ArticleAnalytical chemistry2013
Electrothermal supercharging in mass spectrometry and tandem mass spectrometry of native proteins.
Article in Analytical chemistry, 2013. 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, 59 citations in OpenAlex.
- Unraveling Ribonucleic Acid Unfolding: A Quantitative Comparison of Solution and Gas-Phase Unfolding.Analytical chemistry · 2025Article
- Protons Are Fast and Smart; Proteins Are Slow and Dumb: On the Relationship of Electrospray Ionization Charge States and Conformations.Journal of the American Society for Mass Spectrometry · 2021Article
- Cadmium Exchange with Zinc in the Non-Classical Zinc Finger Protein Tristetraprolin.Inorganic chemistry · 2021Article
- Chiral Tartaric Acid Improves Fracture Toughness of Bioactive Brushite-Collagen Bone Cements.ACS applied bio materials · 2020Article
- Fragmentation of Multi-charged Derivatized Lysine Using Nanospray CID Tandem Mass Spectrometry.Journal of the American Society for Mass Spectrometry · 2019Article
- The Role of Electron Transfer Dissociation in Modern Proteomics.Analytical chemistry · 2018Review
- OH-Radical Oxidation of Lung Surfactant Protein B on Aqueous Surfaces.Mass spectrometry (Tokyo, Japan) · 2018Article
- 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
- Mechanistic and Kinetic Study of Singlet O2 Oxidation of Methionine by On-Line Electrospray Ionization 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
- Investigating protein folding and unfolding in electrospray nanodrops upon rapid mixing using theta-glass emitters.Analytical chemistry · 2015Article
- Effects of cations on protein and peptide charging in electrospray ionization from aqueous solutions.Journal of the American Society for Mass Spectrometry · 2014Article
- Soft supercharging of biomolecular ions in electrospray ionization mass spectrometry.Journal of the American Society for Mass Spectrometry · 2014Article
- Anions in electrothermal supercharging of proteins with electrospray ionization follow a reverse Hofmeister series.Analytical chemistry · 2014Article
- Intact protein mass spectrometry and top-down proteomics.Expert review of proteomics · 2013Article
Corrections and comments
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Authors and funding
4 authors at 1 institution in 1 country.
Funding
Abstract
Electrothermal supercharging of protein ions formed by electrospray ionization from buffered aqueous solutions results in significant increases to both the maximum and average charge states compared to native mass spectrometry in which ions are formed from the same solutions but with lower spray potentials. For eight of the nine proteins investigated, the maximum charge states of protonated ions formed from native solutions with electrothermal supercharging is greater than those obtained from conventional denaturing solutions consisting of water/methanol/acid, although the average charging is slightly lower owing to contributions of small populations of more folded low charge-state structures. Under these conditions, electrothermal supercharging is slightly less effective for anions than for cations. Equivalent sequence coverage (80%) is obtained with electron transfer dissociation of the same high charge-state ion of cytochrome c formed by electrothermal supercharging from native solutions and from denaturing solutions. Electrothermal supercharging should be advantageous for combining structural studies of proteins in native environments with mass spectrometers that have limited high m/z capabilities and for significantly improving tandem mass spectrometry performance for protein ions formed from solutions in which the molecules have native structures and activities.
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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.