Skip to main content
SpringerLink
Log in

1H and 15N resonance assignments and secondary structure of the carbon monoxide complex of sperm whale myoglobin

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

Summary

Sequence-specific backbone 1H and 15N resonance assignments have been made for 95% of the amino acids in sperm whale myoglobin, complexed with carbon monoxide (MbCO). Many assignments for side-chain resonances have also been obtained. Assignments were made by analysis of an extensive series of homonuclear 2D spectra, measured with unlabeled protein, and both 2D and 3D 1H-15N-correlated spectra obtained from uniformly 15N-labeled myoglobin. Patterns of medium-range NOE connectivities indicate the presence of eight helices in positions that are very similar to those found in the crystal structures of sperm whale myoglobin. The resonance assignments of MbCO form the basis for determination of the solution structure and for hydrogen-exchange measurements to probe the stability and folding pathways of myoglobin. They will also form a basis for assignment of the spectra of single-site mutants with altered ligand-binding properties.

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

  • Balasubramanian, S., Lambright, D.G., Marden, M.C. and Boxer, S.G. (1993) Biochemistry, 32, 2202–2212.

    Google Scholar 

  • Bax, A. and Subramanian, S. (1986) J. Magn. Reson., 67, 565–569.

    Google Scholar 

  • Bax, A., Ikura, M., Kay, L.E., Torchia, D.A. and Tschudin, R. (1990) J. Magn. Reson, 86, 304–318.

    Google Scholar 

  • Billeter, M., Braun, W. and Wüthrich, K. (1982) J. Mol. Biol., 155, 321–346.

    Google Scholar 

  • Brantley Jr., R.E., Smerdon, S.J., Wilkinson, A.J., Singleton, E.W. and Olson, J.S. (1993) J. Biol. Chem., 268, 6995–7010.

    Google Scholar 

  • Braunschweiler, L., Bodenhausen, G. and Ernst, R.R. (1983) Mol. Phys., 48, 535–560.

    Google Scholar 

  • Braunstein, D., Ansari, A., Berendzen, J., Cowen, B.R., Egeberg, K.D., Frauenfelder, H., Hong, M.K., Ormos, P., Sauke, T.B., Scholl, R., Schulte, A., Sligar, S.G., Springer, B.A., Steinbach, P.J. and Young, R.D. (1988) Proc. Natl. Acad. Sci. USA 85, 8497–8501.

    Google Scholar 

  • Carver, T.E., Brantley Jr., R.E., Singleton, E.W., Arduini, R.M., Quillin, M.L., Phillips Jr., G.N. and Olson, J.S. (1992) J. Biol. Chem. 267, 14443–14450.

    Google Scholar 

  • Case, D.A. and Karplus, M. (1979) J. Mol. Biol., 132, 343–368.

    Google Scholar 

  • Chazin, W.J., Rance, M. and Wright, P.E. (1988) J. Mol. Biol., 202, 603–622.

    Google Scholar 

  • Chiu, M.L. (1992) Ph.D. Thesis, University of Illinois, Urbana-Champaign, IL.

    Google Scholar 

  • Dalvit, C., Rance, M. and Wright, P.E. (1986) J. Magn. Reson, 69, 356–361.

    Google Scholar 

  • Dalvit, C. and Wright, P.E. (1987) J. Mol. Biol., 194, 313–327.

    Google Scholar 

  • Dalvit, C., Wright, P.E. and Rance, M. (1987) J. Magn. Reson, 71, 539–543.

    Google Scholar 

  • Davis, D.G. (1989) J. Magn. Reson., 81, 603–607.

    Google Scholar 

  • Dodson, G., Hubbard, R.E., Oldfield, T.J., Smerdon, S.J. and Wilkinson, A.J. (1988) Protein Eng., 2, 233–237.

    Google Scholar 

  • Driscoll, P.C., Clore, G.M., Marion, D., Wingfield, P.T. and Gronenborn, A.M. (1990) Biochemistry, 29, 3542–3556.

    Google Scholar 

  • Drobny, G., Pines, A., Sinton, S., Weitekamp, D. and Wemmer, D. (1979) Symp. Faraday Soc., 13, 49–55.

    Google Scholar 

  • Elber, R. and Karplus, M. (1987) Science, 235, 318–321.

    Google Scholar 

  • Fesik, S.W. and Zuiderweg, E.R.P. (1990) Q. Rev. Biophys., 23, 97–131.

    Google Scholar 

  • Frauenfelder, H., Petsko, G.A. and Tsernoglou, D. (1979) Nature, 280, 558–563.

    Google Scholar 

  • Gibson, Q.H., Regan, R., Elber, R., Olson, J.S. and Carver, T.E. (1992) J. Biol. Chem., 267, 22022–22034.

    Google Scholar 

  • Guillemette, J.G., Matsushima-Hibiya, Y., Atkinson, T. and Smith, M. (1991) Protein Eng., 4, 585–592.

    Google Scholar 

  • Hanson, J.C. and Schoenborn, B.P. (1981) J. Mol. Biol., 153, 117–146.

    Google Scholar 

  • Hartmann, H., Parak, F., Steigemann, W., Petsko, G.A., Ponzi, D.R. and Frauenfelder, H. (1982) Proc. Natl. Acad. Sci. USA, 79, 4967–4971.

    Google Scholar 

  • Henry, E.R. (1993) Biophys. J., 64, 869–885.

    Google Scholar 

  • Jennings, P.A. and Wright, P.E. (1993) Science, 262, 892–896.

    Google Scholar 

  • Kottalam, J. and Case, D.A. (1988) J. Am. Chem. Soc., 110, 7690–7697.

    Google Scholar 

  • Kumar, A., Ernst, R.R. and Wüthrich, K. (1980) Biochem. Biophys. Res. Commun., 95, 1–6.

    Google Scholar 

  • Kuriyan, J., Wilz, S., Karplus, M. and Petsko, G.A. (1986) J. Mol. Biol., 192, 133–154.

    Google Scholar 

  • Lambright, D.G., Balasubramanian, S. and Boxer, S.G. (1989) J. Mol. Biol., 207, 289–299.

    Google Scholar 

  • Levy, R.M., Sheridan, R.P., Keepers, J.W., Dubey, G.S., Swaminathan, S. and Karplus, M. (1985) Biophys. J., 48, 509–518.

    Google Scholar 

  • Live, D.H., Davis, D.G., Agosta, W.C. and Cowburn, D. (1984) J. Am. Chem. Soc., 106, 1939–1941.

    Google Scholar 

  • Mabbutt, B.C. and Wright, P.E. (1985) Biochim. Biophys. Acta, 832, 175–185.

    Google Scholar 

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

    Google Scholar 

  • Marion, D., Driscoll, P.C., Kay, L.E., Wingfield, P.T., Bax, A., Gronenborn, A.M. and Clore, G.M. (1989a) Biochemistry, 28, 6150–6156.

    Google Scholar 

  • Marion, D., Kay, L.E., Sparks, S.W., Torchia, D.A. and Bax, A. (1989b) J. Am. Chem. Soc., 111, 1515–1517.

    Google Scholar 

  • Norwood, T.J., Boyd, J., Heritage, J.E., Soffe, N. and Campbell, I.D. (1990) J. Magn. Reson., 87, 488–501.

    Google Scholar 

  • Phillips Jr., G.N. (1990) Biophys. J., 57, 381–383.

    Google Scholar 

  • Phillips Jr., G.N., Arduini, R.M., Springer, B.A. and Sligar, S.G. (1990) Proteins, 7, 358–365.

    Google Scholar 

  • Phillips, S.E.V. (1980) J. Mol. Biol., 142, 531–554.

    Google Scholar 

  • Phillips, S.E.V. and Schoenborn, B.P. (1981) Nature, 292, 81–82.

    Google Scholar 

  • Rance, M. and Byrd, R.A. (1983) J. Magn. Reson., 52, 221–240.

    Google Scholar 

  • Rance, M., Sørensen, O.W., Bodenhausen, G., Wagner, G., Ernst, R.R. and Wüthrich, K. (1983) Biochem. Biophys. Res. Commun., 117, 479–485.

    Google Scholar 

  • Rance, M. and Wright, P.E. (1986) J. Magn. Reson., 66, 372–378.

    Google Scholar 

  • Rance, M., Chazin, W.J., Dalvit, C. and Wright, P.E. (1989) Methods Enzymol., 176, 114–133.

    Google Scholar 

  • Schoenborn, B.P. (1971) Cold Spring Harbor Symp. Quant. Biol., 36, 569–575.

    Google Scholar 

  • Shaka, A.J., Barker, P.B. and Freeman, R. (1985) J. Magn. Reson., 64, 547–552.

    Google Scholar 

  • Shaka, A.J., Lee, C.J. and Pines, A. (1988) J. Magn. Reson., 77, 274–293.

    Google Scholar 

  • Springer, B.A. and Sligar, S.G. (1987) Proc. Natl. Acad. Sci. USA, 84, 8961–8965.

    Google Scholar 

  • Takano, T. (1977a) J. Mol. Biol., 110, 537–568.

    Google Scholar 

  • Takano, T. (1977b) J. Mol. Biol., 110, 569–584.

    Google Scholar 

  • Varadarajan, R., Szabo, A. and Boxer, S.G. (1989) Proc. Natl. Acad. Sci. USA, 82, 5681–5684.

    Google Scholar 

  • Varadarajan, R., Lambright, D.G. and Boxer, S.G. (1989) Biochemistry, 28, 3771–3781.

    Google Scholar 

  • Wagner, G. (1983) J. Magn. Reson., 55, 151–156.

    Google Scholar 

Download references

Author information

Author notes

  1. Yves Thériault

    Present address: Ontogen Corporation, 92009, Carlsbad, CA, U.S.A.

  2. Thomas C. Pochapsky

    Present address: Department of Chemistry, Brandeis University, 02254, Waltham, MA, U.S.A.

  3. Claudio Dalvit

    Present address: Sandoz Pharma, CH-4002, Basel, Switzerland

Authors and Affiliations

  1. Department of Molecular Biology, The Scripps Research Institute, 92037, La Jolla, CA, U.S.A.

    Yves Thériault, Thomas C. Pochapsky, Claudio Dalvit & Peter E. Wright

  2. Department of Biochemistry and Chemistry, University of Illinois, 61801, Urbana, IL, U.S.A.

    Mark L. Chiu & Stephen G. Sligar

Authors
  1. Yves Thériault
    View author publications

    You can also search for this author in PubMed Google Scholar

  2. Thomas C. Pochapsky
    View author publications

    You can also search for this author in PubMed Google Scholar

  3. Claudio Dalvit
    View author publications

    You can also search for this author in PubMed Google Scholar

  4. Mark L. Chiu
    View author publications

    You can also search for this author in PubMed Google Scholar

  5. Stephen G. Sligar
    View author publications

    You can also search for this author in PubMed Google Scholar

  6. Peter E. Wright
    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

Thériault, Y., Pochapsky, T.C., Dalvit, C. et al. 1H and 15N resonance assignments and secondary structure of the carbon monoxide complex of sperm whale myoglobin. J Biomol NMR 4, 491–504 (1994). https://doi.org/10.1007/BF00156616

Download citation

  • Received:

  • Accepted:

  • Issue Date:

  • DOI: https://doi.org/10.1007/BF00156616

Key words

Search

Navigation