Structural thermodynamics of complex oligosaccharide recognition by proteins

Information exchange via glycans is ubiquitous in all domains of life and has an important role in cell-cell recognition. Protein-carbohydrate interactions mediate this communication at molecular or cellular interfaces, but the driving forces for these recognition events are challenging to study. First, many glycan components only occur transiently and at low concentrations, making it difficult to isolate biochemical quantities for interaction analyses. Second, in the functional context of a reversible signaling event, many proteins only show low affinities towards carbohydrates hampering their experimental quantification. In our group we therefore have established model systems for the analysis of protein-oligosaccharide interfaces. We use tailspike proteins from bacteriophages and analyze their interactions with bacterial cell surface oligosaccharides and polysaccharides to understand in which way structural features of protein-carbohydrate complexes influence the thermodynamics and the mechanisms of binding.

For further information please contact Dr. Stefanie Barbirz.

thermodynamic signature of water release from a glucose binding pocket