ArticleJournal of the American Society for Mass Spectrometry2014
Solution dependence of the collisional activation of ubiquitin [M + 7H](7+) ions.
Article in Journal of the American Society for Mass Spectrometry, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 23 papers.
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Who cites it
23 citing papers in PubMed, 50 citations in OpenAlex.
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- Ion Mobility and Gas-Phase Covalent Labeling Study of the Structure and Reactivity of Gaseous Ubiquitin Ions Electrosprayed from Aqueous and Denaturing Solutions.Journal of the American Society for Mass Spectrometry · 2020Article
- Characterizing Thermal Transitions of IgG with Mass Spectrometry.Journal of the American Society for Mass Spectrometry · 2019Article
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- Characterization of hydrogen bonding motifs in proteins: hydrogen elimination monitoring by ultraviolet photodissociation mass spectrometry.Physical chemistry chemical physics : PCCP · 2017Article
- From Compact to String-The Role of Secondary and Tertiary Structure in Charge-Induced Unzipping of Gas-Phase Proteins.Journal of the American Society for Mass Spectrometry · 2017Article
- Action-FRET of a Gaseous Protein.Journal of the American Society for Mass Spectrometry · 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
- Towards the Analysis of High Molecular Weight Proteins and Protein complexes using TIMS-MS.International journal for ion mobility spectrometry : official publication of the International Society for Ion Mobility Spectrometry · 2016Article
- Folding of Protein Ions in the Gas Phase after Cation-to-Anion Proton-Transfer Reactions.Journal of the American Chemical Society · 2016Article
- Charge, Color, and Conformation: Spectroscopy on Isomer-Selected Peptide Ions.The journal of physical chemistry. B · 2016Article
- Charge site assignment in native proteins by ultraviolet photodissociation (UVPD) mass spectrometry.The Analyst · 2016Article
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Authors and funding
4 authors at 3 institutions in 2 countries.
Funding
Abstract
The solution dependence of gas-phase unfolding for ubiquitin [M + 7H](7+) ions has been studied by ion mobility spectrometry-mass spectrometry (IMS-MS). Different acidic water:methanol solutions are used to favor the native (N), more helical (A), or unfolded (U) solution states of ubiquitin. Unfolding of gas-phase ubiquitin ions is achieved by collisional heating and newly formed structures are examined by IMS. With an activation voltage of 100 V, a selected distribution of compact structures unfolds, forming three resolvable elongated states (E1-E3). The relative populations of these elongated structures depend strongly on the solution composition. Activation of compact ions from aqueous solutions known to favor N-state ubiquitin produces mostly the E1 type elongated state, whereas activation of compact ions from methanol containing solutions that populate A-state ubiquitin favors the E3 elongated state. Presumably, this difference arises because of differences in precursor ion structures emerging from solution. Thus, it appears that information about solution populations can be retained after ionization, selection, and activation to produce the elongated states. These data as well as others are discussed.
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