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Dr. Matthew R. Lockett, Dr. Heiko Lange, Dr. Benjamin Breiten, Dr. Annie Heroux, Dr. Woody Sherman, Dr. Dmitrij Rappoport, Patricia O. Yau, Dr. Philip W. Snyder and Prof. Dr. George M. Whitesides The Binding of Benzoarylsulfonamide Ligands to Human Carbonic Anhydrase is Insensitive to Formal Fluorination of the Ligand Angewandte Chemie International Edition 52

Version of Record online: 20 JUN 2013 | DOI: 10.1002/anie.201301813

Thumbnail image of graphical abstract

It's the water that matters. Pairs of benzo- and perfluorobenzoarylsulfonamide ligands bind to human carbonic anhydrase with a conserved binding geometry, an enthalpy-driven binding, and indistinguishable binding affinities (see picture). These data support the pervasive theory that the lock-and-key model disregards an important component of binding: the water, which fills the binding pocket of the protein and surrounds the ligand.

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