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• W2049373071 abstract "We show that the conformational features of the molecular complexes of E. coli β-galactosidase and 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 quantum mechanical results show that the 3D-shapes of the ligand/inhibitor within the enzyme binding site depend on the chemical nature of the compounds. In fact, they depend on the relative size of the stereoelectronic bariers for chair deformation or for rotation around Φ glycosidic linkage." @default.
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• W2049373071 date "2002-04-05" @default.
• W2049373071 modified "2023-10-01" @default.
• W2049373071 title "Conformational Selection of Glycomimetics at Enzyme Catalytic Sites: Experimental Demonstration of the Binding of Distinct High-Energy Distorted Conformations of <i>C</i>-, <i>S</i>-, and <i>O</i>-Glycosides by <i>E. </i><i>C</i><i>oli</i> β-Galactosidases" @default.
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• W2049373071 doi "https://doi.org/10.1021/ja0122445" @default.
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