When bound to proteins, paramagnetic lanthanide ions induce a range of effects that are observable by NMR spectroscopy, including pseudo-contact shifts (PCSs), paramagnetic relaxation enhancements (PREs), and residual dipolar couplings (RDCs).[1] These effects provide valuable constraints that can expedite protein structure refinement,[2] the analysis of protein–protein [3] and protein–ligand interactions,[4] and, potentially, the study of protein ...
