Probing protein conformation, structure and dynamics
The protons present on protein amides and backbone are labile by nature. When dissolved in solution proteins routinely exchange these protons with hydrogen groups in the solution. Hydrogen deuterium exchange mass spectrometry (HDX-MS) takes advantage of this phenomena by exchanging the protons from the protein with deuterium in deuterated solutions. The rate of hydrogen-to-deuterium exchange provides solvent accessibility information which can be used to infer protein structure and conformation. For single protein and protein complexes, HDX can be used to obtain protein structure and conformation information. Additionally, for protein complexes HDX can provide information on protein-protein or protein-ligand interaction sites and conformational changes induced by posttranslational modifications (PTMs).
HDX-MS is a powerful tool for studying protein structures, dynamics, folding, complexes and interactions. This paper will address the advantages of HDX-MS, the information it provides and the complementary role it plays with traditional techniques, as well as the recent innovations in hardware and software, and workflows that have been developed to simplify HDX-MS.