ArticleJournal of the American Society for Mass Spectrometry2024
Charging of DNA Complexes in Positive-Mode Native Electrospray Ionization Mass Spectrometry.
Article in Journal of the American Society for Mass Spectrometry, 2024. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 2 papers.
What it found
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The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
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Who cites it
2 citing papers in PubMed.
- Elucidating HLTF-Mediated DNA Fork Remodeling via Native Mass Spectrometry.Journal of the American Chemical Society · 2026Article
- Native Mass Spectrometry Captures the Conformational Plasticity of Proteins with Low-Complexity Domains.JACS Au · 2025Article
Corrections and comments
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Authors and funding
5 authors.
Funding
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Abstract
Native mass spectrometry (nMS) provides insights into the structures and dynamics of biomacromolecules in their native-like states by preserving noncovalent interactions through "soft" electrospray ionization (ESI). For native proteins, the number of charges that are acquired scales with the surface area and mass. Here, we explore the effect of highly negatively charged DNA on the ESI charge of protein complexes and find a reduction of the mass-to-charge ratio as well as a greater variation. The charge state distributions of pure DNA assemblies show a lower mass-to-charge ratio than proteins due to their greater density in the gas phase, whereas the charge of protein-DNA complexes can additionally be influenced by the distribution of the ESI charges, ion pairing events, and collapse of the DNA components. Our findings suggest that structural features of protein-DNA complexes can result in lower charge states than expected for proteins.
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