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The structure of a transition-state analog of muscle creatine kinase reveals significant asymmetry within the functional homodimer. The amino-terminal region is shown to be intimately involved in subunit association and intersubunit communication.

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A comparison of hydrogenous and perdeuterated haloalkane dehalogenase shows similar overall structures with only slight alterations in surface regions. However, perdeuteration causes exclusion of a critical water nucleophile from the active site leading to a structure of an inactive, low pH enzyme form.
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