Abstract
The relaxation of multiple-quantum coherence due to intramolecular dipole–dipole and chemical shift anisotropy (CSA) relaxation mechanisms is described. It is shown that cross-correlation between the CSAs of the active spins can affect the relaxation of 1 H– 15 N two-spin coherences in the protein backbone. An experiment that enables this effect to be monitored is discussed. Data are presented for perdeuterated 15 N -labelled human dynamic light chain 1 protein (hdlc1). An analysis of the results yields a value for the CSA of the active 1 H .
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