The need of preparing multiple isotope cross-labeled samples for NOE based structural studies of protein-protein or protein-DNA(or RNA) complexes can be circumvented by measuring residual dipolar couplings (RDCs) and using ambiguous interfacial distance constraints.
RDCs provide relative orientational constrains for docking molecules in a complex. The method can be extended to proteins with multiple ligands or even multimeric protein-ligand complexes, by exploiting the symmetry properties of the macromolecules involved.
NMRFAM can assist users in:
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preparing samples in various aligning media, including liquid crystals (LC)
and stretched acrylamide gels (SAG) -
measuring highly precise RDCs using TROSY based pulse sequences (NH and CH ARTSY pulse sequences for protonated and perdeuterated proteins and RNA/DNA are implemented on our Bruker and Agilent spectrometers) -
measuring and using Residual Chemical Shift Anisotropy (RCSA) constraints
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processing and analyzing spectra to extract RDC or RCSA constraints
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measuring SAXS data
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performing complex structure elucidation using XPLOR-NIH