Solid-state NMR study of protein structure. Methods based on the measurement of internuclear distances

Several high-resolutlon solid-state NMR methods have been developed in the last ten years to measure weak homonuclear or heteronuclear dipolar couplings in solid samples. These methods use the magic angle spinning technique and include the rotational resonance and the rf-driven recoupling (RFDR) techniques for the measurement of homonuclear distances and techniques such as REDOR and TEDOR for the measurement of heteronuclear distances. These techniques have been applied to a variety of systems including small peptides, membrane proteins and enzyme-substrate-inhibitor complexes.