The past year has witnessed significant advances in NMR analysis of bio-macromolecules from a broad array of disciplines. First, great progress in the development of methods for measuring residual dipolar couplings in nematic media promises to increase both the size of systems to be studied and the accuracy with which structures can be determined. Second, the ability of solid-state NMR to provide structural information on biological systems is undergoing rapid expansion as a result of recent developments. The structural details that can be derived for biomolecules in the liquid and solid states can be used for the rational design of high-affinity ligands. Such studies are now complemented by NMR screening of synthetic and natural molecular libraries. Several NMR screening protocols have been designed that employ both rational and random elements.