Structural investigation of multivalent carbohydrate-protein interactions using synthetic biomolecules.
Understanding multivalent carbohydrate-protein interactions at the molecular level requires access to structural details of these important biological recognition processes. Recent developments toward this goal comprise the use of conformationally defined molecular rulers in combination with binding assays, crystallographic investigation of complexes of multivalent ligands and their target proteins, and distance measurements in the nanometer range by EPR spectroscopy.
Valentin
V
Wittmann
D000818:Animals; D001665:Binding Sites; D050260:Carbohydrate Metabolism; D002241:Carbohydrates / Q000737:chemistry; D018360:Crystallography, X-Ray; D004578:Electron Spin Resonance Spectroscopy; D006801:Humans; D037102:Lectins / Q000737:chemistry / Q000378:metabolism*; D008958:Models, Molecular; D011485:Protein Binding
D002241:Carbohydrates; D037102:Lectins