ArticleJournal of the American Society for Mass Spectrometry2015
How Closely Related Are Conformations of Protein Ions Sampled by IM-MS to Native Solution Structures?
Article in Journal of the American Society for Mass Spectrometry, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 46 papers.
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Who cites it
46 citing papers in PubMed, 112 citations in OpenAlex.
- IscS Kinetics in Native Mass Spectrometry Buffers Reveal Key Physiochemical Properties that Influence Enzyme Activity.Journal of the American Society for Mass Spectrometry · 2026Article
- Probing the Annular Lipid Belt of Membrane Proteins Using Native Mass Spectrometry.Methods in molecular biology (Clifton, N.J.) · 2026Article
- Improving the Quadrupole to Ion Mobility Region in a Digital Quadrupole/Ion Mobility/Orbitrap Mass Spectrometer.Journal of the American Society for Mass Spectrometry · 2025Article
- Roughhousing with Ions: Surface-Induced Dissociation and Electron Capture Dissociation as Diagnostics of Q-Cyclic IMS-TOF Instrument Tuning Gentleness.Journal of the American Society for Mass Spectrometry · 2025Article
- Structure and Stabilities of Solution and Gas Phase Protein Complexes.Journal of the American Society for Mass Spectrometry · 2024Article
- 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
- Development of a Modular, Open-Source, Reduced-Pressure, Drift Tube Ion Mobility Spectrometer.Journal of the American Society for Mass Spectrometry · 2024Article
- The role of solvation on the conformational landscape of α-synuclein.The Analyst · 2023Article
- Proteomics Methodologies: The Search of Protein Biomarkers Using Microfluidic Systems Coupled to Mass Spectrometry.Proteomes · 2023Review
- Step toward Probing the Nonannular Belt of Membrane Proteins.Analytical chemistry · 2022Article
- Investigation of Charge-State-Dependent Compaction of Protein Ions with Native Ion Mobility-Mass Spectrometry and Theory.Journal of the American Society for Mass Spectrometry · 2022Article
- THE IMS PARADOX: A PERSPECTIVE ON STRUCTURAL ION MOBILITY-MASS SPECTROMETRY.Mass spectrometry reviews · 2021Review
- AgAnalytical chemistry · 2020Article
- Collision-Induced Unfolding Studies of Proteins and Protein Complexes using Drift Tube Ion Mobility-Mass Spectrometer.Analytical chemistry · 2020Article
- Molecular Mechanism of ISC Iron-Sulfur Cluster Biogenesis Revealed by High-Resolution Native Mass Spectrometry.Journal of the American Chemical Society · 2020Article
- Native IM-Orbitrap MS: Resolving What Was Hidden.Trends in analytical chemistry : TRAC · 2020Article
- Ion Activation Methods for Peptides and Proteins.Analytical chemistry · 2020Review
- Topological Characterization of Coordination-Driven Self-assembly Complexes: Applications of Ion Mobility-Mass Spectrometry.Journal of the American Society for Mass Spectrometry · 2019Article
- Transient multimers modulate conformer abundances of prion protein monomer through conformational selection.Scientific reports · 2019Article
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Authors and funding
2 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Here, we critically evaluate the effects of changes in the ion internal energy (E(int)) on ion-neutral collision cross sections (CCS) of ions of two structurally diverse proteins, specifically the [M + 6H](6+) ion of ubiquitin (ubq(6+)), the [M + 5H](5+) ion of the intrinsically disordered protein (IDP) apo-metallothionein-2A (MT), and its partially- and fully-metalated isoform, the [CdiMT](5+) ion. The ion-neutral CCS for ions formed by "native-state" ESI show a strong dependence on E(int). Collisional activation is used to increase E(int) prior to the ions entering and within the traveling wave (TW) ion mobility analyzer. Comparisons of experimental CCSs with those generated by molecular dynamics (MD) simulation for solution-phase ions and solvent-free ions as a function of temperature provide new insights about conformational preferences and retention of solution conformations. The E(int)-dependent CCSs, which reveal increased conformational diversity of the ion population, are discussed in terms of folding/unfolding of solvent-free ions. For example, ubiquitin ions that have low internal energies retain native-like conformations, whereas ions that are heated by collisional activation possess higher internal energies and yield a broader range of CCS owing to increased conformational diversity due to losses of secondary and tertiary structures. In contrast, the CCS profile for the IDP apoMT is consistent with kinetic trapping of an ion population composed of a wide range of conformers, and as the E(int) is increased, these structurally labile conformers unfold to an elongated conformation.
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