ArticleAnalytical chemistry2012
Electrothermal supercharging of proteins in native electrospray ionization.
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 31 papers.
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Who cites it
31 citing papers in PubMed, 83 citations in OpenAlex.
- Zero-Potential No-Discharge APCI Combined With pH and Colorimetric Measurements Reveals a Protein-Dependent Change in Albumin Proton Affinity Under Quantum-Dot Patch Exposure.Journal of mass spectrometry : JMS · 2026Article
- The Role of Nanobubbles in Protein Unfolding during Electrothermal Supercharging.Journal of the American Society for Mass Spectrometry · 2025Article
- Nanobubbles in Electrospray Ionization Mass Spectrometry.Analytical chemistry · 2025Article
- Effects of Nano-Electrospray Ionization Emitter Position on Unintentional In-Source Activation of Peptide and Protein Ions.Journal of the American Society for Mass Spectrometry · 2024Article
- Approaches to Heterogeneity in Native Mass Spectrometry.Chemical reviews · 2022Review
- Surface-induced Dissociation Mass Spectrometry as a Structural Biology Tool.Chemical reviews · 2022Review
- Current perspectives on supercharging reagents in electrospray ionization mass spectrometry.RSC advances · 2021Review
- Structural Properties and Catalytic Implications of the SPASM Domain Iron-Sulfur Clusters inJournal of the American Chemical Society · 2020Article
- Probing Protein Denaturation during Size-Exclusion Chromatography Using Native Mass Spectrometry.Analytical chemistry · 2020Article
- Structural Analysis of the Effect of a Dual-FLAG Tag on Transthyretin.Biochemistry · 2020Article
- The chemical reactions in electrosprays of water do not always correspond to those at the pristine air-water interface.Chemical science · 2019Article
- Protein-Glass Surface Interactions and Ion Desalting in Electrospray Ionization with Submicron Emitters.Journal of the American Society for Mass Spectrometry · 2018Article
- Joule Heating and Thermal Denaturation of Proteins in Nano-ESI Theta Tips.Journal of the American Society for Mass Spectrometry · 2017Article
- Ammonium Bicarbonate Addition Improves the Detection of Proteins by Desorption Electrospray Ionization Mass Spectrometry.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
- 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
- New supercharging reagents produce highly charged protein ions in native mass spectrometry.The Analyst · 2015Article
- Supercharging with m-nitrobenzyl alcohol and propylene carbonate: forming highly charged ions with extended, near-linear conformations.Analytical chemistry · 2015Article
- The use of chromium(III) to supercharge peptides by protonation at low basicity sites.Journal of the American Society for Mass Spectrometry · 2015Article
Corrections and comments
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Authors and funding
4 authors at 1 institution in 1 country.
Funding
Abstract
The formation of high charge-state protein ions with nanoelectrospray ionization (nESI) from purely aqueous ammonium bicarbonate solutions at neutral pH, where the proteins have native or native-like conformations prior to ESI droplet formation, is demonstrated. This "electrothermal" supercharging method depends on the temperature of the instrument entrance capillary, the nESI spray potential, and the solution ionic strength and buffer, although other factors almost certainly contribute. Mass spectra obtained with electrothermal supercharging appear similar to those obtained from denaturing solutions where charging beyond the total number of basic sites can be achieved. For example, a 17+ ion of bovine ubiquitin was formed by nESI of a 100 mM ammonium bicarbonate, pH 7.0, solution, which is three more charges than the total number of basic amino acids plus the N-terminus. Heating of the ESI droplets in the vacuum/atmosphere interface and the concomitant denaturation of the protein in the ESI droplets prior to ion formation appears to be the primary origin of the very high charge-state ions formed from these purely aqueous, buffered solutions. nESI mass spectra resembling those obtained under traditional native or denaturing conditions can be reversibly obtained simply by toggling the spray voltage between low and high values.
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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.