ArticleJournal of the American Society for Mass Spectrometry2010
Effects of supercharging reagents on noncovalent complex structure in electrospray ionization from aqueous solutions.
Article in Journal of the American Society for Mass Spectrometry, 2010. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 55 papers.
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Who cites it
55 citing papers in PubMed, 120 citations in OpenAlex.
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- Triboelectric Nanogenerators: Low-Cost Power Supplies for Improved Electrospray Ionization.International journal of mass spectrometry · 2024Article
- Approaches to Heterogeneity in Native Mass Spectrometry.Chemical reviews · 2022Review
- Current perspectives on supercharging reagents in electrospray ionization mass spectrometry.RSC advances · 2021Review
- Structural Characterization of Carbonic Anhydrase-Arylsulfonamide Complexes Using Ultraviolet Photodissociation Mass Spectrometry.Journal of the American Society for Mass Spectrometry · 2021Article
- Charge Manipulation Using Solution and Gas-Phase Chemistry to Facilitate Analysis of Highly Heterogeneous Protein Complexes in Native Mass Spectrometry.Analytical chemistry · 2021Article
- A kinetic description of how interfaces accelerate reactions in micro-compartments.Chemical science · 2020Article
- On the mechanism of protein supercharging in electrospray ionisation mass spectrometry: Effects on charging of additives with short- and long-chain alkyl constituents with carbonate and sulphite terminal groups.Analytica chimica acta: X · 2019Article
- Chemical Additives Enable Native Mass Spectrometry Measurement of Membrane Protein Oligomeric State within Intact Nanodiscs.Journal of the American Chemical Society · 2019Article
- Corona Discharge Suppression in Negative Ion Mode Nanoelectrospray Ionization via Trifluoroethanol Addition.Analytical chemistry · 2017Article
- Photoelectron Transfer Dissociation Reveals Surprising Favorability of Zwitterionic States in Large Gaseous Peptides and Proteins.Journal of the American Chemical Society · 2017Article
- Interpreting the Collision Cross Sections of Native-like Protein Ions: Insights from Cation-to-Anion Proton-Transfer Reactions.Analytical chemistry · 2017Article
- A Comprehensive Guide for Performing Sample Preparation and Top-Down Protein Analysis.Proteomes · 2017Review
- On the preservation of non-covalent protein complexes during electrospray ionization.Philosophical transactions. Series A, Mathematical, physical, and engineering sciences · 2016Article
- Real-time HD Exchange Kinetics of Proteins from Buffered Aqueous Solution with Electrothermal Supercharging and Top-Down Tandem Mass Spectrometry.Journal of the American Society for Mass Spectrometry · 2016Article
- Influence of Sulfolane on ESI-MS Measurements of Protein-Ligand Affinities.Journal of the American Society for Mass Spectrometry · 2016Article
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Authors and funding
7 authors at 2 institutions in 1 country.
Funding
Abstract
The effects of two supercharging reagents, m-nitrobenzyl alcohol (m-NBA) and sulfolane, on the charge-state distributions and conformations of myoglobin ions formed by electrospray ionization were investigated. Addition of 0.4% m-NBA to aqueous ammonium acetate solutions of myoglobin results in an increase in the maximum charge state from 9+ to 19+, and an increase in the average charge state from 7.9+ to 11.7+, compared with solutions without m-NBA. The extent of supercharging with sulfolane on a per mole basis is lower than that with m-NBA, but comparable charging was obtained at higher concentration. Arrival time distributions obtained from traveling wave ion mobility spectrometry show that the higher charge state ions that are formed with these supercharging reagents are significantly more unfolded than lower charge state ions. Results from circular dichroism spectroscopy show that sulfolane can act as chemical denaturant, destabilizing myoglobin by ∼1.5 kcal/mol/M at 25°C. Because these supercharging reagents have low vapor pressures, aqueous droplets are preferentially enriched in these reagents as evaporation occurs. Less evaporative cooling will occur after the droplets are substantially enriched in the low volatility supercharging reagent, and the droplet temperature should be higher compared with when these reagents are not present. Protein unfolding induced by chemical and/or thermal denaturation in the electrospray droplet appears to be the primary origin of the enhanced charging observed for noncovalent protein complexes formed from aqueous solutions that contain these supercharging reagents, although other factors almost certainly influence the extent of charging as well.
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