ArticleJournal of the American Society for Mass Spectrometry2011
Effects of select anions from the Hofmeister series on the gas-phase conformations of protein ions measured with traveling-wave ion mobility spectrometry/mass spectrometry.
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 14 papers.
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Who cites it
14 citing papers in PubMed, 47 citations in OpenAlex.
- Protons Are Fast and Smart; Proteins Are Slow and Dumb: On the Relationship of Electrospray Ionization Charge States and Conformations.Journal of the American Society for Mass Spectrometry · 2021Article
- Probing Protein Denaturation during Size-Exclusion Chromatography Using Native Mass Spectrometry.Analytical chemistry · 2020Article
- 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
- Unfolding and Folding of the Three-Helix Bundle Protein KIX in the Absence of Solvent.Journal of the American Society for Mass Spectrometry · 2016Article
- Characterization of Traveling Wave Ion Mobility Separations in Structures for Lossless Ion Manipulations.Analytical chemistry · 2015Article
- Effects of cations on protein and peptide charging in electrospray ionization from aqueous solutions.Journal of the American Society for Mass Spectrometry · 2014Article
- Anions in electrothermal supercharging of proteins with electrospray ionization follow a reverse Hofmeister series.Analytical chemistry · 2014Article
- Effects of metal ion adduction on the gas-phase conformations of protein ions.Journal of the American Society for Mass Spectrometry · 2013Article
- Hofmeister salts recover a misfolded multiprotein complex for subsequent structural measurements in the gas phase.Angewandte Chemie (International ed. in English) · 2013Article
- Traveling-wave Ion Mobility-Mass Spectrometry Reveals Additional Mechanistic Details in the Stabilization of Protein Complex Ions through Tuned Salt Additives.International journal for ion mobility spectrometry : official publication of the International Society for Ion Mobility Spectrometry · 2013Article
- Dramatically stabilizing multiprotein complex structure in the absence of bulk water using tuned Hofmeister salts.Faraday discussions · 2013Article
- Solution additives that desalt protein ions in native mass spectrometry.Analytical chemistry · 2012Article
- Bound cations significantly stabilize the structure of multiprotein complexes in the gas phase.Angewandte Chemie (International ed. in English) · 2012Article
- How hot are your ions in TWAVE ion mobility spectrometry?Journal of the American Society for Mass Spectrometry · 2012Article
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Authors and funding
4 authors at 2 institutions in 1 country.
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Abstract
The gas-phase conformations of ubiquitin, cytochrome c, lysozyme, and α-lactalbumin ions, formed by electrospray ionization (ESI) from aqueous solutions containing 5 mM ammonium perchlorate, ammonium iodide, ammonium sulfate, ammonium chloride, ammonium thiocyanate, or guanidinium chloride, are examined using traveling-wave ion mobility spectrometry (TWIMS) coupled to time-of-flight (TOF) mass spectrometry (MS). For ubiquitin, cytochrome c, and α-lactalbumin, adduction of multiple acid molecules results in no significant conformational changes to the highest and lowest charge states formed from aqueous solutions, whereas the intermediate charge states become more compact. The transition to more compact conformers for the intermediate charge states occurs with fewer bound H(2)SO(4) molecules than HClO(4) or HI molecules, suggesting ion-ion or salt-bridge interactions are stabilizing more compact forms of the gaseous protein. However, the drift time distributions for protein ions of the same net charge with the highest levels of adduction of each acid are comparable, indicating that these protein ions all adopt similarly compact conformations or families of conformers. No significant change in conformation is observed upon the adduction of multiple acid molecules to charge states of lysozyme. These results show that the attachment of HClO(4), HI, or H(2)SO(4) to multiply protonated proteins can induce compact conformations in the resulting gas-phase protein ions. In contrast, differing Hofmeister effects are observed for the corresponding anions in solution at higher concentrations.
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