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Addressing the overlap problem in the quantitative analysis of two dimensional NMR spectra: Application to 15N relaxation measurements

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Abstract

A quantitative analysis of 2D 1H-15N spectra is often complicated by resonance overlap. Here a simple method is presented for resolving overlapped correlations by recording 2D projection planes from HNCO data sets. Applications are presented involving the measurement of 15N T relaxation rates in a high molecular weight protein, malate synthase G, and in a system that exchanges between folded and unfolded states, the drkN SH3 domain. By supplementing relaxation data recorded in the conventional way as a series of 2D 1H-15N data sets with a series of a pair of projection planes the number of dynamics probes is increased significantly for both systems studied.

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References

  • Boyd, J. and Soffe, N. (1989) J. Magn. Reson., 85, 406–413.

    Google Scholar 

  • Caffrey, M., Kaufman, J., Stahl, S.J., Wingfield, P.T., Gronenborn, A.M. and Clore, G.M. (1998) J. Magn. Reson., 135, 368–372.

    Google Scholar 

  • Coggins, B.E., Venters, R.A. and Zhou, P. (2004) J. Am. Chem. Soc., 126, 1000–1001.

    Google Scholar 

  • Griesinger, C. and Ernst, R.R. (1987) J. Magn. Reson., 75, 261–271.

    Google Scholar 

  • Grzesiek, S. and Bax, A. (1993) J. Biomol. NMR, 3, 185–204.

    Google Scholar 

  • Gutmanas, A., Tu, L., Yu, V., Orekhov, V.Y. and Billeter, M. (2004) J. Magn. Reson. 167, 107–113.

    Google Scholar 

  • Howard, B.R., Endrizzi, J.A. and Remington, S.J. (2000) Biochemistry, 39, 3156–3168.

    Google Scholar 

  • Kamith, U. and Shriver, J.W. (1989) J. Biol. Chem., 264, 5586–5592.

    Google Scholar 

  • Kay, L.E., Ikura, M., Tschudin, R. and Bax, A. (1990) J. Magn. Reson., 89, 496–514.

    Google Scholar 

  • Kay, L.E., Keifer, P. and Saarinen, T. (1992a) J. Am. Chem. Soc., 114, 10663–10665.

    Google Scholar 

  • Kay, L.E., Nicholson, L.K., Delaglio, F., Bax, A. and Torchia, D.A. (1992b) J. Magn. Reson., 97, 359–375.

    Google Scholar 

  • Kim, S. and Szyperski, T. (2003) J. Am. Chem. Soc., 125, 1385–1393.

    Google Scholar 

  • Kim, S. and Szyperski, T. (2004) J. Biomol. NMR., 28, 117–130.

    Google Scholar 

  • Kupče, E. and Freeman, R. (2003a) J. Biomol. NMR, 27, 101–113.

    Google Scholar 

  • Kupče, E. and Freeman, R. (2003b) J. Am. Chem. Soc., 125, 13958–13959.

    Google Scholar 

  • Kupče, E. and Freeman, R. (2003c) J. Biomol. NMR, 27, 383–387.

    Google Scholar 

  • Kupče, E. and Freeman, R. (2004a) J. Am. Chem. Soc., 126, 6429–6440.

    Google Scholar 

  • Kupče, E. and Freeman, R. (2004b) J. Biomol. NMR, 28, 391–395.

    Google Scholar 

  • Logan, T.M., Olejniczak, E.T., Xu, R.X. and Fesik, S.W. (1993) J. Biomol. NMR, 3, 225–231.

    Google Scholar 

  • McCoy, M.A. (1998) J. Magn. Reson., 130, 341–345.

    Google Scholar 

  • Palmer, A.G., Skelton, N.J., Chazin, W.J., Wright, P.E. and Rance, M. (1992) Mol. Phys., 75, 699–711.

    Google Scholar 

  • Patt, S.L. (1992) J. Magn. Reson., 96, 94–102.

    Google Scholar 

  • Peng, J.W. and Wagner, G. (1992) J. Magn. Reson., 98, 308–332.

    Google Scholar 

  • Pervushin, K., Riek, R., Wider, G. and Wüthrich, K. (1997) Proc. Natl. Acad. Sci. USA, 94, 12366–12371.

    Google Scholar 

  • Schleucher, J., Sattler, M. and Griesinger, C. (1993) Angew. Chem. Int. Ed. Engl., 32, 1489–1491.

    Google Scholar 

  • Tugarinov, V. and Kay, L.E. (2003) J. Mol. Biol., 327, 1121–1133.

    Google Scholar 

  • Tugarinov, V., Muhandiram, R., Ayed, A. and Kay, L.E. (2002) J. Am. Chem. Soc., 124, 10025–10035.

    Google Scholar 

  • Vuister, G.W. and Bax, A. (1992) J Magn. Reson., 98, 428–435.

    Google Scholar 

  • Yamazaki, T., Muhandiram, R. and Kay, L.E. (1994) J. Am. Chem. Soc., 116, 8266–8278.

    Google Scholar 

  • Yang, D. and Kay, L.E. (1999) J. Biomol. NMR, 13, 3–10.

    Google Scholar 

  • Zhang, O. and Forman-Kay, J.D. (1995) Biochemistry, 34, 6784–6794.

    Google Scholar 

  • Zhang, O., Forman-Kay, J.D., Shortle, D. and Kay, L.E. (1997) J. Biomol. NMR, 9, 181–200.

    Google Scholar 

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Tugarinov, V., Choy, WY., Kupče, E. et al. Addressing the overlap problem in the quantitative analysis of two dimensional NMR spectra: Application to 15N relaxation measurements. J Biomol NMR 30, 347–352 (2004). https://doi.org/10.1007/s10858-005-1549-y

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  • DOI: https://doi.org/10.1007/s10858-005-1549-y

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