ArticleJournal of the American Society for Mass Spectrometry2009
Modifying the charge state distribution of proteins in electrospray ionization mass spectrometry by chemical derivatization.
Article in Journal of the American Society for Mass Spectrometry, 2009. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 34 papers.
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Who cites it
34 citing papers in PubMed.
- Impact of Supercharging on Top-Down Characterization of Monoclonal Antibodies by Collision Induced Dissociation.International journal of mass spectrometry · 2026Article
- Native mass spectrometry enabled by infrared matrix-assisted laser desorption electrospray ionization for rapid measurement of protein-ligand biophysical parameters.Analytical and bioanalytical chemistry · 2026Article
- High-throughput screening of fentanyl analogs.Talanta · 2025Article
- Molecular Dynamics Simulations of Native Protein Charging via Proton Transfer during Electrospray Ionization with Grotthuss Diffuse HAnalytical chemistry · 2024Article
- Uncovering Distinct Peptide Charging Behaviors in Electrospray Ionization Mass Spectrometry Using a Large-Scale Dataset.Journal of the American Society for Mass Spectrometry · 2024Article
- A high-throughput approach reveals distinct peptide charging behaviors in electrospray ionization mass spectrometry.bioRxiv : the preprint server for biology · 2023Article
- Free Radical-Based Sequencing for Native Top-Down Mass Spectrometry.Journal of the American Society for Mass Spectrometry · 2022Article
- Proteomics as a tool to gain next level insights into photo-crosslinkable biopolymer modifications.Bioactive materials · 2022Article
- Novel Isobaric Tagging Reagent Enabled Multiplex Quantitative Glycoproteomics via Electron-Transfer/Higher-Energy Collisional Dissociation (EThcD) Mass Spectrometry.Journal of the American Society for Mass Spectrometry · 2022Article
- Enhancement of sensitivity and quantification quality in the LC-MS/MS measurement of large biomolecules with sum of MRM (SMRM).Analytical and bioanalytical chemistry · 2022Article
- Native mass spectrometry of human carbonic anhydrase I and its inhibitor complexes.Journal of biological inorganic chemistry : JBIC : a publication of the Society of Biological Inorganic Chemistry · 2020Article
- Current LC-MS-based strategies for characterization and quantification of antibody-drug conjugates.Journal of pharmaceutical analysis · 2020Review
- Quantitation of Super Basic Peptides in Biological Matrices by a Generic Perfluoropentanoic Acid-Based Liquid Chromatography-Mass Spectrometry Method.Journal of the American Society for Mass Spectrometry · 2019Article
- Top-Down Analysis of Proteins in Low Charge States.Journal of the American Society for Mass Spectrometry · 2019Article
- Fixed-Charge Trimethyl Pyrilium Modification for Enabling Enhanced Top-Down Mass Spectrometry Sequencing of Intact Protein Complexes.Analytical chemistry · 2018Article
- Maillard Proteomics: Opening New Pages.International journal of molecular sciences · 2017Review
- The Impact of Phosphorylation on Electron Capture Dissociation of Proteins: A Top-Down Perspective.Journal of the American Society for Mass Spectrometry · 2017Article
- Modulation of Protein Fragmentation Through Carbamylation of Primary Amines.Journal of the American Society for Mass Spectrometry · 2017Article
- Salt Bridge Rearrangement (SaBRe) Explains the Dissociation Behavior of Noncovalent Complexes.Journal of the American Society for Mass Spectrometry · 2016Article
- Comparison of Ultraviolet Photodissociation and Collision Induced Dissociation of Adrenocorticotropic Hormone Peptides.Journal of the American Society for Mass Spectrometry · 2015Article
Corrections and comments
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Authors and funding
4 authors.
Funding
Abstract
Electrospray ionization (ESI) of denatured proteins produces a broad distribution of multiply-charged ions leading to multiple peaks in the mass spectrum. We investigated changes in the positive-mode ESI charge state distribution produced by several chemical modifications of denatured proteins. Capping carboxylic acid groups with neutral functional groups yields little change in charge state distribution compared with unmodified proteins. The results indicate that carboxyl groups do not play a significant role in the positive charging of denatured proteins in ESI. The modification of proteins with additional basic sites or fixed positive charges generates substantially higher charge states, providing evidence that the number of ionizable sites, rather than molecular size and shape, determines ESI charging for denatured proteins. Fixed charge modification also significantly reduces the number of protons acquired by a protein, in that the charge state envelope is not increased by the full number of fixed charges appended. This result demonstrates that Coulombic repulsion between positive charges plays a significant role in determining charge state distribution by affecting the gas-phase basicity of ionizable sites. Addition of fixed-charge moieties to a protein is a useful approach for shifting protein charge state distributions to higher charge states, and with further work, it may help limit the distribution of protein ions to fewer charge states.
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