| Abstract
| - We show that the conformational features of the molecular complexes of E. coli β-galactosidaseand O-glycosides may differ from those formed with closely related compounds in their chemical nature,such as C- and S-glycosyl analogues. In the particular case presented here, NMR and ab initio quantummechanical results show that the 3D-shapes of the ligand/inhibitor within the enzyme binding site dependon the chemical nature of the compounds. In fact, they depend on the relative size of the stereoelectronicbariers for chair deformation or for rotation around Φ glycosidic linkage.
|
