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1. The Role of Protein Dynamics in Thymidylate Synthase Catalysis: Variants of Conserved 2‘-Deoxyuridine 5‘-Monophosphate (dUMP)-Binding Tyr-261

2. Structure of Cry2Aa Suggests an Unexpected Receptor Binding Epitope

3. Energetic Contributions of Four Arginines to Phosphate-Binding in Thymidylate Synthase Are More than Additive and Depend on Optimization of 'Effective Charge Balance'

4. Contribution of a salt bridge to binding affinity and dUMP orientation to catalytic rate: mutation of a substrate-binding arginine in thymidylate synthase

6. Caspase-6

7. Contributors

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