Publication | Closed Access
Solvent Effects in Carbohydrate Binding by Synthetic Receptors: Implications for the Role of Water in Natural Carbohydrate Recognition
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Citations
22
References
2008
Year
Proteinlipid InteractionEngineeringGlycobiologyPolysaccharideNatural Carbohydrate RecognitionMixed Solvent SystemsCarbohydrate BindingMolecular RecognitionBiophysicsGlycosylationProtein ChemistryBiochemistryG Protein-coupled ReceptorReceptor (Biochemistry)Biomolecular EngineeringSolvent EffectsHydrophobic InteractionsMedicineCarbohydrate-protein InteractionSynthetic Lectins
How do they do it? Carbohydrates are intrinsically difficult to bind in water. Lectins and other proteins succeed, but do they use polar or hydrophobic interactions? Studies of synthetic lectins in mixed solvent systems shed new light onto this contentious issue (see scheme; X=hydrophobic or hydrophilic solubilizing groups; R=H or alkyl group). Supporting information for this article is available on the WWW under http://www.wiley-vch.de/contents/jc_2002/2008/z704733_s.pdf or from the author. Please note: The publisher is not responsible for the content or functionality of any supporting information supplied by the authors. Any queries (other than missing content) should be directed to the corresponding author for the article.
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