Residual dipolar couplings (RDCs) complement standard NOE distance and J-coupling torsion angle data to improve the local and global structure of biomolecules in solution. One powerful application of RDCs is for domain orientation studies, which are especially valuable for structural studies of nucleic acids, where the local structure of a double helix is readily modeled and the orientations of the helical domains can then be determined from RDC data. However, RDCs obtained from only one alignment media generally result in degenerate solutions for the orientation of multiple domains. In protein systems, different alignment media are typically used to eliminate this orientational degeneracy, where the combination of RDCs from two (or more) independent alignment tensors can be used to overcome this degeneracy. It is demonstrated here for native E. coli tRNA(Val) that many of the commonly used liquid crystalline alignment media result in very similar alignment tensors, which do not elimi
|Journal||Journal of Biomolecular NMR|
|State||Published - Mar 2008|
Latham, M., Hanson, P., Brown, D. J., & Pardi, A. (2008). Comparison of alignment tensors generated for native tRNA(Val) using magnetic fields and liquid crystalline media. Journal of Biomolecular NMR, 83–94.