ArticleJournal of the American Chemical Society2016
Folding of Protein Ions in the Gas Phase after Cation-to-Anion Proton-Transfer Reactions.
Article in Journal of the American Chemical Society, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 37 papers.
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Who cites it
37 citing papers in PubMed.
- From Congestion to Clarity: On the Complementarity of Resolving Power and Spectral Simplification for Intact Protein Characterization.Journal of the American Society for Mass Spectrometry · 2026Article
- Time-Resolved Study of In Situ Generated Protein Subcomplexes by Tandem-Trapped Ion Mobility Spectrometry.Journal of mass spectrometry : JMS · 2026Article
- Analytical applications of gas-phase ion chemistry enabled by mass spectrometry.Analytical methods : advancing methods and applications · 2026Review
- Implementation of Infrared-Activated Negative Electron Transfer Dissociation (IR-NETD) Using Xenon on a Quadrupole-Orbitrap-Quadrupole Linear Ion Trap Mass Spectrometer.Journal of the American Society for Mass Spectrometry · 2026Article
- Structural differentiation of protein charge state conformers via gas-phase ion/ion cross-linking mass spectrometry.International journal of mass spectrometry · 2025Article
- Instrumentation at the Leading Edge of Proteomics.Analytical chemistry · 2024Review
- Structural Elucidation and Relative Quantification of Fatty Acid Double Bond Positional Isomers in Biological Tissues Enabled by Gas-Phase Charge Inversion Ion/Ion Reactions.Analysis & sensing · 2024Article
- Metastability of Protein Solution Structures in the Absence of a Solvent: Rugged Energy Landscape and Glass-like Behavior.Journal of the American Chemical Society · 2024Article
- Relative Quantification of Lipid Isomers in Imaging Mass Spectrometry Using Gas-Phase Charge Inversion Ion/Ion Reactions and Infrared Multiphoton Dissociation.Analytical chemistry · 2023Article
- Immunocomplexed Antigen Capture and Identification by Native Top-Down Mass Spectrometry.Journal of the American Society for Mass Spectrometry · 2023Article
- Understanding of protomers/deprotomers by combining mass spectrometry and computation.Analytical and bioanalytical chemistry · 2023Review
- Ion Mobility Mass Spectrometry (IM-MS) for Structural Biology: Insights Gained by Measuring Mass, Charge, and Collision Cross Section.Chemical reviews · 2023Review
- Protein Unfolding in Freeze Frames: Intermediate States are Revealed by Variable-Temperature Ion Mobility-Mass Spectrometry.Analytical chemistry · 2022Article
- Native Mass Spectrometry: Recent Progress and Remaining Challenges.Annual review of biophysics · 2022Review
- Approaches to Heterogeneity in Native Mass Spectrometry.Chemical reviews · 2022Review
- Advanced Strategies for Proton-Transfer Reactions Coupled with Parallel Ion Parking on a 21 T FT-ICR MS for Intact Protein Analysis.Analytical chemistry · 2021Article
- Recent Developments in Gas-Phase Ion/Ion Reactions for Analytical Mass Spectrometry.Analytical chemistry · 2020Review
- Gas-Phase Collisions with Trimethylamine-N-Oxide Enable Activation-Controlled Protein Ion Charge Reduction.Journal of the American Society for Mass Spectrometry · 2019Article
- On the Preservation of Non-covalent Peptide Assemblies in a Tandem-Trapped Ion Mobility Spectrometer-Mass Spectrometer (TIMS-TIMS-MS).Journal of the American Society for Mass Spectrometry · 2019Article
- Native Ion Mobility Mass Spectrometry: When Gas-Phase Ion Structures Depend on the Electrospray Charging Process.Journal of the American Society for Mass Spectrometry · 2019Article
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Authors and funding
3 authors.
Funding
Abstract
The structure and folding of a protein in solution depends on noncovalent interactions within the protein and those with surrounding ions and molecules. Decoupling these interactions in solution is challenging, which has hindered the development of accurate physics-based models for structure prediction. Investigations of proteins in the gas phase can be used to selectively decouple factors affecting the structures of proteins. Here, we use cation-to-anion proton-transfer reactions (CAPTR) to reduce the charge states of denatured ubiquitin ions in the gas phase, and ion mobility to probe their structures. In CAPTR, a precursor charge state is selected (P) and reacted with monoanions to generate charge-reduced product ions (C). Following each CAPTR event, denatured ubiquitin ions (13+ to 6+) yield products that rapidly isomerize to structures that have smaller collision cross sections (Ω). The Ω values of CAPTR product ions depend strongly on C and very weakly on P. Pre- and post-CAPTR activation was then used to probe the potential-energy surfaces of the precursor and product ions, respectively. Post-CAPTR activation showed that ions of different P fold differently and populate different regions of the potential-energy surface of that ion. Finally, pre-CAPTR activation showed that the structures of protein ions can be indirectly investigated using ion mobility of their CAPTR product ions, even for subtle structural differences that are not apparent from ion mobility characterization of the activated precursor ions. More generally, these results show that CAPTR strongly complements existing techniques for characterizing the structures and dynamics of biological molecules in the gas phase.
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