CH/π Interactions in Carbohydrate Recognition
AbstractMany carbohydrate-binding proteins contain aromatic amino acid residues in their binding sites. These residues interact with carbohydrates in a stacking geometry via CH/π interactions. These interactions can be found in carbohydrate-binding proteins, including lectins, enzymes and carbohydrate transporters. Besides this, many non-protein aromatic molecules (natural as well as artificial) can bind saccharides using these interactions. Recent computational and experimental studies have shown that carbohydrate–aromatic CH/π interactions are dispersion interactions, tuned by electrostatics and partially stabilized by a hydrophobic effect in solvated systems. View Full-Text
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Spiwok, V. CH/π Interactions in Carbohydrate Recognition. Molecules 2017, 22, 1038.
Spiwok V. CH/π Interactions in Carbohydrate Recognition. Molecules. 2017; 22(7):1038.Chicago/Turabian Style
Spiwok, Vojtěch. 2017. "CH/π Interactions in Carbohydrate Recognition." Molecules 22, no. 7: 1038.
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