The use of residual dipolar couplings (RDCs) in the analysis of biomolecular structure and dynamics has expanded rapidly since its potential as a source of structural information on proteins was demonstrated in the mid 1990s.1,2 Of course, this work on proteins rested on applications to smaller biomolecular systems that occurred much earlier,3 and even these early applications benefited from prior research on organic molecules in partially ordered liquid crystals.4 However, in the 1990s, the existence of efficient means of introducing magnetically active isotopic labels (13C and 15N) and the availability of triple resonance strategies for selective manipulation and assignment of NMR resonances made widespread application to large biomolecules possible. It was fortuitous that the 13C and 15N labels introduced had small magnetogyric ratios, allowing simple dipolar interactions with directly bonded protons to dominate RDC observations. Prior work had focused on systems with couplings coming from the much larger 1H-1H dipolar and 2H quadrupolar interactions. While large interactions and the resultant increased size of observable couplings may have seemed an advantage, these large interactions also lead to complex spectra and broader lines. In the case of 1H-1H interactions, additional splittings of resonances from protons at long distances arose, and in both cases broader lines resulted from enhanced spin relaxation processes.
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