Water in protein function
Water molecules are an integral part of most proteins, essential for biological function. We currently study water in cavities, channels and binding pockets in several intriguing proteins, including antifreeze proteins, aquaporins, halophilic proteins and haloalkane dehydrogenases.
Legend: Ligands usually bind to proteins by displacing water from the binding site. Intestinal fatty acid-binding protein, a prime example, is filled with water in the apo state (upper right). However, bovine β-lactoglobulin is an extreme exception (lower left); its hydrophobic binding pocket is completely dry. In contrast, carbon nanotubes, despite their highly hydrophobic character, contain ordered chains of water molecules.
J Qvist, M Davidovic, D Hamelberg & B Halle, PNAS 105, 6296–6301 (2008).
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Last updated: 2010-02-23