Forgot your password?
New user?
Document Actions
Water erodes 'lock and key' drug model
Water molecules appear ordered between ligands and the polar wall of the enzyme's binding pocket, and may mean that enthalpy changes from rearranging water structures determine the hydrophobic effect in this system © Proc. Natl. Acad. Sci. USA
US researchers have dealt a severe blow to the idea of a single 'hydrophobic effect' that can help explain how all drugs dock with proteins. A team led by Harvard University's George Whitesides has shown that water structures in binding pockets can cause hydrophobic interactions with thermodynamic behaviour differing from a widely used model. 'One conclusion from that is that there is not one hydrophobic effect but a distribution of hydrophobic effects,' Whitesides tells Chemistry World. More...
http://www.rsc.org/chemistryworld/News/2011/October/17101102.asp
Researchers discover new materials to capture methane