Enzymes in Coherent Motion

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Science  20 Jan 2012:
Vol. 335, Issue 6066, pp. 300-301
DOI: 10.1126/science.1217170

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Subtle conformational changes often play a crucial role in enzyme functions, and enzyme conformations are highly dynamic. The use of only a static structural characterization from an ensemble-averaged measurement at equilibrium is therefore often inadequate for predicting dynamic conformations and understanding correlated enzyme functions. Single-molecule approaches (1), which investigate individual molecules under specific physiological conditions, are a powerful tool for characterizing and analyzing complex enzymatic reaction dynamics and correlated conformational dynamics. On page 319 of this issue, Choi et al. (2) report a novel approach to probing single-molecule conformational dynamics that reveals the conformational motions of the enzyme's active site during enzymatic reaction turnovers.