Over the past few years, a number of methods for the calculation of side-chain conformations in proteins have been described. More recent studies have considered the effect of combinatorial packing, derivations from idealized rotameric structures and, to a limited extent, backbone flexibility on the quality and efficiency of calculations of protein side-chain conformation. Although further work is needed to address the issue of backbone displacements, the recent progress solves the packing problem to a significant degree. This opens the way for fruitful incorporation of these methods into general procedures for homology modeling and studies of ligand-protein interactions.