NMR studies of protein-glycan interactions using uniformly 13C-labelled glycans

Glycans, a large group of carbohydrate-based polymers and conjugates, often serve as contact points in protein interactions and play a key role in processes such as intracellular trafficking and host-pathogen interactions.

However, protein-glycan interactions remain poorly characterized, primarily due to a lack of adequate tools for visualizing the detailed structure of protein-bound glycans.

Nuclear magnetic resonance (NMR) spectroscopy has great potential in this regard, but currently used NMR methods are restricted to small oligosaccharides and fail to visualize high-affinity binding events between glycans and proteins.

Whereas isotopic labelling has facilitated the study of large proteins using NMR, limited access to 13C-labelled glycans has hindered similar study of glycans.

In this project, I will develop a new NMR approach by combining the expression of 13C-labelled glycans with novel NMR experiments tailored for large and complex glycans.

Once established, I will explore the ability of this approach to uncover structural details of model systems that are relevant for viral research and biomass degradation.

By helping to decipher the structure of large and complex glycans in unprecedented detail, I will pave the way for new insights into how polysaccharides and glycoconjugates mediate their biological functions.

The four-year project will be performed at SLU, in close collaboration with chemists and structural biologists in Sweden and abroad.