Abstract
During the last 25 years, high resolution NMR has become one of the most powerful tools available for the elucidation of molecular structure and dynamics. Although the technique has been widely used for investigating samples in the liquid (solution) state, recent developments enable one to study solids as well. Unlike X-ray and neutron diffraction methods which are used so far mainly for solid samples, NMR spectroscopy has emerged to be powerful in studying both solids and liquids. The resolution achievable by the recently developed solid-state NMR techniques makes it possible to compare structures in two different states based on the results obtained by the same technique. Such comparisons are particularly relevant in the case of biologically important molecules like proteins, nucleic acids, and membrane components whose high molecular weights and polymeric nature dictate certain behaviors which are adequately understood only if they are studied in both solution and solid states. The technique of solid-state NMR spectroscopy therefore bridges the information gap between the conventional solution (NMR, ESR, and optical spectroscopy) and solid-state methods (X-ray and neutron diffraction).