ArticleJournal of the American Society for Mass Spectrometry2006
The role of conformation on electron capture dissociation of ubiquitin.
Article in Journal of the American Society for Mass Spectrometry, 2006. 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.
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- Enhancing Top-Down Proteomics of Brain Tissue with FAIMS.Journal of proteome research · 2021Article
- Replacing HChemical science · 2018Article
- Analysis of Photoirradiated Water Accommodated Fractions of Crude Oils Using Tandem TIMS and FT-ICR MS.Environmental science & technology · 2017Article
- Gas-phase protein conformation/multimer ion formation by electrospray ion mobility-mass spectrometry: bovine insulin and ubiquitin.Philosophical transactions. Series A, Mathematical, physical, and engineering sciences · 2016Article
- Oversampling Selective Accumulation Trapped Ion Mobility Spectrometry Coupled to FT-ICR MS: Fundamentals and Applications.Analytical chemistry · 2016Article
- To What Extent is FAIMS Beneficial in the Analysis of Proteins?Journal of the American Society for Mass Spectrometry · 2016Article
- Probing Protein Structure and Folding in the Gas Phase by Electron Capture Dissociation.Journal of the American Society for Mass Spectrometry · 2015Article
- Targeted high-resolution ion mobility separation coupled to ultrahigh-resolution mass spectrometry of endocrine disruptors in complex mixtures.Analytical chemistry · 2015Article
- Structural characterization of holo- and apo-myoglobin in the gas phase by ultraviolet photodissociation mass spectrometry.Chemical science · 2015Article
- Populations of metal-glycan structures influence MS fragmentation patterns.Journal of the American Society for Mass Spectrometry · 2015Article
- Solution dependence of the collisional activation of ubiquitin [M + 7H](7+) ions.Journal of the American Society for Mass Spectrometry · 2014Article
- Evidence for two new solution states of ubiquitin by IMS-MS analysis.The journal of physical chemistry. B · 2014Article
- Characterization of electron transfer dissociation in the Orbitrap Velos HCD cell.Journal of the American Society for Mass Spectrometry · 2013Article
- Electrothermal supercharging in mass spectrometry and tandem mass spectrometry of native proteins.Analytical chemistry · 2013Article
- Does Electron Capture Dissociation Cleave Protein Disulfide Bonds?ChemistryOpen · 2012Article
- Supercharging with trivalent metal ions in native mass spectrometry.Journal of the American Society for Mass Spectrometry · 2012Article
- Electron capture dissociation of hydrogen-deficient peptide radical cations.Journal of the American Society for Mass Spectrometry · 2012Article
- The early life of a peptide cation-radical. Ground and excited-state trajectories of electron-based peptide dissociations during the first 330 femtoseconds.Journal of the American Society for Mass Spectrometry · 2012Article
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3 authors.
Funding
Abstract
Effects of protein conformation on electron capture dissociation (ECD) were investigated using high-field asymmetric waveform ion mobility spectrometry (FAIMS) and Fourier-transform ion cyclotron resonance mass spectrometry. Under the conditions of these experiments, the electron capture efficiency of ubiquitin 6+ formed from three different solution compositions differs significantly, ranging from 51 +/- 7% for ions formed from an acidified water/methanol solution to 88 +/- 2% for ions formed from a buffered aqueous solution. This result clearly indicates that these protein ions retain a memory of their solution-phase structure and that conformational differences can be probed in an ECD experiment. Multiple conformers for the 7+ and 8+ charge states of ubiquitin were separated using FAIMS. ECD spectra of conformer selected ions of the same charge states differ both in electron capture efficiency and in the fragment ion intensities. Conformers of a given charge state that have smaller collisional cross sections can have either a larger or smaller electron capture efficiency. A greater electron capture efficiency was observed for ubiquitin 6+ that has the same collisional cross section as one ubiquitin 7+ conformer, despite the lower charge state. These results indicate that the shape of the molecule can have a greater effect on electron capture efficiency than either collisional cross section or charge state alone. The cleavage locations of different conformers of a given charge state were the same indicating that the presence of different conformers in the gas phase is not due to difference in where charges are located, but rather reflect conformational differences most likely originating from solution. Small neutral losses observed from the singly- and doubly-reduced ubiquitin 6+ do not show a temperature dependence to their formation, consistent with these ions being formed by nonergodic processes.
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