Skip to main content
Log in

Propagation of experimental uncertainties using the Lipari-Szabo model-free analysis of protein dynamics

  • Published:
Journal of Biomolecular NMR Aims and scope Submit manuscript

Abstract

In this paper we make use of the graphical procedure previously described [Jin, D. et al. (1997) J. Am. Chem. Soc., 119, 6923–6924] to analyze NMR relaxation data using the Lipari-Szabo model-free formalism. The graphical approach is advantageous in that it allows the direct visualization of the experimental uncertainties in the motional parameter space. Some general ‘rules’ describing the relationship between the precision of the relaxation measurements and the precision of the model-free parameters and how this relationship changes with the overall tumbling time (τm) are summarized. The effect of the precision in the relaxation measurements on the detection of internal motions not close to the extreme narrowing limit is analyzed. We also show that multiple timescale internal motions may be obscured by experimental uncertainty, and that the collection of relaxation data at very high field strength can improve the ability to detect such deviations from the simple Lipari-Szabo model.

This is a preview of subscription content, log in via an institution to check access.

Access this article

Price excludes VAT (USA)
Tax calculation will be finalised during checkout.

Instant access to the full article PDF.

Similar content being viewed by others

References

  • Abragam, A. (1961) The Principles of Nuclear Magnetism, The International Series of Monographs on Physics, Oxford, Oxford University Press.

    Google Scholar 

  • Boyd, J., Hommel, U. and Campbell, I. (1990) Chem. Phys. Lett., 175, 477-482.

    Google Scholar 

  • Brainard, J.R. and Szabo, A. (1981) Biochemistry, 20, 4618-4628.

    Google Scholar 

  • Bretthorst, G.L. (1990a) J. Magn. Reson., 88, 533-551.

    Google Scholar 

  • Bretthorst, G.L. (1990b) J. Magn. Reson., 88, 552-570.

    Google Scholar 

  • Cai, M., Huang, Y., Prakash, O., Wen, L., Dunkelbarger, S.P., Huang, J.-K., Liu, J. and Krishnamoorthi, R. (1996) Biochemistry, 35, 4784-4794.

    Google Scholar 

  • Clore, G.M., Driscoll, P.C., Wingfield, P.T. and Gronenborn, A.M. (1990a) Biochemistry, 29, 7387-7401.

    Google Scholar 

  • Clore, G.M., Szabo, A., Bax, A., Kay, L.E., Driscoll, P.C. and Gronenborn, A.M. (1990b) J. Am. Chem. Soc., 112, 4989-4991.

    Google Scholar 

  • Combettes, P.L. (1993) Proc. IEEE, 81, 182-208.

    Google Scholar 

  • Epstein, D.M., Benkovic, S.J. and Wright, P.E. (1995) Biochemistry, 34, 11037-11048.

    Google Scholar 

  • Farrow, N.A., Zhang, O., Forman-Kay, J.D. and Kay, L.E. (1995) Biochemistry, 34, 868-878.

    Google Scholar 

  • Farrow, N.A., Zhang, O., Forman-Kay, J.D. and Kay, L.E. (1997) Biochemistry, 36, 2390-2402.

    Google Scholar 

  • Fushman, D., Weisemann, R., Thüring, H. and Rüterjans, H. (1994) J. Biomol. NMR, 4, 61-78.

    Google Scholar 

  • Henry, G.D., Weiner, J.H. and Sykes, B.D. (1986) Biochemistry, 25, 590-598.

    Google Scholar 

  • Hodsdon, M.E. and Cistola, D.P. (1997) Biochemistry, 36, 2278-2290.

    Google Scholar 

  • Jin, D., Figueirido, F., Montelione, G.T. and Levy, R.M. (1997) J. Am. Chem. Soc., 119, 6923-6924.

    Google Scholar 

  • Kass, R.E. and Raftery, A.E. (1995) J. Am. Stat. Assoc., 90, 773-795.

    Google Scholar 

  • Kay, L.E., Torchia, D.A. and Bax, A. (1989) Biochemistry, 28, 8972-8979.

    Google Scholar 

  • Kinosita, K., Kawato, S. and Ikegami, A. (1977) Biophys. J., 20, 289.

    Google Scholar 

  • Kördel, J., Skelton, N.J., Akke, M., Palmer III, A.G. and Chazin, W.J. (1992) Biochemistry, 31, 4856-4866.

    Google Scholar 

  • Korzhnev, D.M., Orekhov, V.Y. and Arseniev, A.S. (1997) J. Magn. Reson., 127, 184-191.

    Google Scholar 

  • Levy, R.M., Karplus, M. and McCammon, J.A. (1981) J. Am. Chem. Soc., 103, 994-996.

    Google Scholar 

  • Li, Y. and Montelione, G.T. (1995) Biochemistry, 34, 2408-2423.

    Google Scholar 

  • Lipari, G. and Szabo, A. (1982) J. Am. Chem. Soc., 104, 4546-4559.

    Google Scholar 

  • Liu, J., Prakash, O., Cai, M., Gong, Y., Wen, L., Wen, J.J., Huang, J.-K. and Krishnamoorthi, R. (1996) Biochemistry, 35, 1516-1524.

    Google Scholar 

  • London, R.E. (1980) Magnetic Resonance in Biology, Vol. I, John Wiley & Sons, New York, NY.

    Google Scholar 

  • Luginbühl, P., Pervushin, K.V., Iwai, H. and Wüthrich, K. (1997) Biochemistry, 36, 7305-7312.

    Google Scholar 

  • Mandel, A.M., Akke, M. and Palmer III, A.G. (1995) J. Mol. Biol., 246, 144-163.

    Google Scholar 

  • Mandel, A.M., Akke, M. and Palmer III, A.G. (1996) Biochemistry, 35, 16009-16023.

    Google Scholar 

  • Nicholson, L.K., Yamazaki, T., Torchia, D.A., Grzesiek, S., Bax, A., Stahl, S.J., Kaufman, J.D., Wingfield, P.T., Lam, P.Y.S., Jadhav, P.K., Hodge, C.N., Domaille, P.J. and Chang, C.-H. (1995) Nat. Struct. Biol., 2, 274-280.

    Google Scholar 

  • Orekhov, V.Y., Pervushin, K.V. and Arseniev, A.S. (1994) Eur. J. Biochem., 219, 887-896.

    Google Scholar 

  • Palmer III, A.G., Rance, M. and Wright, P.E. (1991) J. Am. Chem. Soc., 113, 4371-4380.

    Google Scholar 

  • Papavoine, C.H.M., Remerowski, M.L., Horstink, L.M., Konings, R.N.H., Hilbers, C.W. and van de Ven, F.J.M. (1997) Biochemistry, 36, 4015-4026.

    Google Scholar 

  • Peng, J.-W. and Wagner, G. (1992) Biochemistry, 31, 8571-8586.

    Google Scholar 

  • Schneider, D.M., Dellwo, M.J. and Wand, A.J. (1992) Biochemistry, 31, 3645-3652.

    Google Scholar 

  • Schurr, J.M., Babcock, H.P. and Fujimoto, B.S. (1994) J. Magn. Reson. B., 105, 211-224.

    Google Scholar 

  • Stivers, J.T., Abeygunawardana, C. and Mildvan, A.S. (1996) Biochemistry, 35, 16036-16047.

    Google Scholar 

  • Stone, M.J., Fairbother, W.J., Palmer III, A.G., Reizer, J., Saier, M.H. and Wright, P.E. (1992) Biochemistry, 31, 4394-4406.

    Google Scholar 

  • Tjandra, N., Szabo, A. and Bax, A. (1996a) J. Am. Chem. Soc., 118, 6986-6991.

    Google Scholar 

  • Tjandra, N., Wingfield, P., Stahl, S. and Bax, A. (1996b) J. Biomol. NMR, 8, 273-284.

    Google Scholar 

  • Wallach, D.J. (1967) J. Chem. Phys., 47, 3258.

    Google Scholar 

  • Weaver, A.J., Kemple, M.D. and Prendergast, F.G. (1988) Biophys. J., 54, 1-15.

    Google Scholar 

  • Williams, K.A., Farrow, N.A., Deber, C.M. and Kay, L.E. (1996) Biochemistry, 35, 5145-5157.

    Google Scholar 

  • Wittebort, R.J. and Szabo, A. (1978) J. Chem. Phys., 69, 1722.

    Google Scholar 

  • Woessner, D.E. (1962) J. Chem. Phys., 37, 647-654.

    Google Scholar 

  • Yamasaki, K., Saito, M., Oobatake, M. and Kanaya, S. (1995) Biochemistry, 34, 6587-6601.

    Google Scholar 

  • Zhou, H., McEvoy, M.M., Lowry, D.F., Swanson, R.V., Simon, M.I. and Dahlquist, F.W. (1996) Biochemistry, 35, 433-443.

    Google Scholar 

Download references

Author information

Authors and Affiliations

Authors

Rights and permissions

Reprints and permissions

About this article

Cite this article

Jin, D., Andrec, M., Montelione, G.T. et al. Propagation of experimental uncertainties using the Lipari-Szabo model-free analysis of protein dynamics. J Biomol NMR 12, 471–492 (1998). https://doi.org/10.1023/A:1008313319334

Download citation

  • Issue Date:

  • DOI: https://doi.org/10.1023/A:1008313319334

Navigation