Research in my lab is concerned with the development and application of novel NMR techniques to understand protein structure and function. In particular we are interested in how molecular dynamics, intermolecular recognition and the quaternary organization of multi-domain proteins serve to mediate biological function. NMR spectroscopy is particularly well suited to study such problems and its capabilities are still evolving. One area of continued research is centered on making NMR measurements when the protein is slightly aligned relative to the magnetic field. Most prominent among the benefits of this approach is the appearance of residual dipolar couplings (RDCs) in the NMR spectrum. These RDCs are relatively easily measured and represent an abundant source of highly precise information on the relative orientations of different internuclear 'bonds' within the molecule. In addition, RDCs exhibit sensitivity to molecular motions on the nsec-msec timescales, during which many functionally important motions occur. An ongoing effort is to develop effective experimental as well as analytical tools for the characterization of biomolecular motions at atomic resolution.