Proteins must undergo motions that contribute to their function. Studying these dynamic protein motions can provide great insight into enzyme catalysis. However it is often difficult to resolve these critical atomic-level features to understand their contributions to calalysis. We use a combination of multi-temperature crystallography and multiconformation modeling to describe how separate conformational states can affect discrete steps in a catalytic cycle.

One is the loneliest number: Modeling multiple conformations using room temperature x-ray crystallography

251st National Meeting (2016)

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