Abstract
Residual dipolar couplings arise from small degrees of alignment of molecules in a magnetic field. Media employed for imparting alignment onto biomolecules lacking sufficient magnetic susceptibility anisotropies themselves comprise dilute aqueous phospholipid bicelles, colloidal suspensions of rod-shaped viruses and lamellar phases of quasiternary surfactant systems. The magnitude of the residual dipolar couplings depends upon the degree of ordering and allows the determination of the corresponding internuclear vectors with respect to the molecule’s alignment frame. Inclusion of dipolar constraints into NMR structure calculations leads to improved accuracy of the resulting structures, especially in cases where the information content provided by traditional NOE constraints is limited. This chapter describes the different media used for alignment and the application of dipolar coupling information for protein structure refinement and fold determination.
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References
Annila, A., Aittio, H., Thulin, E., and Drakenberg, T., (1999), J. Biomol. NMR. 14, 223–230.
Barrientos, L. G., Dolan, C., and Gronenborn, A. M., (2000), J. Biomol. NMR. 16, 329–337.
Barrientos, L. G., Louis, J. M., and Gronenborn, A. M., (2001), J. Magn. Reson. 148,159–162.
Bax, A., and Tjandra, N., (1997), J. Biomol. NMR. 10, 289–292.
Bayer, P., Varani, L., and Varani, G., (1999), J. Biomol. NMR. 14, 149–155.
Bewley, C. A., Gustafson, K. R., Boyd, M. R., Covell, D. G., Bax, A., Clore, G. M., and Gronenborn, A. M. (1998), Nat. Struct. Biol. 5, 571–578.
Brünger, A. T., Adams, G. M., Clore, G. M., DeLano, W. L., Gros, P., Grosse-Kunstleve, R. W., Jiang, J. S., Kuszewski, J., Nilges, M., Pannu, N. S., Read, R. J., Rice, L. M., Simonson, T. and Warren, G. L., (1998), Acta Cryst. D. Biol. Crystallogr. 54, 905–921.
Cai, M., Huang, Y., Zheng, R., Wei, S.,Q., Ghirlando, R., Lee, M.,S., Craigie, R., Gronenborn, A.,M.,and Clore, G.,M., (1998), Nat.,Struct.,Biol. 5, 903–909.
Cavagnero, S., Dyson, J. H., and Wright, P. E., (1999), J. Biomol. NMR. 13, 387–391
Clore, G. M., and Gronenborn, A. M., (1989), CRC Critical Rev. Biochem. and Molec. Biol. 24, 479–564.
Clore, G. M., and Gronenborn, A. M., (1998), Proc. Natl. Acad. Sci.U.S.A. 95, 5891–5898.
Clore, G. M., Gronenborn, A. M., and Tjandra, N. (1998a), J. Magn. Reson. 131,159–162.
Clore, G. M., Gronenborn, A. M., and Bax, A. (1998b), J. Magn. Reson. 133, 216–221.
Clore, G. M., Stanch, M. R., and Gronenborn, A. M. (1998c), J. Amer. Chem. Soc. 120, 10571–10572.
Clore, G. M., Stanch, M. R., Bewley, C. A., Cai, M., and Kuszewski, J., (1999), J. Amer. Chem. Soc. 121, 6513–6514.
Chou, J. J., Li, S. and Bax, A., (2000), J. Biomol. NMR. 18, 217–227.
Delaglio, F., Kontaxis, G., and Bax, A., (2000), J. Amer. Chem. Soc. 122, 2142–2143.
Fischer, M. W. F., Losonczi, J. A., Weaver, J. L., and Prestegard, J. H., (1999), Biochemistry 38, 9013–9022.
Fleming, K., Gray, D., Prasannan, S., and Matthews, S., (2000), J. Amer. Chem. Soc. 122, 5224–5225.
Fraden, S., Maret, G., Caspar, D. L. D., and Meyer, R. B., (1989), Phys. Rev. Lett. 63, 2068–2071.
Garrett, D. S., Seok, Y. J., Peterkofsky, A., Gronenborn, A. M., and Clore, G. M., (1999), Nat. Struct. Biol. 6, 166–173.
Glucksman, M. J., Hay, R. D., and Makowski, L., (1986), Science 231, 1273–1276.
Glucksman, M. J., Bhattacharjee, S., and Makowski, L., (1992), J. Mol. Biol. 226, 455–470.
Gomati, R., Appell, J., Bassereau, P., Marignan, J., and Porte, G., (1987), J. Phys. Chem. 91, 6203–6210.
Hansen, M. R., Rance, M., and Pardi, A., (1998a), J. Amer. Chem. Soc. 120, 11210–11211.
Hansen, M. R., Mueller, L., and Pardi, A., (1998b), Nat. Struct. Biol. 5, 1065–1074.
Hus, J.-C., Marion, D., and Blackledge, M., (2000), J. Mol. Biol. 298, 927–936.
Koenig, B. W., Hu, J.-S., Ottiger, M., Bose, S., Hendler, R. W., and Bax, A., (1999), J. Amer. Chem. Soc. 121, 1385–1386.
Kung, H. C., Wang, K. Y., Golier, I., and Bolton, P. H., (1995), J. Magn. Reson. Ser. B. 109, 323–325.
Kuszewski, J., Gronenborn, A. M., and Clore, G. M., (1996), Protein Science 5, 1067–1080.
Kuszewski, J., Gronenborn, A. M., and Clore, G. M., (1997), J. Magn. Reson. 125, 171–177.
Lei, L., Li, P., and Asher, S. A., (1999), J. Amer. Chem. Soc. 121, 4040–4046.
Lipari, G., and Szabo, A., (1982), J. Amer. Chem. Soc. 104, 4546–4559.
Losonczi, J. A. and Prestegard, J. H., (1998), J. Biomol. NMR 12, 447–451.
Losonczi, J. A., Andrec, M., Fischer, M. W., and Prestegard, J. H., (1999), J. Magn. Reson. 138, 334–342.
Makowski, L., Caspar, D. L., and Marvin, D. A., (1980), J. Mol. Biol. 140, 149–181.
McGrath, K. M., (1997), Langmuir 13, 1987–1995.
Nakamura, H., and Okano, K., (1983), Phys. Rev. Lett. 50, 186–189.
Ojennus, D. D., Mitton-Fry, R. M., and Wuttke, D. S., (1999), J. Biomol. NMR. 14, 175–179. Ottiger, M. and Bax, A., (1998), J. Biomol. NMR. 12, 361–372.
Ottiger, M., Delaglio, F., and Bax, A., (1998a), J. Magn. Reson. 131, 373–378.
Ottiger, M., Delaglio, F., Marquardt, J. L., Tjandra, N., and Bax, A., (1998b), J. Magn. Reson. 134, 365–369.
Ottiger, M., and Bax, A., (1999), J. Biomol. NMR. 13, 187–191.
Prestegard, J. H., (1998), Nat. Struct. Biol. 5 Suppl, 517–522.
Prestegard, J. H., Tolman, J. R., Al-Hashimi, H. M. and Andrec, M., (1999) in “Structure Computation and Dynamics in Protein NMR”, Biological Magnetic Resonance, Volume 17, N. R. Krishna and L. J. Berliner, Editors, Kluwer Academic/Plenum Publishers, pp. 311–356.
Prosser, R. S., Losonczi, J. A., and Shiyanovskaya, I. V., (1998), J. Amer. Chem. Soc. 120, 11010–11011.
Rückert, M., and Otting, G., (2000), J. Amer. Chem. Soc. 122, 7793–7797.
Sanders II, C. R., and Landis, G. C., (1995), Biochemistry 34, 4030–4040.
Sanders II, C. R., and Schwonek, J. P., (1992), Biochemistry 31, 8898–8905.
Sass, H.-J., Cordier, F., Hoffmann, A., Rogowski, M., Cousin, A., Omichinski, J. G., Lowen, H., and Grzesiek, S., (1999), J. Amer. Chem. Soc. 121, 2047–2055.
Sass, H.-J., Musco, G., Stahl, S. J., Wingfield, P. T. and Grzesiek, S., (2000), J. Biomol. NMR. 18, 303–309.
Skrynnikov, N. R., Goto, N. K., Yang, D., Choy, W.-Y., Tolman, J. R., Mueller, G. A. and Kay, L. E., (2000), J. Mol. Biol. 295, 1265–1273.
Stubbs, G., Warren, S., and Holmes, K. (1977), Nature 267, 216–221.
Tian, F., Bolon, P. J., and Prestegard, J. H. (1999), J. Amer. Chem. Soc. 121, 7712–7713.
Tjandra, N., Grzesiek, S., and Bax, A., (1996), J. Amer. Chem. Soc. 118, 6264–6272.
Tjandra, N., and Bax, A., (1997a), Science 278, 1111–1114.[erratum in Science (1997) 278, 1697].
Tjandra, N., and Bax, A., (1997b), J. Magn. Reson. 124, 512–515.
Tjandra, N., Omichinski, J. G., Gronenbom, A. M., Clore, G. M., and Bax, A., (1997), Nat. Struct. Biol. 4, 732–738.
Tolman, J. R., Flanagan, J. M., Kennedy, M. A., and Prestegard, J. H., (1995), Proc. Natl. Acad. Sci. U.S.A. 92, 9279–9283.
Tolman, J. R., Flanagan, J. M., Kennedy, M. A., and Prestegard, J. H., (1997), Nat. Struct. Biol. 4, 292–297.
Tolman, J. R., and Prestegard, J. H., (1996a), J. Magn. Reson. Series B 112, 245–252.
Tolman, J. R., and Prestegard, J. H., (1996b), J. Magn. Reson. Series B 112, 269–274.
Torbert, J. and Maret, G., (1979), J. Mol. Biol. 134, 843–845.
Tycko, R., Blanco, F. J., and Ishii, Y., (2000), J. Amer. Chem. Soc. 122, 9340–9341.
Wang, H., Eberstadt, M., Olejniczak, E. T., Meadows, R. P., and Fesik, S.W., (1998a), J. Biomol. NMR 12, 443–446.
Wang, Y.-X., Marquardt, J. L., Wingfield, P., Stahl, S. J., Lee-Huang, S., Torchia, D., and Bax, A., (1998b), J. Amer. Chem. Soc. 120, 7385–7386.
Warren, J. J., and Moore, P. B., (2001), J. Magn. Reson., 149, 271–275.
Won, Y.-Y., Davis, H. T., and Bates, F. S., (1999), Science 283, 960–963.
Wolf, Y. I., Grishin, N. V., and Koonin, E.V., (2000), J. Mol. Biol. 299, 897–905.
Wüthrich, K., (1986), NMR of Proteins and Nucleic Acids (Wiley, New York)
Zweckstetter, M., and Bax, A., (2000), J. Am. Chem. Soc. 122, 3791–3792.
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Gronenborn, A.M. (2002). Protein Structure Refinement using Residual Dipolar Couplings. In: Krishna, N.R., Berliner, L.J. (eds) Protein NMR for the Millennium. Biological Magnetic Resonance, vol 20. Springer, Boston, MA. https://doi.org/10.1007/0-306-47936-2_8
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DOI: https://doi.org/10.1007/0-306-47936-2_8
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