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• W3013064910 abstract "In E. coli dihydrofolate reductase, unusual conformationalmotions of a functional M20 loop that interacts with substrate andcoenzyme have been construed as evidence for dynamical effects inenzyme catalysis. By computing this loop’s conformational freeenergies in the apoenzyme, we show that it is sensitive to the treatmentof long-range electrostatic interactions and the solvation box sizein modeling/simulations. These results provide important guidelinesfor computing reaction/binding free energy profiles of proteins withfunctional loops." @default.
• W3013064910 created "2020-04-03" @default.
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• W3013064910 date "2020-03-19" @default.
• W3013064910 modified "2023-09-25" @default.
• W3013064910 title "Sensitivity of Functional Loop Conformations on Long-Range Electrostatics:Implications for M20 Loop Dynamics in E. coli DihydrofolateReductase" @default.
• W3013064910 doi "https://doi.org/10.1021/acs.jctc.9b01285.s001" @default.
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