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Dissecting the Hydrophobic Effect on the Molecular Level: The Role of Water, Enthalpy, and Entropy in Ligand Binding to Thermolysin

Authors


  • G.K. is grateful to the EU for providing an ERC Advanced Grant (DrugProfilBind 268145). We thank the beamline support staff at the Helmholtz-Zentrum Berlin, Bessy II for radiation time and their advice during data collection. We thank the HZB for financial support of travel costs.

Abstract

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The hydrophobic effect is associated with the successive replacement of water molecules in the binding site of a protein by hydrophobic groups of the ligand. Although the hydrophobic effect is assumed to be entropy-driven, large changes in enthalpy and entropy are observed with the model system thermolysin. Structural changes in the binding features of the water molecules ultimately determine the thermodynamics of the hydrophobic effect.

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