Angewandte Chemie International Edition
© WILEY-VCH Verlag GmbH & Co. KGaA, Weinheim
Cover Picture: Contribution of Ligand Desolvation to Binding Thermodynamics in a Ligand–Protein Interaction (Angew. Chem. Int. Ed. 38/2006)
Ligand–protein interactions are associated with the desolvation of a ligand as it enters the protein-binding pocket (see cover picture). Homans and co-workers describe in their Communication on page 6374 ff. an estimate of the thermodynamic cost associated with this desolvation process. These data permit a complete breakdown of the binding thermodynamics into contributions from the ligand, protein, and solvent for the interaction of a small-molecule ligand with the mouse major urinary protein.
Also of Interest
Structure and Smell
In his Minireview on page 6254 ff., C. S. Sell discusses why prediction of the odor character, intensity, and threshold for a given molecule from its structure will remain a statistical exercise despite our increased understanding of the mechanism of olfaction.
The fundamental interaction of metal atoms with dinitrogen is considered in the Review by H.-J. Himmel and M. Reiher on page 6264 ff. DFT calculations show the extent of N2 activation in these complexes.
In their Communication on page 6290 ff., S. K. Kim and co-workers report how photodissociation of [D1]thiophenol produces two distinct phenylthiyl radicals in which the reactive singly occupied molecular orbital is oriented either parallel or perpendicular to the molecular plane.