A TROSY CPMG sequence for characterizing chemical exchange in large proteins
Tóm tắt
A new NMR spin relaxation experiment is described for measuring chemical exchange time constants from approximately 0.5 ms to 5 ms in 15N-labeled macromolecules. The pulse sequence is based on the Carr–Purcell–Meiboom–Gill technique [Carr and Purcell (1954) Phys. Rev., 94, 630–638; Meiboom and Gill (1958) Rev. Sci. Instrum., 29, 688–691; Loria et al. (1999) J. Am. Chem. Soc., 121, 2331–2332], but implements TROSY selection [Pervushin et al. (1997) Proc. Natl. Acad. Sci. USA, 94, 12366–12371] to permit measurement of exchange linebroadening contributions to the narrower component of the 1H-15N scalar-coupled doublet. This modification extends the size limitation imposed on relaxation measurements due to the fast decay of transverse magnetization in larger macromolecules. The new TROSY-CPMG experiment is demonstrated on a [U-98% 15 N] labeled sample of basic pancreatic trypsin inhibitor and a [U-83% 2H, U-98% 15 N] labeled sample of triosephosphate isomerase, a 54 kDa homodimeric protein.
Tài liệu tham khảo
Akke, M. and Palmer, A.G. (1996) J. Am. Chem. Soc., 118, 911-912.
Alber, T., Banner, D.W., Bloomer, A.C., Petsko, G.A., Phillips, D., Rivers, P.S. and Wilson, I.A. (1981) Phil. Trans. R. Soc. London, B293, 159-171.
Cavanagh, J., Palmer, A.G., Wright, P.E. and Rance, M. (1991) J. Magn. Reson., 91, 429-436.
Davenport, R.C., Bash, P.A., Seaton, B.A., Karplus, M., Petsko, G.A. and Ringe, D. (1991) Biochemistry, 30, 5821-5826.
Davis, D.G., Perlman, M.E. and London, R.E. (1994) J. Magn. Reson., B104, 266-275.
Deverell, C., Morgan, R.E. and Strange, J.H. (1970) Mol. Phys., 18, 553-559.
Felli, I.C., Desvaux, H. and Bodenhausen, G. (1998) J. Biomol. NMR, 12, 509-521.
Frauenfelder, H., Sligar, S.G. and Wolynes, P.G. (1991) Science, 254, 1598-1603.
Glushka, J., Lee, M., Coffin, S. and Cowburn, D. (1989) J. Am. Chem. Soc., 111, 7716-7722.
Goldman, M. (1984) J. Magn. Reson., 60, 437-452.
Huang, K., Andrec, M., Heald, S., Blake, P. and Prestegard, J.H. (1997) J. Biomol. NMR, 10, 45-52.
Ishima, R., Wingfield, P.T., Stahl, S.J., Kaufman, J.D. and Torchia, D.A. (1998) J. Am. Chem. Soc., 120, 10534-10542.
Kay, L.E., Muhandiram, D.R., Wolf, G., Shoelson, S.E. and Forman-Kay, J.D. (1998) Nat. Struct. Biol., 5, 156-163.
Kroenke, C.D., Loria, J.P., Lee, L.K., Rance, M. and Palmer, A.G. (1998) J. Am. Chem. Soc., 120, 7905-7915.
Lolis, E., Alber, T., Davenport, R.C., Rose, D., Hartman, F.C. and Petsko, G.A. (1990) Biochemistry, 29, 6609-6618.
Lolis, E. and Petsko, G.A. (1990) Biochemistry, 29, 6619-6625.
Loria, J.P., Rance, M. and Palmer, A.G. (1999a) J. Am. Chem. Soc., 121, 2331-2332.
Loria, J.P., Rance, M. and Palmer, A.G. (1999b) J. Magn. Reson., 141, 180-184.
Luz, Z. and Meiboom, S. (1963) J. Chem. Phys., 39, 366-370.
Mori, S., Abeygunawardana, C., O'Neil Johnson, M. and van Zijl, P.C.M. (1995) J. Magn. Reson., B108, 94-98.
Mosteller, F. and Tukey, J.W. (1977) Data Analysis and Regression. A Second Course in Statistics, Addison-Wesley, Reading, MA.
Noble, M.E.M., Wierenga, R.K., Lambeir, A.-M., Opperdoes, F.R., Thunnissen, A.-M.W.H., Kalk, K.H., Groendijk, H. and Hol, W.G.J. (1991) Proteins Struct. Funct. Genet., 10, 50-69.
Palmer, A.G. (1997) Curr. Opin. Struct. Biol., 7, 732-737.
Palmer, A.G., Cavanagh, J., Wright, P.E. and Rance, M. (1991) J. Magn. Reson., 93, 151-170.
Palmer, A.G., Skelton, N.J., Chazin, W.J., Wright, P.E. and Rance, M. (1992) Mol. Phys., 75, 699-711.
Pervushin, K., Riek, R., Wider, G. and Wüthrich, K. (1997) Proc. Natl. Acad. Sci. USA, 94, 12366-12371.
Piotto, M., Saudek, V. and Sklenár, V. (1992) J. Biomol. NMR, 2, 661-665.
Rance, M., Loria, J.P. and Palmer, A.G. (1999) J. Magn. Reson., 136, 92-101.
Salzmann, M., Wider, G., Pervushin, K., Senn, H. and Wüthrich, K. (1999) J. Am. Chem. Soc., 121, 844-848.
Sklenár, V., Piotto, M., Leppik, R. and Saudek, V. (1993) J. Magn. Reson., A102, 241-245.
Sørensen, M.D., Meissner, A. and Sørensen, O.W. (1997) J. Biomol. NMR, 10, 181-186.
Szyperski, T., Luginbühl, P., Otting, G., Güntert, P. and Wüthrich, K. (1993) J. Biomol. NMR, 3, 151-164.
Verlinde, C.L.M.J., Noble, M.E.M., Kalk, K.H., Groendijk, H., Wierenga, R.K. and Hol, W.G.J. (1991) Eur. J. Biochem., 198, 53-57.
Williams, J.C. and McDermott, A.E. (1995) Biochemistry, 34, 8309-8319.