Partial NMR assignments for uniformly (13C, 15N)-enriched BPTI in the solid state

Journal of Biomolecular NMR - Tập 16 - Trang 209-219 - 2000
Ann McDermott1, Tatyana Polenova1, Anja Bockmann1, Kurt.W. Zilm2, Eric K. Paulsen2, Rachel W. Martin2, Gaetano T. Montelione3
1Department of Chemistry, Columbia University, New York, U.S.A.
2Department of Chemistry, Yale University, New Haven, U.S.A
3Center for Advanced Biotechnology and Medicine, Rutgers University, Piscataway, U.S.A.

Tóm tắt

We demonstrate that high-resolution multidimensional solid state NMR methods can be used to correlate many backbone and side chain chemical shifts for hydrated micro-crystalline U-13C,15N Basic Pancreatic Trypsin Inhibitor (BPTI), using a field strength of 800 MHz for protons, magic angle sample spinning rates of 20 kHz and proton decoupling field strengths of 140 kHz. Results from two homonuclear transfer methods, radio frequency driven dipolar recoupling and spin diffusion, were compared. Typical 13C peak line widths are 0.5 ppm, resulting in Cα-Cβ and Cα-CO regions that exhibit many resolved peaks. Two-dimensional carbon–carbon correlation spectra of BPTI have sufficient resolution to identify and correlate many of the spin systems associated with the amino acids. As a result, we have been able to assign a large number of the spin systems in this protein. The agreement between shifts measured in the solid state and those in solution is typically very good, although some shifts near the ion binding sites differ by at least 1.5 ppm. These studies were conducted with approximately 0.2 to 0.4 μmol of enriched material; the sensitivity of this method is apparently adequate for other biological systems as well.

Từ khóa


Tài liệu tham khảo

Baldus, M., Geurts, D.G., Hediger, S. and Meier, B.H. (1996) J. Magn. Reson., A 118, 140–144.

Baldus, M. and Meier, B.H. (1996) J. Magn. Reson., A 121, 65–69.

Baldus, M., Geurts, D.G. and Meier, B.H. (1998a) SSNMR, 11, 157–168.

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

Baldus, M., Tomaselli, M., Meier, B.H. and Ernst, R.R. (1994) Chem. Phys. Lett., 230, 329–336.

Bennett, A.E., Ok, J.H., Griffin, R.G. and Vega, S. (1992) J. Chem. Phys., 96, 8624–8627.

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

Bennett, A.E., Rienstra, C.M., Griffiths, J.M., Zhen, W.G., Lansbury, P.T. and Griffin, R.G. (1998) J. Chem. Phys., 108, 9463–9479.

Benzinger, T.L.S., Gregory, D.M., Burkoth, T.S., Miller-Auer, H., Lynn, D.G., Botto, R.E. and Meredith, S.C. (1998) Proc. Natl. Acad. Sci. USA, 95, 13407–13412.

Clore, G.M. and Gronenborn, A.M. (1994) Methods Enzymol., 239, 349–363.

Cole, H.B.R. and Torchia, D.A. (1991) Chem. Phys., 158, 278–281.

de Dios, A.C., Pearson, J.G. and Oldfield, E. (1993) Science, 260, 1491–1495.

Feng, X., Verdegem, P.J.E., Lee, Y.K., Sandström, D., Edén, M., Bovee-Geurts, P., de Grip, W.J., Lugtenburg, J., de Groot, H.J.M. and Levitt, M.H. (1997) J. Am. Chem. Soc., 119, 6853–6857.

Fujiwara, T., Sugase, K., Kainosho, M., Ono, A., Ono, A.M. and Akutsu, H. (1995) J. Am. Chem. Soc., 117, 11351–11352.

Gregory, D.M., Mitchell, D.J., Stringer, J.A., Kiihne, S., Shiels, J.C., Callahan, J., Mehta, M.A. and Drobny, G.P. (1995) Chem. Phys. Lett., 246, 654–663.

Griffin, R.G. (1998) Nat. Struct. Biol., 5, 508–512 S.

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

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

Hediger, S., Signer, P., Tomaselli, M., Ernst, R.R. and Meier, B.H. (1997) J. Magn. Reson., 125, 291–301.

Hing, A.W., Vega, S. and Schaefer, J. (1992) J. Magn. Reson., 96, 205–209.

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

Hohwy, M., Rienstra, C.M., Jaroniec, C.P. and Griffin, R.G. (1999) J. Chem. Phys., 110, 7983–7992.

Hong, M., 1999 ENC Conference Abstract, Orlando, FL, M & T Poster #73.

Hong, M. and Griffin, R.G. (1998) J. Am. Chem. Soc., 120, 7113–7114.

Jansson, M., Li, Y.C., Jendeberg, L., Anderson, S., Montelione, G.L. and Nilsson, B. (1996) J. Biomol. NMR, 7, 131–141.

Kay, L.E., Ikura, M., Tschudin, R. and Bax, A. (1990) J. Magn. Reson., 89, 496–514.

Ketchum, R.R., Hu, W. and Cross, T.A. (1993) Science, 261, 1457–1460.

Lansbury, P.T. Jr., Costa, P.R., Griffiths, J.M., Simon, E.J., Auger, M., Halverson, K.J., Kocisko, D.A., Hendsch, Z.S., Ashburn, T.T., Spencer, R.G.S., Tidor, B. and Griffin, R.G. (1995) Nat. Struct. Biol., 2, 990–998.

Lee, Y.K., Kurur, N.D., Helmle, M., Johannessen, O.G., Nielsen, N.C. and Levitt, M.H. (1995) Chem. Phys. Lett., 242, 304–309.

Long, J.R., Sun, B.Q., Bowen, A. and Griffin, R.G. (1994) J. Am. Chem. Soc., 116, 11950–11956.

Marassi, F.M., Ramamoorthy, A. and Opella, S.J. (1997) Proc. Natl. Acad. Sci. USA, 94, 8551–8556.

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

McDowell, L.M., Klug, C.A., Beusen, D.D. and Schaefer, J. (1996) Biochemistry, 35, 5395–5403.

Michal, C.A. and Jelinski, L.W. (1997) J. Am. Chem. Soc., 119, 9059–9060.

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

Otting, G., Liepinsh, E. and Wüthrich, K. (1993) Biochemistry, 32, 3571–3582.

Rienstra, C.M., Hatcher, M.E., Mueller, L.J., Sun, B.-Q., Fesik, S.W., Herzfeld, J. and Griffin, R.G. (1998) J. Am. Chem. Soc., 120, 10602–10612.

Rosen, M.K., Gardner, K.H., Willis, R.C., Parris, W.E., Pawson, T. and Kay, L.E. (1996) J. Mol. Biol., 263, 627–636.

Saito, H., Tabeta, R., Shoji, A., Ozaki, T. and Ando, I. (1983) Macromolecules, 16, 1050–1057.

Spera, S. and Bax, A. (1991) J. Am. Chem. Soc., 113, 5490–5492.

States, D.J., Haberkorn, R.A. and Ruben, D.J. (1982) J. Magn. Reson., 48, 286–292.

Straus, S.K., Bremi, T. and Ernst, R.R. (1996) Chem. Phys. Lett., 262, 709–715.

Straus, S.K., Bremi, T. and Ernst, R.R. (1998b) J. Biomol. NMR, 12, 39–50.

Sun, B.Q., Costa, P.R. and Griffin, R.G. (1995a) J. Magn. Reson., A 112, 191–198.

Sun, B.Q., Costa, P.R., Kocisko, D., Lansbury, P.T. and Griffin, R.G. (1995b) J. Chem. Phys., 102, 702–707.

Thompson, L.K., McDermott, A.E., Raap, J., van der Wielen, C.M., Lugtenberg, J., Herzfeld, J. and Griffin, R.G. (1992) Biochemistry, 31, 7931–7938.

Tuchsen, E. and Hansen, P.E. (1988) Biochemistry, 27, 8568–8576.

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

Wagner, G. (1983) Quart. Rev. Biophys., 16, 1–57.

Wagner, G. and Bruhwiler, D. (1986) Biochemistry, 25, 5839–5843.

Wagner, G., DeMarco, A. and Wüthrich, K. (1976) Biophys. Struct. Mech., 2, 139–158.

Wishart, D.S., Sykes, B.D. and Richards, F.M. (1991) J. Mol. Biol., 222, 311–333.

Wu, X. and Zilm, K.W. (1993) J. Magn. Reson., A 104, 154–165.

Xu, R., Ayers, B., Cowburn, D. and Muir, T. (1999) Proc. Natl. Acad. Sci. USA, 96, 388–393.

Thông tin
Thông tin xuất bản

Journal of Biomolecular NMR

Tập 16

209-219

Thông tin tác giả