Skip to main content
SpringerLink
Log in

Methods for sequential resonance assignment in solid, uniformly 13C, 15N labelled peptides: Quantification and application to antamanide

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

Abstract

The application of adiabatic polarization-transfer experiments to resonance assignment in solid, uniformly 13C-15N-labelled polypeptides is demonstrated for the cyclic decapeptide antamanide. A homonuclear correlation experiment employing the DREAM sequence for adiabatic dipolar transfer yields a complete assignment of the Cα and aliphatic side-chain 13C resonances to amino acid types. The same information can be obtained from a TOBSY experiment using the recently introduced P91 12 TOBSY sequence, which employs the J couplings as a transfer mechanism. A comparison of the two methods is presented. Except for some aromatic phenylalanine resonances, a complete sequence-specific assignment of the 13C and 15N resonances in antamanide is achieved by a series of selective or broadband adiabatic triple-resonance experiments. Heteronuclear transfer by adiabatic-passage Hartmann–Hahn cross polarization is combined with adiabatic homonuclear transfer by the DREAM and rotational-resonance tickling sequences into two- and three-dimensional experiments. The performance of these experiments is evaluated quantitatively.

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

  • Baldus, M. (1996) Structural information from high-resolution solid-state NMR: Methodological improvements, Ph.D. Thesis, ETH Zürich, Diss. No. 11847.

  • Baldus, M., Geurts, D.G., Hediger, S. and Meier, B.H. (1996) J. Magn. Reson., A118, 140-144.

    Google Scholar 

  • Baldus, M. and Meier, B.H. (1996) J. Magn. Reson., A121, 65-69.

    Google Scholar 

  • Baldus, M., Petkova, A.T., Herzfeld, J. and Griffin, R.G. (1998) Mol. Phys., 95, 1197-1207.

    Google Scholar 

  • Bennett, A.E., Rienstra, C.M., Auger, M., Lakshmi, K.V. and Griffin, R.G. (1995) J. Chem. Phys., 103, 6951-6958.

    Google Scholar 

  • Braunschweiler, L. and Ernst, R.R. (1983) J. Magn. Reson., 53, 512-528.

    Google Scholar 

  • Bystrov, V.F. (1976) Prog. NMR Spectrosc., 10, 41-81.

    Google Scholar 

  • Costa, P.R., Sun, B.Q. and Griffin, R.G. (1997) J. Am. Chem. Soc., 119, 10821-10830.

    Google Scholar 

  • Ernst, M. (1993) Untersuchungen zur Dynamik von Peptiden und Proteinen mit NMR-Relaxationsmethoden, Ph.D. Thesis, ETH Zürich, Diss. No. 10390.

  • Fesik, S.W., Eaton, H.L., Olejniczak, E.T. and Zuiderweg, E.R.P. (1990) J. Am. Chem. Soc., 112, 886-888.

    Google Scholar 

  • Garwood, M. and Ke, Y. (1991) J. Magn. Reson., 94, 511-525.

    Google Scholar 

  • Griffin, R.G. (1998) Nat. Struct. Biol., 5 (supplement), 508-512.

    Google Scholar 

  • Grimmer, A.R., Kretschmer, A. and Cajipe, V.B. (1997) Magn. Reson. Chem., 35, 86-90.

    Google Scholar 

  • Hardy, E.H., Verel, R. and Meier, B.H. (2001) J. Magn. Reson., 148, 459-464.

    Google Scholar 

  • Hediger, S., Meier, B.H. and Ernst, R.R. (1995) Chem. Phys. Lett., 240, 449-456.

    Google Scholar 

  • Hediger, S., Meier, B.H., Kurur, N.D., Bodenhausen, G. and Ernst, R.R. (1994) Chem. Phys. Lett., 223, 283-288.

    Google Scholar 

  • Hohwy, M., Jakobsen, H.J., Eden, M., Levitt, M.H. and Nielsen, N.C. (1998) J. Chem. Phys., 108, 2686-2694.

    Google Scholar 

  • Hong, M. (1999) J. Biomol. NMR, 15, 1-14.

    Google Scholar 

  • Hu, J.S. and Bax, A. (1997) J. Am. Chem. Soc., 119, 6360-6368.

    Google Scholar 

  • Hwang, T., van Zijl, P.C.M. and Garwood, M. (1998) J. Magn. Reson., 133, 200-203.

    Google Scholar 

  • Kao, L. and Barfield, M. (1985) J. Am. Chem. Soc., 107, 2323-2330.

    Google Scholar 

  • Karle, I.L., Wieland, T., Schermer, D. and Ottenheym, H.C.J. (1979) Proc. Natl. Acad. Sci. USA, 76, 1532-1536.

    Google Scholar 

  • Kessler, H., Bats, J.W., Lautz, J. and Muller, A. (1989a) Liebigs Ann. Chem., 913-928.

  • Kessler, H., Muller, A. and Pook, K.H. (1989b) Liebigs Ann. Chem., 903-912.

  • Langer, B., Schnell, I., Spiess, H.W. and Grimmer, A.R. (1999) J. Magn. Reson., 138, 182-186.

    Google Scholar 

  • Lee, M. and Goldburg, W.I. (1965) Phys. Rev., 140, A1261-1271.

    Google Scholar 

  • Live, D.H., Davis, D.G., Agosta, W.C. and Cowburn, D. (1984) J. Am. Chem. Soc., 106, 1939-1943.

    Google Scholar 

  • Marion, D. and Wüthrich, K. (1983) Biochem. Biophys. Res. Commun., 113, 967-974.

    Google Scholar 

  • McDermott, A., Polenova, T., Bockmann, A., Zilm, K.W., Paulson, E.K., Martin, R.W. and Montelione, G.T. (2000) J. Biomol. NMR, 16, 209-219.

    Google Scholar 

  • Meier, B.H. and Earl, W.L. (1987) J. Am. Chem. Soc., 109, 7937-7942.

    Google Scholar 

  • Nakai, T. and McDowell, C.A. (1992) Mol. Phys., 77, 569-584.

    Google Scholar 

  • Pauli, J., Baldus, M., van Rossum, B., de Groot, H. and Oschkinat, H. (2001) Chem. BioChem., 2, 272-281.

    Google Scholar 

  • Pauli, J., van Rossum, B., Forster, H., de Groot, H.J.M. and Oschkinat, H. (2000) J. Magn. Reson., 143, 411-416.

    Google Scholar 

  • Rienstra, C.M., Hohwy, M., Hong, M. and Griffin, R.G. (2000) J. Am. Chem. Soc., 122, 10979-10990.

    Google Scholar 

  • Sakakibara, S., Shimonishi, Y., Kishida, Y., Okada, M. and Sugihara, H. (1967) Bull. Chem. Soc. Jpn., 40, 2164-2167.

    Google Scholar 

  • Schnolzer, M., Alewood, P., Jones, A., Alewood, D. and Kent, S.B. (1992) Int. J. Pept. Protein Res., 40, 180-193.

    Google Scholar 

  • Sø rensen, O.W. (1990) J. Magn. Reson., 86, 435-440.

    Google Scholar 

  • Straus, S.K., Bremi, T. and Ernst, R.R. (1997) J. Biomol. NMR, 10, 119-128.

    Google Scholar 

  • Sun, B.Q., Rienstra, C.M., Costa, P.R., Williamson, J.R. and Griffin, R.G. (1997) J. Am. Chem. Soc., 119, 8540-8546.

    Google Scholar 

  • Takegoshi, K., Nomura, K. and Terao, T. (1995) Chem. Phys. Lett., 232, 424-428.

    Google Scholar 

  • Takegoshi, K., Nomura, K. and Terao, T. (1997) J. Magn. Reson., 127, 206-216.

    Google Scholar 

  • Tycko, R. (1996) J. Biomol. NMR, 8, 239-251.

    Google Scholar 

  • Verel, R., Baldus, M., Ernst, M. and Meier, B.H. (1998) Chem. Phys. Lett., 287, 421-428.

    Google Scholar 

  • Verel, R., Baldus, M., Nijman, M., Vanos, J.W.M. and Meier, B.H. (1997) Chem. Phys. Lett., 280, 31-39.

    Google Scholar 

  • Verel, R., Ernst, M. and Meier, B.H. (2001) J. Magn. Reson., 150, 81-99.

    Google Scholar 

  • Wieland, T. (1968) Angew. Chem. Int. Ed. Engl., 7, 204-208.

    Google Scholar 

  • Wieland, T. and Faulstich, H. (1978) Crit. Rev. Biochem., 5, 185-260.

    Google Scholar 

  • Zhang, S., Meier, B.H. and Ernst, R.R. (1994) J. Magn. Reson., A108, 30-37.

    Google Scholar 

Download references

Author information

Authors and Affiliations

  1. Laboratory of Physical Chemistry, ETH Hönggerberg, CH-8093, Zürich, Switzerland

    Andreas Detken, Edme H. Hardy, Matthias Ernst & Beat H. Meier

  2. CREST, Japan Science and Technology Corporation, Tokyo Metropolitan University, 1-1 Minami-ohsawa, Hachioji, Tokyo, 192-0397, Japan

    Masatsune Kainosho

  3. Institute for Protein Research, Osaka University, 3-2 Yamadaoka, Suita, Osaka, 565-0871, Japan

    Toru Kawakami & Saburo Aimoto

Authors
  1. Andreas Detken
    View author publications

    You can also search for this author in PubMed Google Scholar

  2. Edme H. Hardy
    View author publications

    You can also search for this author in PubMed Google Scholar

  3. Matthias Ernst
    View author publications

    You can also search for this author in PubMed Google Scholar

  4. Masatsune Kainosho
    View author publications

    You can also search for this author in PubMed Google Scholar

  5. Toru Kawakami
    View author publications

    You can also search for this author in PubMed Google Scholar

  6. Saburo Aimoto
    View author publications

    You can also search for this author in PubMed Google Scholar

  7. Beat H. Meier
    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

Detken, A., Hardy, E.H., Ernst, M. et al. Methods for sequential resonance assignment in solid, uniformly 13C, 15N labelled peptides: Quantification and application to antamanide. J Biomol NMR 20, 203–221 (2001). https://doi.org/10.1023/A:1011212100630

Download citation

  • Issue Date:

  • DOI: https://doi.org/10.1023/A:1011212100630

Search

Navigation