References
- K. Bromek, D. Lee, R. Hauhart, M. Krych-Goldberg, J.P. Atkinson, P.N. Barlow, and K.Pervushin, Polychromatic selective population inversion for TROSY experiments withlarge proteins, J Am Chem Soc 127,405-411 (2005). https://doi.org/10.1021/ja0462326
- G.M. Clore and A.M. Gronenborn, NMR structure determination of proteins and proteincomplexes larger than 20 kDa, Curr Opin Chem Biol 2, 564-570 (1998). https://doi.org/10.1016/S1367-5931(98)80084-7
- A. Eletsky, H.S. Atreya, G. Liu, and T. Szyperski, Probing structure and functional dynamics of (large) proteins with aromatic rings: L-GFT-TROSY (4,3)D HCCH NMR spectroscopy, J Am Chem Soc 127, 14578-14579 (2005). https://doi.org/10.1021/ja054895x
- R Ernst, G. Bodenhausen, and G. Wokaun, Principles of nuclear magnetic resonance in one and two dimensions, Oxford University Press, Oxford (1987).
- H. Geen and R. Freeman, Band-selective radiofrequency pulses, J Magn Reson 93, 93-141 (1991).
-
N.K. Goto, K.H. Gardner, G.A. Mueller, RC. Willis, and L.E. Kay, A robust and costeffective method for the production of Val, Leu, Ile
$({\delta}^1)$ methyl-protonated$^{15}N-,\;^{13}C-,\;^2H-$ labeled proteins, J Biomol NMR 13, 369-374 (1999). https://doi.org/10.1023/A:1008393201236 - M. Kainosho, T. Torizawa, Y. Iwashita, T. Terauchi, A. Mei Ono, and P. Guntert, Optimal isotope labelling for NMR protein structure determinations, Nature 440, 52-57 (2006).
- L.E. Kay and K.H. Gardner, Solution NMR spectroscopy beyond 25 kDa, Curr Opin Struct BioI 7, 722-731 (1997). https://doi.org/10.1016/S0959-440X(97)80084-X
- N. Khaneja, B. Luy, and S.J. Glaser, Boundary of quantum evolution under decoherence, Proc Natl Acad Sci USA 100, 13162-13166 (2003). https://doi.org/10.1073/pnas.2134111100
- E. Kupce, J. Boyd, and I.D. Campbell, Short selective pulses for biochemicalapplications, J Magn Reson B 106: 300-303 (1995). https://doi.org/10.1006/jmrb.1995.1049
- E. Kupce and R. Freeman, Wide-band excitation with polychromatic pulses, J Magn Reson A 108,268-273 (1994). https://doi.org/10.1006/jmra.1994.1123
- D. Lee, C. Hilty, G. Wider, and K. WUthrich, Effective rotational correlation times ofproteins from NMR relaxation interference, J Magn Reson 178, 72-76 (2006). https://doi.org/10.1016/j.jmr.2005.08.014
-
D. Lee, B. Vogeli, and K. Pervushin, Detection of
$C^',C^{\alpha}$ correlations in proteins using a new time- and sensitivity-optimal experiment, J Biomol NMR 31, 273-278 (2005). https://doi.org/10.1007/s10858-005-2361-4 - D. Marion, M. Ikura, R Tschudin, and A. Bax, Rapid recording of 2D NMR-spectra without phase cycling - Application to the study of hydrogen-exchange in proteins, J Magn Reson 85, 393-399 (1989).
- E. Miclet, D.C. Williams Jr, G.M. Clore, D.L. Bryce, J. Boisbouvier, and A. Bax,Relaxation-optimized NMR spectroscopy of methylene groups in proteins and nucleicacids, J Am Chem Soc 126, 10560-10570 (2004). https://doi.org/10.1021/ja047904v
-
K. Pervushin, R. Riek, G. Wider, and K. Wuthrich, Attenuated
$T_2$ relaxation by mutual cancellation of dipole- dipole coupling and chemical shift anisotropy indicates an avenue to NMR structures of very large biological macromolecules in solution, Proc Natl Acad Sci USA 94,12366-12371 (1997). https://doi.org/10.1073/pnas.94.23.12366 -
K. Pervushin, B. Vogeli, and A. Eletsky, Longitudinal
$^{'}H$ relaxation optimization in TROSY NMR spectroscopy, J Am Chem Soc 124,12898-12902 (2002). https://doi.org/10.1021/ja027149q - R. Riek, J. Fiaux, E.B. Bertelsen, A.L. Horwich, and K. Wuthrich, Solution NMRtechniques for large molecular and supramolecular structures, J Am Chem Soc 124,12144-12153 (2002). https://doi.org/10.1021/ja026763z
- R. Riek, G. Wider, K. Pervushin, and K. WUthrich, Polarization transfer by crosscorrelated relaxation in solution NMR with very large molecules, Proc Natl Acad Sci USA 96, 4918-4923 (1999). https://doi.org/10.1073/pnas.96.9.4918
- P. Schanda and B. Brutscher, Very fast two-dimensional NMR spectroscopy for realtimeinvestigation of dynamic events in proteins on the time scale of seconds, J AmChem Soc 127, 8014-8015 (2005). https://doi.org/10.1021/ja051306e
- P. Schanda, E. Kupce, and B. Brutscher, SOFAST-HMQC experiments for recordingtwo-dimensional heteronuclear correlation spectra of proteins within a few seconds, J Biomol NMR 33, 199-211 (2005). https://doi.org/10.1007/s10858-005-4425-x
- A.J. Shaka, J. Keeler, T. Frenkiel, and R. Freeman, An improved sequence for broadband decoupling - WALTZ-16, J Magn Reson 52, 335-338 (1983).
-
V. Tugarinov, P.M. Hwang, J.E. Ollerenshaw, and L.E. Kay, Cross-correlated relaxation enhanced
$^{1}H-^{13}C$ NMR spectroscopy of methyl groups in very high molecular weight proteins and protein complexes, J Am Chem Soc 125, 10420-10428 (2003). https://doi.org/10.1021/ja030153x -
V. Tugarinov, L.E. Kay, I. Ibraghimov, and V.Y. Orekhov, High-resolution fourdimensional
$^{1}H-^{13}C$ NOE spectroscopy using methyl-TROSY, sparse data acquisition, and multidimensional decomposition, J Am Chem Soc 127, 2767-2775 (2005). https://doi.org/10.1021/ja044032o - Y. Xu, Y. Zheng, J.S. Fan, and D. Yang, A new strategy for structure determination of large proteins in solution without deuteration, Nat Methods 3, 931-937 (2006). https://doi.org/10.1038/nmeth938
- K. Wuthrich, NMR of proteins and nucleic acids. Wiley, New York (1986).
- C. Zwahlen, S.J. Vincent, L. Dibari, M.H. Levitt, and G. Bodenhausen, Quenching spindiffusion in selective measurements of transient Overhauser effects in nuclear magnetic resonance - Applications to oligonucleotides, J Am Chem Soc 116, 362-368 (1994). https://doi.org/10.1021/ja00080a041
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