Abstract
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.
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