Exploration of conformational flexibility and hydrogen bonding of xylosides in different solvents, as a model system for enzyme active site interactions

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The predominantly populated conformation of carbohydrates in solution does not necessarily represent the biologically active species; rather, any conformer accessible without too large an energy penalty may be present in a biological pathway. Thus, the conformational preferences of a naphthyl xyloside, which initiates in vivo synthesis of antiproliferative glycosaminoglycans, have been studied by using NMR spectroscopy in a variety of solvents. Equilibria comprising the conformations C-4(1), S-2(0) and C-1(4) were found, with a strong dependence on the hydrogen bonding ability of the solvent. Studies of fluorinated analogues revealed a direct hydrogen bond from the hydroxyl group at C2 to the fluorine atom at C4 by a (1h)J(F4,HO2) coupling. Hydrogen bond directionality was further established via comparisons of fluorinated levoglucosan molecules.


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Subject classification (UKÄ) – MANDATORY

  • Chemical Sciences
Original languageEnglish
Pages (from-to)5465-5472
JournalOrganic and Biomolecular Chemistry
Issue number33
Publication statusPublished - 2013
Publication categoryResearch