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Local mobility of 15N labeled biomolecules characterized through cross-correlation rates: Applications to paramagnetic proteins*

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Abstract

The mobility of 15N labeled proteins can be characterized by measuring the cross-correlation rates δN,NI that govern the conversion of Zeeman order Nz of an amide 15N nucleus into longitudinal two-spin order 2NzIz involving the amide 15N and 1H nuclei. This represents an alternative to the measurement of 15N self-relaxation rates 1/T1 and 1/T2 or 1/T1ρ. The rate of interconversion between Nz and 2NzIz is due to cross-correlation between fluctuations of different interactions and is not affected by a variety of relaxation mechanisms that contribute to the self-relaxation rates 1/T1, 1/T2 and 1/T1ρ. Spin diffusion among protons, which affects the measurements, can be quenched by various means that are evaluated by experiments and simulations. By applying an off-resonance radio-frequency (RF) field in the vicinity of the nitrogen resonance, the spectral density function J(ω) can be determined at the frequency origin and at the nitrogen Larmor frequency. The methods are applied to the paramagnetic High-Potential Iron-Sulfur Protein iso I (HiPIP I) from E. halophila in its reduced state.

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References

  • Akke, M. and Palmer III, A.G. (1996) J. Am. Chem. Soc., 118, 911-912.

    Google Scholar 

  • Banci, L., Bertini, I. and Luchinat, C. (1991) Nuclear and Electron Relaxation, VCH, Weinheim.

    Google Scholar 

  • Banci, L., Bertini, I., Eltis, L.D., Felli, I.C., Kastrau, D.H.W., Luchinat, C., Piccioli, M., Pierattelli, R. and Smith, M. (1994) Eur. J. Biochem., 225, 715-725.

    Google Scholar 

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

    Google Scholar 

  • Bertini, I., Luchinat, C. and Tarchi, D. (1993) Chem. Phys. Lett., 203, 445-449.

    Google Scholar 

  • Bertini, I., Felli, I.C., Kastrau, D.H.W., Luchinat, C., Piccioli, M. and Viezzoli, M.S. (1994) Eur. J. Biochem., 225, 703-714.

    Google Scholar 

  • Bertini, I., Felli, I.C., Luchinat, C. and Rosato, A. (1996a) Proteins Struct. Funct. Genet., 24, 158-164.

    Google Scholar 

  • Bertini, I., Couture, M.M.J., Donaire, A., Eltis, L.D., Felli, I.C., Luchinat, C., Piccioli, M. and Rosato, A. (1996b) Eur. J. Biochem., 241, 440-452.

    Google Scholar 

  • Bertini, I. and Luchinat, C. (1996c) NMR of paramagnetic substances, Coordination Chemistry Reviews, Elsevier, Amsterdam.

    Google Scholar 

  • Boelens, R., Koning, T.M.G. and Kaptein, R. (1988) J. Mol. Struct., 173, 299-311.

    Google Scholar 

  • Borgias, B.A., Gochin, M., Kerwood, D.J. and James, T.L. (1990) Prog. NMR Spectrosc., 22, 83-100.

    Google Scholar 

  • Boyd, J., Hommel, U. and Campbell, I. (1990) Chem. Phys. Lett., 175, 477-482.

    Google Scholar 

  • Brüschweiler, R. and Ernst, R.R. (1991) J. Chem. Phys., 96, 1758-1766.

    Google Scholar 

  • Breiter, D.R., Meyer, T.E., Rayment, I. and Holden, H.M. (1991) J. Biol. Chem., 266, 18660-18667.

    Google Scholar 

  • Dayie, K.T. and Wagner, G. (1994) J. Magn. Reson., A111, 121-126.

    Google Scholar 

  • Cordier, F., Brütscher, B. and Marion, D. (1996) J. Biomol. NMR, 7, 163-168

    Google Scholar 

  • Desvaux, H., Berthault, P., Birlirakis, N., Goldman, M. and Piotto, M. (1995) J. Magn. Reson., A113, 47-52.

    Google Scholar 

  • Desvaux, H. and Goldman, M. (1996) J. Magn. Reson., B110, 198-201.

    Google Scholar 

  • Desvaux, H. (1997) J. Magn. Reson., 127, 1-16.

    Google Scholar 

  • Dickson, D.P.E., Johnson, C.E., Cammak, R., Evans, M.C.W., Hall, D.O. and Rao, K. (1974) Biochem. J., 139, 105-108.

    Google Scholar 

  • Ernst, R.R., Bodenhausen, G. and Wokaun, A. (1987) Principles of Nuclear Magnetic Resonance in One and Two Dimensions, Clarendon Press, Oxford.

    Google Scholar 

  • Farrow, N.A., Muhandiram, R., Singer, A.U., Pascal, S.M., Kay, C.M., Gish, G., Shoelson, S.E., Pawson, T., Forman-Kay, J.D. and Kay, L.E. (1994) Biochemistry, 33, 5984-6003.

    Google Scholar 

  • Grzesiek, S. and Bax, A. (1993) J. Am. Chem. Soc., 115, 12593-12594.

    Google Scholar 

  • Guéron, M. (1975) J. Magn. Reson., 19, 58-66.

    Google Scholar 

  • Iwagami, S.G., Creagh, A.L., Haynes, C.A., Borsari, M., Felli, I.C., Piccioli, M. and Eltis, L.E. (1995) Protein Sci., 4, 2562-2572.

    Google Scholar 

  • Kay, L.E., Torchia, D.A. and Bax, A. (1989) Biochemistry, 28, 8972-8979.

    Google Scholar 

  • Kay, L.E., Nicholson, L.K., Delaglio, F., Bax, A. and Torchia, D.A. (1992) J. Magn. Reson., 97, 359-375.

    Google Scholar 

  • Lefèvre, J.F., Dayie, K.T., Peng, J.W. and Wagner, G. (1996) Biochemistry, 35, 2674-2686.

    Google Scholar 

  • Li, D., Agarwal, A. and Cowan, J.A. (1996) Inorg. Chem., 35, 1121-1125.

    Google Scholar 

  • Lipari, G. and Szabo, A. (1982) J. Am. Chem. Soc., 104, 4546-4559.

    Google Scholar 

  • Mäler, L., Mulder, F.A.A. and Kowalewski, J. (1996) J. Magn. Reson., A117, 220-227.

    Google Scholar 

  • Malliavin, T.E., Delsuc, M.-A. and Lallemand, J.Y. (1992) J. Biomol. NMR, 2, 349-360.

    Google Scholar 

  • Palmer III, A.G., Skelton, N.J., Chazin, W.J., Wright P.E. and Rance, M. (1992) Mol. Phys., 75, 699-711.

    Google Scholar 

  • Palmer III, A.G., Williams, J. and McDermott, A. (1996) J. Phys. Chem., 100, 13293-13310.

    Google Scholar 

  • Peng, J.W. and Wagner, G. (1992) J. Magn. Reson., 98, 308-332.

    Google Scholar 

  • Peng, J.W. and Wagner, G. (1995) Biochemistry, 34, 16733-16752.

    Google Scholar 

  • Pervushin, K., Riek, R., Wider, G. and Wüthrich, K. (1997) Proc. Natl. Acad. Sci. USA, 94, 12366-12371.

    Google Scholar 

  • Piotto, M., Saudek, V. and Sklenar, V. (1992) J. Biomol. NMR, 2, 661-665.

    Google Scholar 

  • Press, W.H., Flannery, B.P., Teukolsky, S.A. and Vetterling, W.T. (1992) Numerical recipes in C, 2nd ed., Cambridge University Press, Cambridge.

    Google Scholar 

  • Reif, B., Hennig, M. and Griesinger, C. (1997) Science, 276, 1230-1233.

    Google Scholar 

  • Sklenar, V., Torchia, D. and Bax, A. (1987) J. Magn. Reson., 79, 375-379.

    Google Scholar 

  • Schwager M. and Bodenhausen, G. (1996) J. Magn. Reson., B111 40-49.

    Google Scholar 

  • Solomon, I. (1955) Phys. Rev., 99, 559-565.

    Google Scholar 

  • Tjandra, N., Szabo, A. and Bax, A. (1996a) J. Am. Chem. Soc., 118, 6986-6991.

    Google Scholar 

  • Tjandra, N., Wingfield, P., Stahl, S. and Bax, A. (1996b) J. Biomol. NMR, 8, 273-284.

    Google Scholar 

  • Vasavada, K.S. and Nageswara Rao, B.D. (1989) J. Magn. Reson., 81, 275-283.

    Google Scholar 

  • Vincent, S.J.F., Zwahlen, C., Bolton, P.H., Logan, T.M. and Bodenhausen, G. (1996) J. Am. Chem. Soc., 118, 3531-3532.

    Google Scholar 

  • Wagner, G. (1993) Curr. Opin. Struct. Biol., 3, 748-754.

    Google Scholar 

  • Werbelow, L. and Thévand, A. (1993) J. Magn. Reson., 101, 317.

    Google Scholar 

  • Zeng, L., Fischer, M.W.F. and Zuiderweg, E.R.P. (1996) J. Biomol. NMR, 7, 157-162.

    Google Scholar 

  • Zinn-Justin, S., Berthault, P., Guenneuges, M. and Desvaux, H. (1997) J. Biomol. NMR, 10, 363-372.

    Google Scholar 

  • Zwahlen, C., Vincent, S.J.F., Di Bari, L., Levitt, M.H. and Bodenhausen, G. (1994) J. Am. Chem. Soc., 116, 362-368.

    Google Scholar 

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Felli, I.C., Desvaux, H. & Bodenhausen, G. Local mobility of 15N labeled biomolecules characterized through cross-correlation rates: Applications to paramagnetic proteins*. J Biomol NMR 12, 509–521 (1998). https://doi.org/10.1023/A:1008301016608

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