The past year has witnessed significant advances in NMR analysis of bio-mac
romolecules 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 so
lid-state NMR to provide structural information on biological systems is un
dergoing rapid expansion as a result of recent developments. The structural
details that can be derived for biomolecules in the liquid and solid state
s can be used for the rational design of high-affinity ligands. Such studie
s are now complemented by NMR screening of synthetic and natural molecular
libraries. Several NMR screening protocols have been designed that employ b
oth rational and random elements.