Skip to main content
SpringerLink
Log in

Direct measurement of the 15N CSA/dipolar relaxation interference from coupled HSQC spectra

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

Abstract

Here we propose a method for the measurement of the 15N CSA/dipolar relaxation interference based on direct comparison of the 15N doublet components observed in a 1H-coupled 1H-15N HSQC-type spectrum. This allows the determination of the cross-correlation rates with no need for correction factors associated with other methods. The signal overlap problem of coupled HSQC spectra is addressed here by using the IPAP scheme (Ottiger et al., 1998). The approach is applied to the B3 domain of protein G to show that the method provides accurate measurements of the 15N CSA/dipolar cross-correlation rates.

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

Access this article

Log in via an institution

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

Instant access to the full article PDF.

Institutional subscriptions

Similar content being viewed by others

References

  • Bartels, C., Xia, T., Guntert, P., Billeter, M. and Wüthrich, K. (1995) J. Biomol. NMR, 5, 1-10.

    Google Scholar 

  • Boisbouvier, J., Brutscher, B., Simorre, J.-P. and Marion, D. (1999) J. Biomol. NMR, 14, 241-252.

    Google Scholar 

  • Brutscher, B. (2000) Concepts Magn. Reson., 12, 207-229.

    Google Scholar 

  • Dayie, K.T., Brodsky, A.S. and Williamson, J.R. (2002) J. Mol. Biol., 317, 263-278.

    Google Scholar 

  • Fushman, D. and Cowburn, D. (1998) J. Am. Chem. Soc., 120, 7109-7110.

    Google Scholar 

  • Fushman, D. and Cowburn, D. (2001) In Methods in Enzymology, Vol. 339, James, T., Schmitz, U. and Doetsch, V., Eds., pp. 109-126.

  • Fushman, D., Cahill, S. and Cowburn, D. (1997) J. Mol. Biol., 266, 173-194.

    Google Scholar 

  • Fushman, D., Tjandra, N. and Cowburn, D. (1998) J. Am. Chem. Soc., 120, 10947-10952.

    Google Scholar 

  • Fushman, D., Tjandra, N. and Cowburn, D. (1999) J. Am. Chem. Soc., 121, 8577-8582.

    Google Scholar 

  • Ghose, R. and Prestegard, J.H. (1998) J. Magn. Reson., 134, 308-314.

    Google Scholar 

  • Goldman, M. (1984) J. Magn.Reson., 60, 437-452.

    Google Scholar 

  • Hiyama, Y., Niu, C., Silverton, J., Bavoso, A. and Torchia, D. (1988) J. Am. Chem. Soc., 110, 2378-2383.

    Google Scholar 

  • Kroenke, C.D., Loria, J.P., Lee, L.K., Rance, M. and Palmer, A.G.I. (1998) J. Am. Chem. Soc., 120, 7905-7915.

    Google Scholar 

  • Oas, T.G., Hartzell, C.J., Dahlquist, F.W. and Drobny, G.P. (1987) J. Am. Chem. Soc., 109, 5962-5966.

    Google Scholar 

  • Ottiger, M., Delaglio, F. and Bax, A. (1998) J. Magn. Reson., 131, 373-378.

    Google Scholar 

  • Pang, Y. and Zuiderweg, E.R. (2000) J. Am. Chem. Soc., 122, 4841-4842.

    Google Scholar 

  • Press, W.H., Teukolsky, S.A., Vetterling, W.T. and Flannery, B.P. (1992) Numerical Recipes in C, Cambridge University Press, New York, NY.

    Google Scholar 

  • Schwalbe, H., Carlomagno, T., Hennig, M., Junker, J., Reif, B., Richter, C. and Griesinger, C. (2001) Meth. Enzymol., 338, 35-81.

    Google Scholar 

  • Tessari, M., Mulder, F.A.A., Boelens, R. and Vuister, G.W. (1997a) J. Mag. Reson., 127, 128-123.

    Google Scholar 

  • Tessari, M., Vis, H., Boelens, R., Kaptein, R. and Vuister, G.W. (1997b) J. Am. Chem. Soc., 119, 8985-8990.

    Google Scholar 

  • Tjandra, N. and Bax, A. (1997) J. Am. Chem. Soc., 119, 8076-8082.

    Google Scholar 

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

    Google Scholar 

  • Yang, D., Konrat, R. and Kay, L.E. (1997) J. Amer. Chem. Soc., 119, 11938-11940.

    Google Scholar 

Download references

Author information

Authors and Affiliations

  1. Department of Chemistry and Biochemistry, Center of Biomolecular Structure and Organization, University of Maryland, 1115 Agriculture/Life Science Surge Bldg., College Park, MD,  20742-3360, U.S.A

    Jennifer B. Hall & David Fushman

  2. Department of Molecular Biology, Center for Structural Biology, Lerner Research Institute, Cleveland Clinic Foundation, Cleveland, OH,  44195, U.S.A

    Kwaku T. Dayie

Authors
  1. Jennifer B. Hall
    View author publications

    You can also search for this author in PubMed Google Scholar

  2. Kwaku T. Dayie
    View author publications

    You can also search for this author in PubMed Google Scholar

  3. David Fushman
    View author publications

    You can also search for this author in PubMed Google Scholar

Corresponding author

Correspondence to David Fushman.

Rights and permissions

Reprints and permissions

About this article

Cite this article

Hall, J.B., Dayie, K.T. & Fushman, D. Direct measurement of the 15N CSA/dipolar relaxation interference from coupled HSQC spectra. J Biomol NMR 26, 181–186 (2003). https://doi.org/10.1023/A:1023546107553

Download citation

  • Issue Date:

  • DOI: https://doi.org/10.1023/A:1023546107553

Search

Navigation