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CH/? Interactions in Carbohydrate Recognition.


ABSTRACT: Many carbohydrate-binding proteins contain aromatic amino acid residues in their binding sites. These residues interact with carbohydrates in a stacking geometry via CH/? 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/? interactions are dispersion interactions, tuned by electrostatics and partially stabilized by a hydrophobic effect in solvated systems.

SUBMITTER: Spiwok V 

PROVIDER: S-EPMC6152320 | biostudies-literature | 2017 Jun

REPOSITORIES: biostudies-literature

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CH/π Interactions in Carbohydrate Recognition.

Spiwok Vojtěch V  

Molecules (Basel, Switzerland) 20170623 7


Many 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  ...[more]

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