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.
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Abbreviations
- IL-1:
-
interleukin-1
- IL-1β:
-
interleukin-1β
- IRAP:
-
interleukin-1 receptor antagonist protein
References
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.
Clore, G.M., Bax, A., Driscoll, P.C., Wingfield, P.T. and Gronenborn, A.M. (1990)Biochemistry,29, 8172–8184.
Dalgarno, D.C., Levine, B.A. and Williams, R.J.P. (1983)Bioscience Reports,3, 443–452.
Dinarello, C.A. (1991)Blood,77, 1627–1652.
Driscoll, P.C., Clore, G.M., Marion, D., Wingfield, P.T. and Gronenborn, A.M. (1990a)Biochemistry,29, 3542–3556.
Driscoll, P.C., Gronenborn, A.M., Wingfield, P.T. and Clore, G.M. (1990b)Biochemistry, 29, 4668–4682.
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.
Ikura, M., Kay, L.E. and Bax, A. (1990)Biochemistry,29, 4659–4667.
Pardi, A., Wagner, G. and Wüthrich, K. (1983)Eur. J. Biochem.,137, 445–454.
Pastore, A. and Saudek, V. (1990)J. Magn. Reson.,90, 165–176.
Richarz, R. and Wüthrich, K. (1978)Biopolymers,17, 2133–2141.
Spera, S. and Bax, A. (1991)J. AM. Chem. Soc.,113, 5490–5492.
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.
Williamson, M.P. (1990)Biopolymers,29, 1423–1431.
Wishart, D.S., Sykes, B.D. and Richards, F.M. (1991)J. Mol. Biol.,222, 311–333.
Wishart, D.S., Sykes, B.D. and Richards, F.M. (1992)Biochemistry,31, 1647–1651.
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Stockman, B.J., Scahill, T.A., Strakalaitis, N.A. et al. Proton, carbon, and nitrogen chemical shifts accurately delineate differences and similarities in secondary structure between the homologous proteins IRAP and IL-1β. J Biomol NMR 2, 591–596 (1992). https://doi.org/10.1007/BF02192848
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DOI: https://doi.org/10.1007/BF02192848