ArticleThe Analyst2016
Electrothermal supercharging of proteins in native MS: effects of protein isoelectric point, buffer, and nanoESI-emitter tip size.
Article in The Analyst, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 9 papers.
What it found
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The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
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Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.
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Who cites it
9 citing papers in PubMed.
- Unraveling Ribonucleic Acid Unfolding: A Quantitative Comparison of Solution and Gas-Phase Unfolding.Analytical chemistry · 2025Article
- Tunable Heteroassembly of a Plant Pseudoenzyme-Enzyme Complex.ACS chemical biology · 2021Article
- Rapid structural discrimination of IgG antibodies by multicharge-state collision-induced unfolding.RSC advances · 2021Article
- Native Mass Spectrometry of Membrane Proteins.Analytical chemistry · 2021Review
- Probing Protein Denaturation during Size-Exclusion Chromatography Using Native Mass Spectrometry.Analytical chemistry · 2020Article
- Ion Mobility and Surface Collisions: Submicrometer Capillaries Can Produce Native-like Protein Complexes.Analytical chemistry · 2020Article
- Protein-Glass Surface Interactions and Ion Desalting in Electrospray Ionization with Submicron Emitters.Journal of the American Society for Mass Spectrometry · 2018Article
- Submicrometer Emitter ESI Tips for Native Mass Spectrometry of Membrane Proteins in Ionic and Nonionic Detergents.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
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
2 authors.
Funding
Abstract
The extent of charging resulting from electrothermal supercharging for protein ions formed from various buffered aqueous solutions using nanoESI emitters with tip diameters between ∼1.5 μm and ∼310 nm is compared. Charging increases with decreasing tip size for proteins that are positively charged in solution but not for proteins that are negatively charged in solution. These results suggest that Coulombic attraction between positively charged protein molecules and the negatively charged glass surfaces in the tips of the emitters causes destabilization and even unfolding of proteins prior to nanoESI. Coulombic attraction to the negatively charged glass surfaces does not occur for negatively charged proteins and the extent of charging with electrothermal supercharging decreases with decreasing tip size. Smaller droplets are formed with smaller tips, and these droplets have shorter lifetimes for protein unfolding with electrothermal supercharging to occur prior to gaseous ion formation. Results from this study demonstrate simple principles to consider in order to optimize the extent of charging obtained with electrothermal supercharging, which should be useful for obtaining more structural information in tandem mass spectrometry.
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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.