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- W3181567426 abstract "Aromatic platforms are ubiquitous recognition motifs occurring in protein carbohydrate- binding domains (CBDs), RNA receptors and enzymes. They stabilize the glycoside/ receptor complexes by participating in stacking CH/π interactions with either the α- or β- face of the corresponding pyranose units. In addition, the role played by aromatic units in the stabilization of glycoside cationic transition states has started being recognized in recent years. Extensive studies carried out during the last decade have allowed the dissection of the main contributing forces that stabilize the carbohydrate/aromatic complexes, while helping delineate not only the standing relationship between the glycoside/ aromatic chemical structures and the strength of this interaction but also their potential influence on glycoside reactivity." @default.
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- W3181567426 date "2022-02-01" @default.
- W3181567426 modified "2023-10-06" @default.
- W3181567426 title "Aromatic Interactions in Glycochemistry: From Molecular Recognition to Catalysis" @default.
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- W3181567426 doi "https://doi.org/10.2174/0929867328666210709120216" @default.
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