Journal of Biomolecular NMR

, Volume 2, Issue 6, pp 591–596 | Cite as

Proton, carbon, and nitrogen chemical shifts accurately delineate differences and similarities in secondary structure between the homologous proteins IRAP and IL-1β

  • Brian J. Stockman
  • Terrence A. Scahill
  • Nancy A. Strakalaitis
  • David P. Brunner
  • Anthony W. Yem
  • Martin R. DeibelJr.
Article

Summary

1Hα,13Cα, and15Nα secondary chemical shifts, defined as the difference between the observed value and the random coil value, have been calculated for interleukin-1 receptor antagonist protein and interleukin-1β. Averaging of the secondary chemical shifts with those of adjacent residues was used to smooth out local effects and to obtain a correlation dependent on secondary structure. Differences and similarities in the placement of secondary structure elements in the primary segdences of these structurally homologous proteins are manifested in the smoothed secondary chemical shifts of all three types of nuclei. The close correlation observed between the secondary chemical shifts and the previously defined locations of secondary structure, as defined by traditional methods, exemplifies the advantage of chemical shifts to delineate regions of secondary structure.

Keywords

Interleukin-1β Interleukin-1 receptor antagonist protein Protein NMR spectroscopy Secondary chemical shift 

Abbreviations

IL-1

interleukin-1

IL-1β

interleukin-1β

IRAP

interleukin-1 receptor antagonist protein

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References

  1. Carter, D.B., Deibel Jr., M.R., Dunn, C.J., Tomich, C.-S.C., Laborde, A.L., Slightom, J.L., Berger, A.E., Bienkowski, M.J., Sun, F.F., McEwan, R.N., Harris, P.K.W., Yem, A.Y., Waszak, G.A., Chosay, J.G., Sieu, L.C., Hardee, M.M., Zurcher-Neely, H.A., Reardon, I.M., Heinrikson, R.L., Truesdell, S.E., Shelly, J.A., Eessalu, T.E., Taylor, B.M. and Tracey, D.E. (1990)Nature,344, 633–638.PubMedGoogle Scholar
  2. Clore, G.M., Bax, A., Driscoll, P.C., Wingfield, P.T. and Gronenborn, A.M. (1990)Biochemistry,29, 8172–8184.PubMedGoogle Scholar
  3. Dalgarno, D.C., Levine, B.A. and Williams, R.J.P. (1983)Bioscience Reports,3, 443–452.PubMedGoogle Scholar
  4. Dinarello, C.A. (1991)Blood,77, 1627–1652.PubMedGoogle Scholar
  5. Driscoll, P.C., Clore, G.M., Marion, D., Wingfield, P.T. and Gronenborn, A.M. (1990a)Biochemistry,29, 3542–3556.PubMedGoogle Scholar
  6. Driscoll, P.C., Gronenborn, A.M., Wingfield, P.T. and Clore, G.M. (1990b)Biochemistry, 29, 4668–4682.PubMedGoogle Scholar
  7. Eisenberg, S.P., Evans, R.J., Arend, W.P., Verderber, E., Brewer, M.T., Hannum, C.H. and Thompson, R.C. (1990)Nature,343, 341–346.PubMedGoogle Scholar
  8. Ikura, M., Kay, L.E. and Bax, A. (1990)Biochemistry,29, 4659–4667.PubMedGoogle Scholar
  9. Pardi, A., Wagner, G. and Wüthrich, K. (1983)Eur. J. Biochem.,137, 445–454.PubMedGoogle Scholar
  10. Pastore, A. and Saudek, V. (1990)J. Magn. Reson.,90, 165–176.Google Scholar
  11. Richarz, R. and Wüthrich, K. (1978)Biopolymers,17, 2133–2141.Google Scholar
  12. Spera, S. and Bax, A. (1991)J. AM. Chem. Soc.,113, 5490–5492.Google Scholar
  13. Stockman, B.J., Scahill, T.A., Roy, M., Ulrich, E.L., Strakalaitis, N.A., Brunner, D.P., Yem, A.W. and Deibel Jr., M.R., (1992)Biochemistry,31, 5237–5245.PubMedGoogle Scholar
  14. Williamson, M.P. (1990)Biopolymers,29, 1423–1431.PubMedGoogle Scholar
  15. Wishart, D.S., Sykes, B.D. and Richards, F.M. (1991)J. Mol. Biol.,222, 311–333.PubMedGoogle Scholar
  16. Wishart, D.S., Sykes, B.D. and Richards, F.M. (1992)Biochemistry,31, 1647–1651.PubMedGoogle Scholar

Copyright information

© ESCOM Science Publishers B.V. 1992

Authors and Affiliations

  • Brian J. Stockman
    • 1
  • Terrence A. Scahill
    • 1
  • Nancy A. Strakalaitis
    • 2
  • David P. Brunner
    • 2
  • Anthony W. Yem
    • 1
  • Martin R. DeibelJr.
    • 1
  1. 1.Upjohn LaboratoriesThe Upjohn CompanyKalamazooUSA
  2. 2.Chemical DivisionThe Upjohn CompanyKalamazooUSA

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