ArticleAnalytical chemistry2012
Electrochemistry-assisted top-down characterization of disulfide-containing proteins.
Article in Analytical chemistry, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 30 papers.
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Who cites it
30 citing papers in PubMed.
- Absolute Quantitation of Peptides and Proteins by Coulometric Mass Spectrometry After Derivatization.International journal of mass spectrometry · 2024Article
- Top-down mass spectrometry and assigning internal fragments for determining disulfide bond positions in proteins.The Analyst · 2022Article
- Electrocatalytic redox neutral [3 + 2] annulation ofChemical science · 2020Article
- Top-Down Analysis of Disulfide-Linked Proteins Using Photoinduced Radical Reactions and ET-DDC.International journal of mass spectrometry · 2019Article
- A New Quantification Method Using Electrochemical Mass Spectrometry.Journal of the American Society for Mass Spectrometry · 2019Article
- Characterization of Protein Disulfide Linkages by MS In-Source Dissociation Comparing to CID and ETD Tandem MS.Journal of the American Society for Mass Spectrometry · 2019Article
- Acetone/Isopropanol Photoinitiating System Enables Tunable Disulfide Reduction and Disulfide Mapping via Tandem Mass Spectrometry.Analytical chemistry · 2018Article
- Top-Down Characterization of Proteins with Intact Disulfide Bonds Using Activated-Ion Electron Transfer Dissociation.Analytical chemistry · 2018Article
- Custom selenoprotein production enabled by laboratory evolution of recoded bacterial strains.Nature biotechnology · 2018Article
- Assigning Peptide Disulfide Linkage Pattern Among Regio-Isomers via Methoxy Addition to Disulfide and Tandem Mass Spectrometry.Journal of the American Society for Mass Spectrometry · 2017Article
- Selective Gas-Phase Ion/Ion Reactions: Enabling Disulfide Mapping via Oxidation and Cleavage of Disulfide Bonds in Intermolecularly-Linked Polypeptide Ions.Analytical chemistry · 2016Article
- Probing Protein 3D Structures and Conformational Changes Using Electrochemistry-Assisted Isotope Labeling Cross-Linking Mass Spectrometry.Journal of the American Society for Mass Spectrometry · 2016Article
- In-Depth Characterization of Protein Disulfide Bonds by Online Liquid Chromatography-Electrochemistry-Mass Spectrometry.Journal of the American Society for Mass Spectrometry · 2016Article
- Enhancing Performance of Liquid Sample Desorption Electrospray Ionization Mass Spectrometry Using Trap and Capillary Columns.International journal of mass spectrometry · 2015Article
- Screening Method for the Discovery of Potential Bioactive Cysteine-Containing Peptides Using 3D Mass Mapping.Journal of the American Society for Mass Spectrometry · 2015Article
- Enhancing Protein Disulfide Bond Cleavage by UV Excitation and Electron Capture Dissociation for Top-Down Mass Spectrometry.International journal of mass spectrometry · 2015Article
- Paper-Based Electrochemical Cell Coupled to Mass Spectrometry.Journal of the American Society for Mass Spectrometry · 2015Article
- Online Investigation of Aqueous-Phase Electrochemical Reactions by Desorption Electrospray Ionization Mass Spectrometry.Journal of the American Society for Mass Spectrometry · 2015Article
- Mechanisms and energetics of free radical initiated disulfide bond cleavage in model peptides and insulin by mass spectrometry.Chemical science · 2015Article
- Integration of electrochemistry with ultra-performance liquid chromatography/mass spectrometry.European journal of mass spectrometry (Chichester, England) · 2015Article
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5 authors.
Funding
Abstract
Covalent disulfide bond linkage in a protein represents an important challenge for mass spectrometry (MS)-based top-down protein structure analysis as it reduces the backbone cleavage efficiency for MS/MS dissociation. This study presents a strategy for solving this critical issue via integrating electrochemistry (EC) online with a top-down MS approach. In this approach, proteins undergo electrolytic reduction in an electrochemical cell to break disulfide bonds and then undergo online ionization into gaseous ions for analysis by electron-capture dissociation (ECD) and collision-induced dissociation (CID). The electrochemical reduction of proteins allows one to remove disulfide bond constraints and also leads to increased charge numbers of the resulting protein ions. As a result, sequence coverage was significantly enhanced, as exemplified by β-lactoglobulin A (24 vs 75 backbone cleavages before and after electrolytic reduction, respectively) and lysozyme (5 vs 66 backbone cleavages before and after electrolytic reduction, respectively). This methodology is fast and does not need chemical reductants, which would have an important impact in high-throughput proteomics research.
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