Biophysical studies of weakly aligned biomolecules

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The last ten years have seen a revolution in the use of residual dipolar couplings in macromolecular structure determination by NMR spectroscopy. In liquid crystals, macromolecules partially align and non-zero averaging of the dipolar couplings occurs. These 'residual' dipolar couplings provide both angular and distance information and can be used to determine atomic structures. Under the previous funding period, we developed new methods for measuring residual dipolar couplings using polymer-stabilized liquid crystals. By spinning these media at the magic angle, dipolar couplings and chemical shift anisotropies are removed but can be selectively re-introduced with REDOR-like recoupling pulse sequences. We propose to continue our research on weakly aligned biomolecules for NMR spectroscopy and, as a new direction, for applications in small-angle X-ray scattering (SAXS).  Both NMR and SAXS are important tools for visualizing the three dimensional structures of biomolecules.  By using liquid crystals and other orienting systems, we can extend the range and usefulness of these techniques.  The tangible benefits are a better understanding of basic life processes involving proteins and other biomolecules and improved tools for drug development and design in health research.