Abstract
Classic proposals for catalysis by enzymes focused on their ability to position active site residues and substrates for reaction, yet atomic motions are central to the transformation of substrates to products, and more recent studies have started to reveal the role of dynamics in enzyme function. Understanding enzyme catalysis requires both perspectives: knowing how restricted reactants and catalytic groups are; knowing what motions are coupled to the reaction coordinate; and relating these features to the underlying energetics that describe catalysis.
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