Advanced Fragmentation Methods in Biomolecular Mass Spectrometry: Probing Primary and Higher Order Structure with Electrons, Photons and Surfaces
Chapter 10: Photoactivation and Dissociation in Biomolecular Mass Spectrometry
Published:11 Dec 2020
Rachelle Black, Perdita E. Barran, Lennart A. I. Ramakers, 2020. "Photoactivation and Dissociation in Biomolecular Mass Spectrometry", Advanced Fragmentation Methods in Biomolecular Mass Spectrometry: Probing Primary and Higher Order Structure with Electrons, Photons and Surfaces, Frederik Lermyte
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The well-established and preeminent method used to fragment ions in a mass spectrometry (MS) experiment is collision-induced dissociation (CID).1 This is a standard operating procedure in most commercial mass spectrometers with undoubted benefits in reproducibility especially in ‘omic applications.2–4 In a classic CID experiment, a given molecular ion is accelerated through a region of the mass spectrometer filled with an inert gas. Fragmentation proceeds via collisions which results in the transfer of kinetic energy to break the weakest bonds in a given analyte. This preference for weaker bonds can be disadvantageous, for example in cleaving post-translational modifications (PTMs), and when applied to noncovalent protein complexes, the energy deposited prior to fragmentation substantially perturbs the tertiary structure. CID is common in bottom-up proteomics investigations where peptide ions cannot inform on the tertiary or quaternary structure of the protein but do provide valuable information to map the primary structure.