Hydrogen/deuterium exchange monitored by mass spectrometry (HDX-MS) is a versatile technique used to study protein conformational stability, protein-protein and protein-ligand interaction.

AbstractHere, the conformational stability of a subtilisin serine protease from Bacillus lentus is studied at pH 10.8, which is an applicationrelevant condition for enzymes for laundry applications. Importantly, no structure has yet been produced for these conditions, but with HDX-MS we were able to quickly probe the dynamic structure extensively. The analysis was performed on an automated setup including a HDX compatible liquid handler with LC and a maXis II UHR-Q-TOF with ETD providing high flexibility, stability and reproducibility.