Abstract
Protein function depends critically on dynamics encoded into the native structure. Such structural dynamics are carefully coordinated to display the cooperativity and temporal timing necessary to execute the specific reaction. Determination of such key structural rearrangements requires monitoring protein reactions in real time. In this work, we used synchrotron-based time-resolved X-ray solution scattering (TR-XSS) to visualize structural changes in the Escherichia coli Adenylate kinase (AdK) enzyme upon laser-induced release of a protected ATP substrate.
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