This yields $$ \rho \left( t \right) = I_1z \textCos^2 \left( \tau_\textm \tilded \mathord\left/ , \right. \kern-\nulldelimiterspace 2 \right) + I_2z \sin^2 \left( \tau_\textm \tilded \mathord\left/ \vphantom \tilded 2 \right. \kern-\nulldelimiterspace 2 \right) + \frac12\left( I_1y I_2x – I_1x I_2y \right)\sin \left( \tau_\textm \tilded \right), $$ (12)where \( \tilded \) depends on the dipolar

coupling strength (Bennett et al. 1992). The first two terms indicate transfer of longitudinal magnetization, while the third term represents double quantum E7080 in vivo selleck states, which can be eliminated by phase cycling. If a short mixing time τ m ~ 1 ms is used, only correlations between spins separated by one bond are promoted, which is the optimal condition for the assignment of the chemical shifts. Intermolecular transfer between 13C spins with RFDR is difficult due to rapid relayed spin diffusion along the multispin 13C-labeled molecular network (Boender et al. 1995). An alternative is to generate 13C–13C correlations by 1H spin diffusion (Mulder et al. 1998). In a CP3 or CHHC proton-mediated spin diffusion experiment, the 13C magnetization

is transferred back to 1H after the first precession interval. Next, 1H spin diffusion is allowed to take place during a mixing period. Finally, the signal is transferred again to 13C by a third CP step and detected. In this way, mixing by the strong 1H dipolar interactions is combined with the high resolution of a 13C MAS spectrum. An effective transfer range, d max, can be determined for short mixing times, and intermolecular distance constraints can be resolved with this sequence (de Boer et al. 2002). In practice, a limited number of such constraints can be very useful for elucidating the structure of solids. Heteronuclear correlation spectroscopy Another class

of experiments that is widely used in biological solid-state NMR is 1H–13C heteronuclear correlation spectroscopy. A straightforward 1H–13C correlation experiment consists of Ketotifen the CP scheme, where t 1 is inserted after the first 1H π/2 pulse and the CP interval constitutes the mixing step. This is known as wideline separation, since broad 1H lines in the indirect dimension are separated by correlation with 13C shifts in the direct dimension (Schmidt-Rohr and Spiess 1994). Modern FSLG MAS NMR methods also provide a direct correlation of proton signals of the protein with 13C responses (van Rossum et al. 1997). For heteronuclear transfer of magnetization, LG–CP methods are most convenient to improve the 1H resolution (Fig. 3b).