BiophysicsWashington State UniversityPullmanU.S.A

Personalised recommendations