ArticleJournal of the American Society for Mass Spectrometry2014
Effects of cations on protein and peptide charging in electrospray ionization from aqueous solutions.
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 14 papers.
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Who cites it
14 citing papers in PubMed, 24 citations in OpenAlex.
- PNGaseF-Generated N-Glycans Adduct onto Peptides in the Gas Phase.Journal of the American Society for Mass Spectrometry · 2025Article
- Effects of Molecular Size on Resolution in Charge Detection Mass Spectrometry.Analytical chemistry · 2022Article
- Direct observation of ion emission from charged aqueous nanodrops: effects on gaseous macromolecular charging.Chemical science · 2021Article
- Study on the Inhibitory Activity of a Synthetic Defensin Derived from Barley Endosperm against Common Food Spoilage Yeast.Molecules (Basel, Switzerland) · 2020Article
- Stoichiometry of Nucleotide Binding to Proteasome AAA+ ATPase Hexamer Established by Native Mass Spectrometry.Molecular & cellular proteomics : MCP · 2020Article
- Probing Protein Denaturation during Size-Exclusion Chromatography Using Native Mass Spectrometry.Analytical chemistry · 2020Article
- Gas-Phase Collisions with Trimethylamine-N-Oxide Enable Activation-Controlled Protein Ion Charge Reduction.Journal of the American Society for Mass Spectrometry · 2019Article
- OH-Radical Oxidation of Lung Surfactant Protein B on Aqueous Surfaces.Mass spectrometry (Tokyo, Japan) · 2018Article
- Characterization of Intramolecular Interactions of Cytochrome c Using Hydrogen-Deuterium Exchange-Trapped Ion Mobility Spectrometry-Mass Spectrometry and Molecular Dynamics.Analytical chemistry · 2017Article
- Addressing a Common Misconception: Ammonium Acetate as Neutral pH "Buffer" for Native Electrospray Mass Spectrometry.Journal of the American Society for Mass Spectrometry · 2017Article
- Influence of Alkylammonium Acetate Buffers on Protein-Ligand Noncovalent Interactions Using Native Mass Spectrometry.Journal of the American Society for Mass Spectrometry · 2017Article
- Theoretical predictor for candidate structure assignment from IMS data of biomolecule-related conformational space.International journal for ion mobility spectrometry : official publication of the International Society for Ion Mobility Spectrometry · 2015Article
- Supercharging with m-nitrobenzyl alcohol and propylene carbonate: forming highly charged ions with extended, near-linear conformations.Analytical chemistry · 2015Article
- Kinetic intermediates of holo- and apo-myoglobin studied using HDX-TIMS-MS and molecular dynamic simulations.Journal of the American Society for Mass Spectrometry · 2015Article
Corrections and comments
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Authors and funding
3 authors at 1 institution in 1 country.
Funding
Abstract
The effects of eight different cations with ionic radii between 69 and 337 pm on the charging of peptides and proteins with electrospray ionization from aqueous acetate salt solutions are reported. Significant adduction occurs for all cations except NH4(+), and the average protein charge is lower when formed from solutions containing salts compared with solutions without salts added. Circular dichroism and ion mobility results show the protein conformations are different in pure water compared with salt solutions, which likely affects the extent of charging. The average charge of protein and peptide ions formed from solutions with Li(+) and Cs(+), which have Gibbs solvation free energies (GSFEs) that differ by 225 kJ/mol, is similar. Lower charge states are typically formed from solutions with tetramethylammonium and tetraethylammonium that have lower GSFE values. Loss of the larger cations that have the lowest GSFEs is facile when adducted protein ions are collisionally activated, resulting in the formation of lower analyte charge states. This reaction pathway provides a route to produce abundant singly protonated protein ions under native mass spectrometry conditions. The average protein and peptide charge with NH4(+) is nearly the same as that with Rb(+) and K(+), cations with similar GSFE and ionic radii. This indicates that proton transfer from NH4(+) to proteins plays an insignificant role in the extent of protein charging in native mass spectrometry.
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Registered trials
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.