This research develops and applies hydrogen/deuterium exchange mass spectrometry (HDX-MS) for determining the dynamics and physical-chemical properties of proteins, biopharmaceuticals, glycoproteins, peptides, peptide-metal complexes, receptors, and biocatalysts. 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, and comparability measurements among innovator drugs and biosimilar drug candidates. The HDX-MS laboratory can now conduct measurements on membrane and transmembrane proteins with fully automated apparatus. Research is conducted at the nearby NIST & UMD joint Institute for Bioscience & Biotechnology Research. The well-equipped laboratory includes a fully automated HDX Orbitrap tandem mass spectrometer with ETD capability, a cryo-EM, SAXS, neutron source, a wide variety of analytical and preparation chromatographs, and numerous optical/NMR spectroscopic instruments.

 

key words

Bioactivity; Biocatalyst; Biomolecule; Biosimilar; Cell signaling; Conformation; ECD; Electron capture dissociation; Electron transfer dissociation; ETD; Glycan; Glycoeptitope; Glycoprotein; Glycosylation; H/D exchange; Hydrogen-deuterium exchange; HDX-MS; HXMS; Ion fragmentation; Mass spectra; Mass spectrometry; Membrane protein; Myristoylated protein; Myristoylation; Peptide; Protein; Structure function; Tandem mass spectrometry; Transmembrane protein;

Citizenship:  Open to U.S. citizens

Level:  Open to Postdoctoral applicants