An NMR perspective on enzyme dynamics

Nuclear magnetic resonance (NMR) relaxation techniques have proved effective in the study of multiple time-scale dynamics of enzymes in different phases of the catalytic cycle. Some of the documented studies using NMR in enzyme dynamics include conformational selection in ribonuclease A, reaction of coordinate compression in E. coli dihydrofolate reductase, substrate binding and drug resistance in HIV protease, protein dynamics during turnover in cyclophilin A and mesophilic and thermophilic enzymes. In all these applications, NMR showed that protein motion plays important roles in all aspects of catalysis.