Abstract
The DREAM scheme is an efficient adiabatic homonuclear polarization-transfer method suitable for multi-dimensional experiments in biomolecular solid-state NMR. The bandwidth and dynamics of the polarization transfer in the DREAM experiment depend on a number of experimental and spin-system parameters. In order to obtain optimal results, the dependence of the cross-peak intensity on these parameters needs to be understood and carefully controlled. We introduce a simplified model to semi-quantitatively describe the polarization-transfer patterns for the relevant spin systems. Numerical simulations for all natural amino acids (except tryptophane) show the dependence of the cross-peak intensities as a function of the radio-frequency-carrier position. This dependency can be used as a guide to select the desired conditions in protein spectroscopy. Practical guidelines are given on how to set up a DREAM experiment for optimized Cα/Cβ transfer, which is important in sequential assignment experiments.
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Abbreviations
- NMR:
-
Nuclear magnetic resonance
- MAS:
-
Magic-angle spinning
- CP:
-
Cross-polarization
- DREAM:
-
Dipolar recoupling enhanced by amplitude modulation
References
Allen FH (2002) The Cambridge structural database: a quarter of a million crystal structures and rising. Acta Crystallogr B 58(Pt 3 Pt 1):380–388
Cheng VB, Suzukawa HH, Wolfsberg M (1973) Investigations of a nonrandom numerical-method for multidimensional integration. J Chem Phys 59(8):3992–3999
Delaglio F, Grzesiek S, Vuister GW, Zhu G, Pfeifer J, Bax A (1995) NMR-Pipe: a multidimensional spectral processing system based on UNIX pipes. J Biomol NMR 6:277–293
Detken A, Hardy E, Ernst M, Meier BH (2002) Simple and efficient decoupling in magic-angle spinning solid- state NMR: the XiX scheme. Chem Phys Lett 356(3–4):298–304
Ernst M, Meier BH (2010) Adiabatic polarization-transfer methods in MAS spectroscopy. Encycl Magn Reson (EMR) online: doi:10.1002/9780470034590.emrstm9780470030004.pub9780470034592
Fung B, Khitrin A, Ermolaev K (2000) An improved broadband decoupling sequence for liquid crystals and solids. J Magn Reson 142(1):97–101
Gath J, Habenstein B, Bousset L, Melki R, Meier BH, Böckmann A (2011) Solid-state NMR sequential assignments of α-synuclein. Biomol NMR Assign: (in press, available on the web)
Habenstein B, Wasmer C, Bousset L, Sourigues Y, Schütz A, Loquet A, Meier BH, Melki R, Böckmann A (2011) Extensive de novo solid-state NMR assignments of the 33 kDa C-terminal domain of the Ure2 prion. J Biomol NMR 51(3):235–243
Hediger S, Meier BH, KURUR N, BODENHAUSEN G, Ernst R (1994) NMR cross polarization by adiabatic passage through the Hartmann-Hahn condition (APHH). Chem Phys Lett 223:283–288
Hediger S, Meier BH, Ernst R (1995) Adiabatic passage Hartmann-Hahn cross polarization in NMR under magic angle sample spinning. Chem Phys Lett 240:449
Jeener J, Meier BH, Bachmann P, Ernst RR (1979) Investigation of exchange processes by two-dimensional NMR spectroscopy. J Chem Phys 71(11):4546
Kneller D, Kuntz I (1993) UCSF sparky—an NMR display, annotation and assignment tool. J Cell Biochem 53:254
Loquet A, Bousset L, Gardiennet C, Sourigues Y, Wasmer C, Habenstein B, Schütz A, Meier BH, Melki R, Böckmann A (2009) Prion fibrils of Ure2p assembled under physiological conditions contain highly ordered, natively folded modules. J Mol Biol 394(1):108–118
Marion D, Wüthrich K (1983) Application of phase sensitive two-dimensional correlated spectroscopy (COSY) for measurements of 1H-1H spin-spin coupling constants in proteins. Biochem Biophys Res Commun 113:967–974
Radloff C, Ernst R (1989) Spin topology filtration in NMR. Mol Phys 66(1):161–197
Schuetz A, Wasmer C, Habenstein B, Verel R, Greenwald J, Riek R, Böckmann A, Meier BH (2010) Protocols for the sequential solid-state NMR spectroscopic assignment of a uniformly labeled 25 kDa protein: HET-s(1-227). ChemBioChem 11(11):1543–1551
Shi L, Kawamura I, Jung K-H, Brown LS, Ladizhansky V (2010) Conformation of a seven-helical transmembrane photosensor in the lipid environment. Angew Chem Int Ed Engl 50(6):1302–1305
Smith S, Levante T, Meier BH, Ernst R (1994) Computer simulations in magnetic resonance: an object oriented programming approach. J Magn Reson Ser A 106:75–105
Sperling LJ, Berthold DA, Sasser TL, Jeisy-Scott V, Rienstra CM (2010) Assignment strategies for large proteins by magic-angle spinning NMR: the 21-kDa disulfide-bond-forming enzyme DsbA. J Mol Biol 399(2):268–282
Verel R (2001) Adiabatic methods for homonuclear dipolar recoupling in magic angle spinning solid-state NMR. DISS ETH 14152
Verel R, Meier BH (2004) Polarization-transfer methods in solid-state magic-angle- spinning NMR: adiabatic CN pulse sequences. ChemPhysChem 5(6):851–862
Verel R, Baldus M, Ernst M, Meier BH (1998) A homonuclear spin-pair filter for solid-state NMR based on adiabatic-passage techniques. Chem Phys Lett 287:421–428
Verel R, Ernst M, Meier BH (2001) Adiabatic dipolar recoupling in solid-state NMR: the DREAM scheme. J Magn Reson 150(1):81–99
Wang Y, Jardetzky O (2002) Probability-based protein secondary structure identification using combined NMR chemical-shift data. Protein Sci 11(4):852–861
Wasmer C, Schütz A, Loquet A, Buhtz C, Greenwald J, Riek R, Böckmann A, Meier BH (2009) The molecular organization of the fungal prion HET-s in its amyloid form. J Mol Biol 394(1):119–127
Westfeld T (2010) Polarization transfer dynamics in multi-spin systems using the DREAM scheme. Diss ETH 19196:1–153
Ye C, Fu R, Hu J, HOU L, Ding S (1993) C-13 chemical-shift anisotropies of solid amino-acids. Magn Reson Chem 31(8):699–704
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Westfeld, T., Verel, R., Ernst, M. et al. Properties of the DREAM scheme and its optimization for application to proteins. J Biomol NMR 53, 103–112 (2012). https://doi.org/10.1007/s10858-012-9627-4
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DOI: https://doi.org/10.1007/s10858-012-9627-4