Skip to main content
SpringerLink
Log in

Phase labeling of C−H and C−C spin-system topologies: Application in constant-time PFG-CBCA(CO)NH experiments for discriminating amino acid spin-system types

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

Summary

Triple-resonance experiments facilitate the determination of sequence-specific resonance assignments of medium-sized 13C, 15N-enriched proteins. Some triple-resonance experiments can also be used to obtain information about amino acid spin-system topologies by proper delay tuning. The constant-time PFG-CBCA(CO)NH experiment allows discrimination between five different groups of amino acids by tuning (phase labeling) independently the delays for proton-carbon refocusing and carbon-carbon constant-time frequency labeling. The proton-carbon refocusing delay allows discrimination of spin-system topologies based on the number of protons attached to Cα and Cβ atoms (i.e. C-H phase labeling). In addition, tuning of the carbon-carbon constant-time frequency-labeling delay discriminates topologies based on the number of carbons directly coupled to Cα and Cβ atoms (i.e. C-C phase labeling). Classifying the spin systems into these five groups facilitates identification of amino acid types, making both manual and automated analysis of assignments easier. The use of this pair of optimally tuned PFG-CBCA(CO)NH experiments for distinguishing five spin-system topologies is demonstrated for the 124-residue bovine pancreatic ribonuclease A protein.

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

References

  • Bax, A. and Grzesiek, S. (1993) Acc. Chem. Res., 26, 131–138.

    Google Scholar 

  • Clore, G.M. and Gronenborn, A.M. (1991) Science, 252, 1390–1399.

    Google Scholar 

  • Clubb, R.T. and Wagner, G. (1992) J. Biomol. NMR, 2, 389–394.

    Google Scholar 

  • Dötsch, V., Oswald, R.E. and Wagner, G. (1996a) J. Magn. Reson., B 110, 304–308.

    Google Scholar 

  • Dötsch, V., Oswald, R.E. and Wagner, G. (1996b) J. Magn. Reson., B 110, 107–111.

    Google Scholar 

  • Dötsch, V. and Wagner, G. (1996) J. Magn. Reson., B 111, 310–313.

    Google Scholar 

  • FarmerII, B.T. and Venters, R.A. (1996) J. Biomol. NMR, 7, 59–71.

    Google Scholar 

  • Feng, W., Rios, C.B. and Montelione, G.T. (1996) J. Biomol. NMR, 8, 98–104.

    Google Scholar 

  • Friedrichs, M.S., Mueller, L. and Wittekind, M. (1994) J. Biomol. NMR, 4, 703–726.

    Google Scholar 

  • Gehring, K. and Guittet, E. (1995) J. Magn. Reson., B 109, 206–208.

    Google Scholar 

  • Grzesiek, S. and Bax, A. (1992a) J. Magn. Reson., 99, 201–207.

    Google Scholar 

  • Grzesiek, S. and Bax, A. (1992b) J. Am. Chem. Soc., 114, 6291–6293.

    Google Scholar 

  • Grzesiek, S., Anglister, J. and Bax, A. (1993) J. Magn. Reson., B 101, 114–119.

    Google Scholar 

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

    Google Scholar 

  • Ikura, M., Kay, L.E. and Bax, A. (1990) Biochemistry, 29, 4659–4667.

    Google Scholar 

  • Kay, L.E., Wittekind, M., McCoy, M., Friedrichs, M.S. and Mueller, L. (1992a) J. Magn. Reson., 98, 443–450.

    Google Scholar 

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

    Google Scholar 

  • Lyons, B.A. and Montelione, G.T. (1993) J. Magn. Reson., B 101, 206–209.

    Google Scholar 

  • Marion, D., Ikura, M., Tschudin, R. and Bax, A. (1989) J. Magn. Reson., 85, 393–399.

    Google Scholar 

  • McCoy, M.A. and Mueller, L. (1992) J. Am. Chem. Soc., 114, 2108–2112.

    Google Scholar 

  • Meadows, R.P., Olejniczak, E.T. and Fesik, S.W. (1994) J. Biomol. NMR, 4, 79–96.

    Google Scholar 

  • Montelione, G.T. and Wagner, G. (1989) J. Am. Chem. Soc., 111, 5474–5475.

    Google Scholar 

  • Montelione, G.T. and Wagner, G. (1990) J. Magn. Reson., 87, 183–188.

    Google Scholar 

  • Montelione, G.T., Lyons, B.A., Emerson, S.D. and Tashiro, M. (1992) J. Am. Chem. Soc., 114, 10974–10975.

    Google Scholar 

  • Morris, G.A. and Freeman, R. (1979) J. Am. Chem. Soc., 101, 760–761.

    Google Scholar 

  • Muhandiram, D.R. and Kay, L.E. (1994) J. Magn. Reson., B 103, 203–216.

    Google Scholar 

  • Olejniczak, E.T., Xu, R.X., Petros, A.M. and Fesik, S.W. (1992) J. Magn. Reson., 100, 444–450.

    Google Scholar 

  • Olejniczak, E.T. and Fesik, S.W. (1994) J. Am. Chem. Soc., 116, 2215–2216.

    Google Scholar 

  • PalmerIII, A.G., Fairbrother, W.J., Cavanagh, J., Wright, P. and Rance, M. (1992) J. Biomol. NMR, 2, 103–108.

    Google Scholar 

  • Powers, R., Gronenborn, A.M., Clore, G.M. and Bax, A. (1991) J. Magn. Reson., 94, 209–213.

    Google Scholar 

  • Santoro, J. and King, G.C. (1992) J. Magn. Reson., 97, 202–207.

    Google Scholar 

  • Shaka, A.J., Barker, P.B. and Freeman, R. (1985) J. Magn. Reson., 77, 274–293.

    Google Scholar 

  • Tashiro, M., Rios, C.B. and Montelione, G.T. (1995) J. Biomol. NMR, 6, 211–216.

    Google Scholar 

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

    Google Scholar 

  • Wishart, D.S., Bigam, C.G., Holm, A., Hodges, R.S. and Sykes, B.D. (1995) J. Biomol. NMR, 5, 67–81.

    Google Scholar 

  • Wittekind, M., Metzler, W.J. and Mueller, L. (1993) J. Magn. Reson., B 101, 214–217.

    Google Scholar 

  • Wüthrich, K. (1986) NMR of Proteins and Nucleic Acids, Wiley, New York, NY, U.S.A.

    Google Scholar 

  • Yamazaki, T., Forman-Kay, J.D. and Kay, L.E. (1993) J. Am. Chem. Soc., 115, 11054–11055.

    Google Scholar 

  • Yamazaki, T., Pascal, S.M., Singer, A.U., Forman-Kay, J.D. and Kay, L.E. (1995) J. Am. Chem. Soc., 117, 3556–3564.

    Google Scholar 

  • Zimmerman, D.E., Kulikowski, C., Wang, L., Lyons, B. and Montelione, G.T. (1994) J. Biomol. NMR, 4, 241–256.

    Google Scholar 

  • Zimmerman, D.E. and Montelione, G.T. (1995) Curr. Opin. Struct. Biol., 5, 664–673.

    Google Scholar 

Download references

Author information

Authors and Affiliations

  1. Center for Advanced Biotechnology and Medicine, Rutgers University, 08854-5638, Piscataway, NJ, USA

    Carlos B. Rios, Wenqing Feng, Mitsuru Tashiro, Zhigang Shang & Gaetano T. Montelione

  2. Department of Molecular Biology and Biochemistry, Rutgers University, 08854-5638, Piscataway, NJ, USA

    Carlos B. Rios, Wenqing Feng, Mitsuru Tashiro, Zhigang Shang & Gaetano T. Montelione

Authors
  1. Carlos B. Rios
    View author publications

    You can also search for this author in PubMed Google Scholar

  2. Wenqing Feng
    View author publications

    You can also search for this author in PubMed Google Scholar

  3. Mitsuru Tashiro
    View author publications

    You can also search for this author in PubMed Google Scholar

  4. Zhigang Shang
    View author publications

    You can also search for this author in PubMed Google Scholar

  5. Gaetano T. Montelione
    View author publications

    You can also search for this author in PubMed Google Scholar

Rights and permissions

Reprints and permissions

About this article

Cite this article

Rios, C.B., Feng, W., Tashiro, M. et al. Phase labeling of C−H and C−C spin-system topologies: Application in constant-time PFG-CBCA(CO)NH experiments for discriminating amino acid spin-system types. J Biomol NMR 8, 345–350 (1996). https://doi.org/10.1007/BF00410332

Download citation

  • Received:

  • Accepted:

  • Issue Date:

  • DOI: https://doi.org/10.1007/BF00410332

Keywords

Search

Navigation