Protein-Ligand Interaction Analysis
Map protein-protein and protein-ligand interactions by hydrogen-deuterium exchange, and see which regions become protected on binding.
Binding affinity numbers tell you that two things interact. They don’t tell you where, or whether the interaction changes the shape of either partner beyond the contact surface. HDX-MS fills that gap: label both the free and complex states, compare deuterium uptake peptide by peptide, and the regions that go quiet on binding are usually the interface or somewhere allosterically coupled to it, which is its own useful finding.
This works for protein-protein complexes, small-molecule binding, peptide ligands, and cofactors: basically anything that changes solvent accessibility when it binds.
Common reasons clients come to us
- Checking whether a new ligand binds the same pocket as a known one
- Investigating an allosteric effect that shows up functionally but isn’t obviously located
- Confirming a proposed mechanism of action with structural evidence
- Comparing binding footprints across a series of related compounds
Sample Requirements
As a starting point, plan on roughly 200 µg of target protein and 1 mg of compound. The real amount depends on the protein size and how many states you want to compare, so we’ll confirm quantities with you before anything ships.
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