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Validation of protein dynamics

We can validate Alphafold structural predictions using HDX, with this useful in the analysis of disordered regions 

Epitope mapping of antibodies

We can screen multiple nanobodies/antibodies to determine their binding interfaces and allosteric changes induced upon binding

Small molecule and substrate binding sites

HDX is powerful to screen small molecule binding pockets and lipid binding sites, and can reveal unexpected allosteric conformational changes

About us

This webpage is the collaborative Hydrogen deuterium exchange mass spectrometry (HDX-MS) arm of the Burke laboratory at the University of Victoria. We have worked extensively with multiple industrial/biotech partners and >50 academic laboratories to carry out HDX-MS analysis, and are excited to expand to a larger customer base. We offer competitive rates, and first class expertise in the study of challenging H/DX projects. 

Hydrogen deuterium exchange mass spectrometry (HDX-MS) is used to measure the exchange rate of amide hydrogens with deuterated solvent. The exchange rate of amide hydrogens is exquisitely sensitive to changes in secondary structure and solvent accessibility, and this technique has been used extensively to characterize protein folding, as well as protein-protein, protein-lipid, and protein-small molecule binding sites. Building on our >20 year history of using this technique with >80 publications using HDX-MS to study almost all aspects of protein dynamics we are now providing this service to interested academic and industrial partners. 

HDX-MS experiments can be carried out with a variety of stimuli, including protein binding partners, ligands, and membrane surfaces. Importantly, HDX-MS provides information on allosteric conformational changes. Our laboratory has made significant progress in the use of HDX-MS to study membrane localized signalling complexes that have been challenging to study by other structural approaches. We provide epitope mapping of antibody binding sites, and mapping of protein-protein interactions. We also provide screening of oncogenic specific drug binding interfaces.

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