Macromolecular Complexes

hpr IIA sidechains smallThe 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.

hpr IIA sidechains2RDCs 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:

  • preparing samples in various aligning media, including liquid crystals (LC)liquid crystals and stretched acrylamide gels (SAG)
  • funnelmeasuring 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
  • processing and analyzing spectra to extract RDC or RCSA constraints
  • measuring SAXS data
  • performing complex structure elucidation using XPLOR-NIH