Dissecting the Hydrophobic Effect on the Molecular Level: The Role of Water, Enthalpy, and Entropy in Ligand Binding to Thermolysin1. Issue 6 (2nd January 2013)

• Record Type: Journal Article
• Authors: Biela, Adam; Nasief, Nader N.; Betz, Michael; Heine, Andreas; Hangauer, David; Klebe, Gerhard
• Is Part Of: Angewandte Chemie international edition. Volume 52:Issue 6(2013)
• Page Start: 1822
• Page End: 1828
• Publication Date: 2013-01-02
• Subjects: Chemistry -- Periodicals; 540
• DOI: 10.1002/anie.201208561
• Languages: English
• ISSNs: 1433-7851

Abstract

<abstract abstract-type="graphical" xml:lang="en"> <title> <x xml:space="preserve">Abstract</x> </title> <p> <bold>The hydrophobic effect</bold> 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.<boxed-text content-type="graphic" position="anchor" orientation="portrait"><graphic position="anchor" mimetype="image" xlink:href="ark:/27927/pgg1v48gcg7" orientation="portrait" xlink:type="simple" xmlns:xlink="http://www.w3.org/1999/xlink" /></boxed-text></p> </abstract>