Abstract
Hydrogen/deuterium exchange mass spectrometry (HDX-MS) has within the last 25 years evolved to become a well-established technique for analysing the solution-phase conformational dynamics and molecular interactions of proteins, attributes that can be difficult to access by other methods for structural analysis. This review presents the latest development within HDX-MS with a special focus on how improvements in instrumentation, methodology and data analysis have expanded the capability of HDX-MS to analyse complex and hitherto elusive protein states. Such protein states include large or multi-protein complexes, lipid-associated or integral membrane proteins, proteins with highly dynamic regions, disulfide-bonded proteins, heavily glycosylated proteins and proteins in formulations.
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