ArticleJournal of the American Society for Mass Spectrometry2026
From Congestion to Clarity: On the Complementarity of Resolving Power and Spectral Simplification for Intact Protein Characterization.
Article in Journal of the American Society for Mass Spectrometry, 2026. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Not yet cited in PubMed.
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Abstract
Top-down mass spectrometry (TDMS) is a powerful platform for the structural and functional analysis of intact proteins, enabling the detailed characterization of proteoforms and precise localization of post-translational modifications. The incorporation of alternative fragmentation techniques, such as electron transfer dissociation, electron transfer higher-energy collisional dissociation, and ultraviolet photodissociation, in instruments such as Tribrid Orbitrap mass spectrometers enhances sequence coverage and improves the confidence in PTM assignment. However, tandem mass spectrometry of intact proteins >30 kDa presents substantial challenges. The resulting spectra are often highly complex with overlapping product ion signals that complicate spectral interpretation. Although increasing the mass resolution can help resolve closely spaced product ions, it is often insufficient to fully alleviate spectral congestion for large proteins. In such cases, proton transfer charge reduction (PTCR) can simplify mass spectra by dispersing product ions across a wider mass-over-charge (
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