Two one-dimensional H-1 MMR techniques for efficiently screening Libraries of compounds for binding to macromolecules are described that exploit the changes in relaxation or diffusion rates of small molecules which occur upon complex formation. The techniques are demonstrated by detecting ligands that bind to the FK506 binding protein and the catalytic domain of stromelysin in the presence of compounds that do not bind to these proteins. These one-dimensional methods detect complex formation between a ligand and a macromolecule and thus eliminate false positives often observed with other techniques. In addition, since these methods monitor signals of the uncomplexed compound rather than the bound ligand or macromolecule, ligands for macromolecules of unlimited size can be detected. Furthermore, active compounds can be directly identified from a mixture, significantly reducing the time and material needed for screening large libraries of compounds.