Recent developments in spin-1/2 isotope labeling and NMR pulse sequence advances have been leveraged to investigate μs – ms motions in enzyme function. These studies have identified concerted motions that occur over large regions of enzymes and often involve highly conserved amino acids. In combination with functional studies these NMR-identified motions have been implicated in partaking in the rate-determining step in the catalytic cycle. This review examines several of the more recent solution NMR studies that demonstrate the essential nature of conformational motions.
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