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Dr. Adam Biela, Nader N. Nasief, Michael Betz, Dr. Andreas Heine, Prof. Dr. David Hangauer and Prof. Dr. Gerhard Klebe Dissecting the Hydrophobic Effect on the Molecular Level: The Role of Water, Enthalpy, and Entropy in Ligand Binding to Thermolysin Angewandte Chemie International Edition 52

Version of Record online: 2 JAN 2013 | DOI: 10.1002/anie.201208561

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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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