ArticleJournal of the American Society for Mass Spectrometry2019
Gas-Phase Collisions with Trimethylamine-N-Oxide Enable Activation-Controlled Protein Ion Charge Reduction.
Article in Journal of the American Society for Mass Spectrometry, 2019. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 16 papers.
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Who cites it
16 citing papers in PubMed.
- Probing the Annular Lipid Belt of Membrane Proteins Using Native Mass Spectrometry.Methods in molecular biology (Clifton, N.J.) · 2026Article
- Hybrid Detergents Facilitate Scalable Charge Reduction and Stabilize Membrane Proteins While Retaining Lipid Interactions.Chemistry (Weinheim an der Bergstrasse, Germany) · 2025Article
- Design and Synthesis of Hetero-Bicephalic Detergents for Native Mass Spectrometry of Membrane Proteins.Journal of the American Chemical Society · 2025Article
- Stabilization of Protein Interactions through Electrospray Additives in Negative Ion Mode Native Mass Spectrometry.Analytical chemistry · 2025Article
- Native Mass Spectrometry of Membrane Protein-Lipid Interactions in Different Detergent Environments.Analytical chemistry · 2024Article
- Native mass spectrometry of membrane protein-lipid interactions in different detergent environments.bioRxiv : the preprint server for biology · 2024Article
- What's the defect? Using mass defects to study oligomerization of membrane proteins and peptides in nanodiscs with native mass spectrometry.Methods (San Diego, Calif.) · 2023Review
- Emergence of mass spectrometry detergents for membrane proteomics.Analytical and bioanalytical chemistry · 2023Review
- Electrospray ionization of native membrane proteins proceedsRSC advances · 2022Article
- Charge Engineering Reveals the Roles of Ionizable Side Chains in Electrospray Ionization Mass Spectrometry.JACS Au · 2021Article
- Lipid Head Group Adduction to Soluble Proteins Follows Gas-Phase Basicity Predictions: Dissociation Barriers and Charge Abstraction.International journal of mass spectrometry · 2021Article
- Discovery of Potent Charge-Reducing Molecules for Native Ion Mobility Mass Spectrometry Studies.Analytical chemistry · 2020Article
- Collision-Induced Unfolding Studies of Proteins and Protein Complexes using Drift Tube Ion Mobility-Mass Spectrometer.Analytical chemistry · 2020Article
- Charge Reduction of Membrane Proteins in Native Mass Spectrometry Using Alkali Metal Acetate Salts.Analytical chemistry · 2020Article
- Scratching the surface: native mass spectrometry of peripheral membrane protein complexes.Biochemical Society transactions · 2020Review
- Imidazole Derivatives Improve Charge Reduction and Stabilization for Native Mass Spectrometry.Analytical chemistry · 2019Article
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11 authors.
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Abstract
Modulating protein ion charge is a useful tool for the study of protein folding and interactions by electrospray ionization mass spectrometry. Here, we investigate activation-dependent charge reduction of protein ions with the chemical chaperone trimethylamine-N-oxide (TMAO). Based on experiments carried out on proteins ranging from 4.5 to 35 kDa, we find that when combined with collisional activation, TMAO removes approximately 60% of the charges acquired under native conditions. Ion mobility measurements furthermore show that TMAO-mediated charge reduction produces the same end charge state and arrival time distributions for native-like and denatured protein ions. Our results suggest that gas-phase collisions between the protein ions and TMAO result in proton transfer, in line with previous findings for dimethyl- and trimethylamine. By adjusting the energy of the collisions experienced by the ions, it is possible to control the degree of charge reduction, making TMAO a highly dynamic charge reducer that opens new avenues for manipulating protein charge states in ESI-MS and for investigating the relationship between protein charge and conformation. ᅟ.
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