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Two-dimensional  13 C- 13 C correlation experiments are widely employed in structure determination of protein assemblies using solid-state nuclear magnetic resonance. Here, we investigate the process of  13 C- 13 C magnetisation transfer at a moderate magic-angle-spinning frequency of 30 kHz using some of the prominent second-order dipolar recoupling schemes. The effect of isotropic chemical-shift difference and spatial distance between two carbons and amplitude of radio frequency on  1 H channel on the magnetisation transfer efficiency of these schemes is discussed in detail.

13C-13C Homonuclear Recoupling in Solid-State Nuclear Magnetic Resonance at a Moderately High Magic-Angle-Spinning Frequency