This research develops and applies hydrogen/deuterium exchange mass spectrometry (HDX-MS) for measuring the dynamics and physical-chemical properties of proteins, biopharmaceuticals, and vaccines. Topics of particular interest include the effects of post-translational modifications (PTMs) on protein dynamic structure and protein-ligand interactions, structure-function relationships between glycan structure and glycoprotein folding, vaccine stability, and comparability measurements among innovator drugs and biosimilar drug candidates. Research is conducted at the nearby NIST & UMD joint Institute for Bioscience & Biotechnology Research (IBBR). The HDX-MS lab includes a fully automated HDX robotic sample handler, custom state-of-the-art subzero chromatography apparatus, and tribrid Orbitrap mass spectrometer with ETD, UVPD, CID, and HCD.

 

key words

Biologics; Biomolecule; Biopharmaceutical; Biosimilar; Cell signaling; Conformation; Electron transfer dissociation; ETD; Glycan; Glycoeptitope; Glycoprotein; Glycosylation; H/D exchange; Hydrogen-deuterium exchange; HDX-MS; HXMS; Ion fragmentation; Mass spectrometry; Membrane protein; Peptide; Protein; Structure function; UV photodissociation; Vaccine

Citizenship:  Open to U.S. citizens

Level:  Open to Postdoctoral applicants