The Dependence of Carbohydrate-Aromatic Interaction Strengths on the Structure of the Carbohydrate.

ABSTRACT: Interactions between proteins and carbohydrates are ubiquitous in biology. Therefore, understanding the factors that determine their affinity and selectivity are correspondingly important. Herein, we have determined the relative strengths of intramolecular interactions between a series of monosaccharides and an aromatic ring close to the glycosylation site in an N-glycoprotein host. We employed the enhanced aromatic sequon, a structural motif found in the reverse turns of some N-glycoproteins, to facilitate face-to-face monosaccharide-aromatic interactions. A protein host was used because the dependence of the folding energetics on the identity of the monosaccharide can be accurately measured to assess the strength of the carbohydrate-aromatic interaction. Our data demonstrate that the car

SUBMITTER: Hsu CH 

PROVIDER: S-EPMC4924591 | biostudies-literature | 2016 Jun

REPOSITORIES: biostudies-literature