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Opportunity at National Institute of Standards and Technology (NIST)

Hydrogen/Deuterium Exchange Mass Spectrometry of Proteins and Biosimilar Drugs

Location

Material Measurement Laboratory, Biomolecular Measurement Division

RO# Location
50.64.51.B6750 Gaithersburg, MD

Please note: This Agency only participates in the February and August reviews.

Advisers

Name E-mail Phone
Hudgens, Jeffrey Warren jeffrey.hudgens@nist.gov 240-314-6485 (IBBR/NIST, Rockville)

Description

This research develops and applies hydrogen/deuterium exchange mass spectrometry (HDX-MS) for determining the dynamic physical-chemical properties of proteins, 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. This 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 MALDI-TOF/TOF, a wide variety of analytical and preparation chromatographs, and numerous optical/NMR spectroscopic instruments.

 

Keywords:
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;

Eligibility

Citizenship:  Open to U.S. citizens
Level:  Open to Postdoctoral applicants
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