Defining the role of active-site loop fluctuations in dihydrofolate reductase catalysis
Author:
Publisher
Proceedings of the National Academy of Sciences
Subject
Multidisciplinary
Reference37 articles.
1. Enzyme Dynamics: The Statistical Physics Approach
2. Viscosity-dependent structural fluctuations in enzyme catalysis
3. A perspective on biological catalysis
4. Backbone Dynamics in Dihydrofolate Reductase Complexes: Role of Loop Flexibility in the Catalytic Mechanism
5. Enzyme Dynamics During Catalysis
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