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- W2788343488 abstract "Significance Fluorination has become a key design strategy for the development of a broad range of small-molecule therapeutics. As a result, there is significant interest in understanding how fluorine substituents affect interactions between ligands and their protein targets. In this context, we elucidate the molecular details of fluorine recognition in the fluoroacetyl–CoA thioesterase, which has evolved a 10 6 -fold selectivity for a single fluorine atom as part of its native function in organofluorine biosynthesis. Using a combination of thermodynamic, kinetic, and biophysical experiments, we show that fluorine recognition is entropically driven by interaction with a hydrophobic residue in the binding site. These findings highlight the importance of hydrophobic and solvation effects in mediating fluorine-binding selectivity driven by natural selection." @default.
- W2788343488 created "2018-03-06" @default.
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- W2788343488 date "2018-02-16" @default.
- W2788343488 modified "2023-09-23" @default.
- W2788343488 title "Entropy drives selective fluorine recognition in the fluoroacetyl–CoA thioesterase from <i>Streptomyces cattleya</i>" @default.
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- W2788343488 doi "https://doi.org/10.1073/pnas.1717077115" @default.
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- W2788343488 hasPublicationYear "2018" @default.
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