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Extra info for Annual Reports on NMR Spectroscopy

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Soc. 125 (2003) 10420–10428. M. Korzhnev, K. Kloiber, V. Kanelis, V. E. Kay, Probing slow dynamics in high molecular weight proteins by methyl-TROSY NMR spectroscopy: application to a 723-residue enzyme, J. Am. Chem. Soc. 126 (2004) 3964–3973. G. E. E. London, Direct measurements of the dissociationrate constant for inhibitor-enzyme complexes via the T1ρ and T2 (CPMG) methods, J. Magn. Reson. B104 (1994) 266–275. 56 Hazime Saitô [91] M. G. Palmer III, Monitoring macromolecular motions on microsecond to millisecond time scales by R1ρ-R1 constant relaxation time NMR spectroscopy, J.

94 (1997) 12366–12371. P. Loria, M. G. Palmer III, A TROSY CPMG sequence for characterizing chemical exchange in large proteins, J. Biomol. NMR 15 (1999) 151–155. Y. M. E. Kay, Double- and zero-quantum NMR relaxation dispersion experiments sampling millisecond time scale dynamics in protein, J. Am. Chem. Soc. 126 (2004) 1886–1891. [88] V. M. E. E. Kay, Cross-correlated relaxation enhanced 1H-13C NMR spectroscopy of methyl groups in very high molecular weight proteins and protein complexes, J. Am.

Natl. Acad. Sci. U. S. A. 94 (1997) 12366–12371. P. Loria, M. G. Palmer III, A TROSY CPMG sequence for characterizing chemical exchange in large proteins, J. Biomol. NMR 15 (1999) 151–155. Y. M. E. Kay, Double- and zero-quantum NMR relaxation dispersion experiments sampling millisecond time scale dynamics in protein, J. Am. Chem. Soc. 126 (2004) 1886–1891. [88] V. M. E. E. Kay, Cross-correlated relaxation enhanced 1H-13C NMR spectroscopy of methyl groups in very high molecular weight proteins and protein complexes, J.

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