Structural proteomic techniques have recently evolved because of advances
in mass spectrometry (MS). Several MS techniques, such as, Hydrogen-deuterium
exchange, oxidative footprinting or radical probe mass spectrometry, chemical
crosslinking, affinity purification, and ion mobility separation, can now be used to
analyse protein interaction networks, conformational changes, protein structures, and
other downstream applications. This article examines proteomic MS techniques'
progression from convectional to advanced techniques, tandem MS techniques, MS of
multiprotein complexes, and emerging MS techniques for structural proteomics. Also,
the applications that were gleaned from these techniques were reviewed. Lastly, the
future of this rapidly emerging field was highlighted.
Keywords: Affinity purification, Chemical crosslinking, Hydrogen-deuterium exchange, Ion mobility, Mass spectrometry, Oxidative footprinting, Radical probe mass spectrometry (RP-MS), Structural proteomics.
