ArticleAnalytical chemistry2011
Negative electrospray droplet exposure to gaseous bases for the manipulation of protein charge state distributions.
Article in Analytical chemistry, 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 22 papers.
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Who cites it
22 citing papers in PubMed, 61 citations in OpenAlex.
- Dynamic Additive Scanning for Precise Control in Electrospray Ionization Mass Spectrometry.ACS measurement science au · 2026Article
- Proton transfer reagent cations for ion-ion charge state manipulation of high mass negatively-charged analytes in an electrodynamic ion trap.The Analyst · 2026Article
- FlexESI: An Automated Vapor-Switching Interface for Enhanced Flexibility and Sensitivity in Electrospray Ionization.ACS measurement science au · 2025Article
- Precursor Resolution via Ion Z-State Manipulation: A Tandem Mass Spectrometry Approach for the Analysis of Mixtures of Multiply-Charged Ions.Journal of mass spectrometry : JMS · 2025Review
- Digital Ion Trap Isolation and Mass Analysis of Macromolecular Analytes with Multiply Charged Ion Attachment.Journal of the American Society for Mass Spectrometry · 2024Article
- Single-Frequency Ion Parking in a Digital 3D Quadrupole Ion Trap.International journal of mass spectrometry · 2024Article
- Ion parking in native mass spectrometry.The Analyst · 2024Article
- Electrospray Photochemical Oxidation of Proteins.Journal of the American Society for Mass Spectrometry · 2019Article
- Capillary HILIC-MS: A New Tool for Sensitive Top-Down Proteomics.Analytical chemistry · 2018Article
- Gas-Phase Stability of Negatively Charged Organophosphate Metabolites Produced by Electrospray Ionization and Matrix-Assisted Laser Desorption/Ionization.Journal of the American Society for Mass Spectrometry · 2017Article
- Charging of Proteins in Native Mass Spectrometry.Journal of the American Society for Mass Spectrometry · 2017Article
- Electrothermal supercharging of proteins in native MS: effects of protein isoelectric point, buffer, and nanoESI-emitter tip size.The Analyst · 2016Article
- New supercharging reagents produce highly charged protein ions in native mass spectrometry.The Analyst · 2015Article
- High-throughput bioconjugation for enhanced 193 nm photodissociation via droplet phase initiated ion/ion chemistry using a front-end dual spray reactor.Analytical chemistry · 2015Article
- Investigating protein folding and unfolding in electrospray nanodrops upon rapid mixing using theta-glass emitters.Analytical chemistry · 2015Article
- On-line desalting of crude oil in the source region of a Fourier transform ion cyclotron resonance mass spectrometer.Journal of the American Society for Mass Spectrometry · 2014Article
- Electrothermal supercharging in mass spectrometry and tandem mass spectrometry of native proteins.Analytical chemistry · 2013Article
- Electrospray ionization-induced protein unfolding.Journal of the American Society for Mass Spectrometry · 2012Article
- Basic vapor exposure for tuning the charge state distribution of proteins in negative electrospray ionization: elucidation of mechanisms by fluorescence spectroscopy.Journal of the American Society for Mass Spectrometry · 2012Article
- Electrothermal supercharging of proteins in native electrospray ionization.Analytical chemistry · 2012Article
Corrections and comments
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Authors and funding
2 authors at 1 institution in 1 country.
Funding
Abstract
The exposure of electrospray droplets to vapors of reagents of various base strengths affects protein negative charge state distributions independent of initial solution conditions. Volatile bases are introduced into the counter-current nitrogen drying gas of an electrospray interface to interact with charged droplets as they undergo desolvation/disintegration, shifting charge state distributions of proteins to higher, more negative, charge states. Alterations of charge state distributions can implicate protein folding/unfolding phenomena. Species bound by relatively weak interactions can be preserved, at least to some extent, allowing for the observation of high charge states of protein-ligand complexes, such as high negative charge states of holomyoglobin. The binding of carbonic anhydrase with its Zn(2+) cofactor is apparently preserved when the holo-form of the protein is exposed to basic vapors (i.e., the Zn(2+) ion remains associated with the protein), but this prevents the appearance of charge states higher than -17. Charge state distributions of proteins containing disulfide bonds shift slightly with the leak-in of basic vapors, but when these disulfide bonds are reduced with dithiothreitol in solution, charge states higher than the number of acidic sites (Asp, Glu, and C-terminus) are observed. Since there is no observed change in the distributions of buffered proteins exposed to these reagent vapors, the charge state changes are attributed largely to a pH affect. High pK(a) and highly volatile reagents have been found to be the most effective in terms of observing the maximum negative charge state of the biomolecule of interest.
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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.