ArticleJournal of the American Society for Mass Spectrometry2011
Ion mobility-mass spectrometry reveals conformational changes in charge reduced multiprotein complexes.
Article in Journal of the American Society for Mass Spectrometry, 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 19 papers.
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Who cites it
19 citing papers in PubMed, 47 citations in OpenAlex.
- Stabilization of Protein Interactions through Electrospray Additives in Negative Ion Mode Native Mass Spectrometry.Analytical chemistry · 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
- Protein Complex Heterogeneity and Topology Revealed by Electron Capture Charge Reduction and Surface Induced Dissociation.ACS central science · 2024Article
- Protein complex heterogeneity and topology revealed by electron capture charge reduction and surface induced dissociation.bioRxiv : the preprint server for biology · 2024Article
- Ion Mobility Mass Spectrometry (IM-MS) for Structural Biology: Insights Gained by Measuring Mass, Charge, and Collision Cross Section.Chemical reviews · 2023Review
- Imidazole Derivatives Improve Charge Reduction and Stabilization for Native Mass Spectrometry.Analytical chemistry · 2019Article
- Interpreting the Collision Cross Sections of Native-like Protein Ions: Insights from Cation-to-Anion Proton-Transfer Reactions.Analytical chemistry · 2017Article
- Charging of Proteins in Native Mass Spectrometry.Journal of the American Society for Mass Spectrometry · 2017Article
- Conformational Space and Stability of ETD Charge Reduction Products of Ubiquitin.Journal of the American Society for Mass Spectrometry · 2017Article
- Structures of the kinetically trapped i-motif DNA intermediates.Physical chemistry chemical physics : PCCP · 2016Article
- Ultra-High Resolution Ion Mobility Separations Utilizing Traveling Waves in a 13 m Serpentine Path Length Structures for Lossless Ion Manipulations Module.Analytical chemistry · 2016Article
- A simple heated-capillary modification improves the analysis of non-covalent complexes by Z-spray electrospray ionization.Rapid communications in mass spectrometry : RCM · 2016Article
- Ion Mobility-Mass Spectrometry Reveals Highly-Compact Intermediates in the Collision Induced Dissociation of Charge-Reduced Protein Complexes.Journal of the American Society for Mass Spectrometry · 2016Article
- Analysis of Native-Like Proteins and Protein Complexes Using Cation to Anion Proton Transfer Reactions (CAPTR).Journal of the American Society for Mass Spectrometry · 2015Article
- Huntingtin N-Terminal Monomeric and Multimeric Structures Destabilized by Covalent Modification of Heteroatomic Residues.Biochemistry · 2015Article
- Extensive Charge Reduction and Dissociation of Intact Protein Complexes Following Electron Transfer on a Quadrupole-Ion Mobility-Time-of-Flight MS.Journal of the American Society for Mass Spectrometry · 2015Article
- Bound cations significantly stabilize the structure of multiprotein complexes in the gas phase.Angewandte Chemie (International ed. in English) · 2012Article
- Ion mobility-mass spectrometry for structural proteomics.Expert review of proteomics · 2012Review
- Mass spectrometry: come of age for structural and dynamical biology.Current opinion in structural biology · 2011Review
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Authors and funding
3 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Characterizing intact multiprotein complexes in terms of both their mass and size by ion mobility-mass spectrometry is becoming an increasingly important tool for structural biology. Furthermore, the charge states of intact protein complexes can dramatically influence the information content of gas-phase measurements performed. Specifically, protein complex charge state has a demonstrated influence upon the conformation, mass resolution, ion mobility resolution, and dissociation properties of protein assemblies upon collisional activation. Here we present the first comparison of charge-reduced multiprotein complexes generated by solution additives and gas-phase ion-neutral reaction chemistry. While the charge reduction mechanism for both methods is undoubtedly similar, significant gas-phase activation of the complex is required to reduce the charge of the assemblies generated using the solution additive strategy employed here. This activation step can act to unfold intact protein complexes, making the data difficult to correlate with solution-phase structures and topologies. We use ion mobility-mass spectrometry to chart such conformational effects for a range of multi-protein complexes, and demonstrate that approaches to reduce charge based on ion-neutral reaction chemistry in the gas-phase consistently produce protein assemblies having compact, 'native-like' geometries while the same molecules added in solution generate significantly unfolded gas-phase complexes having identical charge states.
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Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.