Characterization of polyacrylamide-stabilized Pfl phage liquid crystals for protein NMR spectroscopy.
A new polymer-stabilized nematic liquid crystal has been characterized for the measurement of biomolecular residual dipolar couplings. Filamentous Pf1 phage were embedded in a polyacrylamide matrix that fixes the orientation of the particles. The alignment was characterized by the quadrupolar splitting of the 2H NMR water signal and by the measurement of 1H-15N residual dipolar couplings (RDC) in the archeal translation elongation factor 1beta. Protein dissolved in the polymer-stabilized medium orients quantitatively as in media without polyacrylamide. We show that the quadrupolar splitting and RDCs are zero in media in which the Pf1 phage particles are aligned at the magic angle. This allows measurement of J and dipolar couplings in a single sample.