SOLID-STATE NMR-STUDY OF PROTEIN-STRUCTURE - METHODS BASED ON THE MEASUREMENT OF INTERNUCLEAR DISTANCES

Several high-resolution solid-state NMR methods have been developed in the last ten years to measure weak homonuclear or heteronuclear dipol ar couplings in solid samples. These methods use the magic angle spinn ing technique and include the rotational resonance and the rf-driven r ecoupling (RFDR) techniques for the measurement of homonuclear distanc es and techniques such as REDOR and TEDOR for the measurement of heter onuclear distances. These techniques have been applied to a variety of systems including small peptides, membrane proteins and enzyme-substr ate-inhibitor complexes.