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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.

The existence of the trimeric form both in detergents and lipids is in contrast to undulating layers of dimers in crystals [249]. The conformational flexibility of ASR was examined utilizing site-specifically measured backbone order parameters from DIPSHIFT measurements and 15N spin–lattice relaxation rates in the rotating frame R1ρ [250]. The magnitudes of the observed order parameters indicate that both the well-defined TM regions and the less structured intramembrane loops undergo restricted submicrosecond time scale motions.

126 (2004) 1314–1315. D. R. Tolman, G.

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