1. Interacciones de Van der Waals Van der Waals Interactions Dominate Ligand-Protein Association in a Protein Binding Site Occluded from Solvent Water

2. Las nubes electrónicas de los átomos se influyen mutuamente. Se induce la formación de un dipolo eléctrico transitorio. Estos dipolos se atraen: interacción de van der Waals

3. The van der Waals interactions are of the order of 2.8-4.0Å. The "binding" energy is very low and of the order of <1 kcal/mol, and does not display a large orientational dependency.

6. Structure of the Ligand 2-Methoxy- 3-isobutylpyrazine (IBMP) Mouse major urinari protein

9. Stereoview of the superimposition of the ligand binding sites observed in crystal structures of uncomplexed Y120F MUP (blue) and Y120F MUP (red) in complex with IBMP (green). No ordered water molecules are observable within the binding site in either structure. Figure prepared using MOLMOL.30

10. Stereoview of the superimposition of the ligand binding sites observed in crystal structures of complexes of wild-type MUP (red) with IBMP (green) and Y120F MUP (blue) with IBMP (magenta). The ligand-protein hydrogen bond observed in the wild-type protein is indicated by the dotted line. Figure prepared using MOLMOL.30