ArticleJournal of the American Society for Mass Spectrometry2012
Supercharging with trivalent metal ions in native mass spectrometry.
Article in Journal of the American Society for Mass Spectrometry, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 11 papers.
What it found
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Who cites it
11 citing papers in PubMed, 26 citations in OpenAlex.
- Charge Reduction of Membrane Proteins in Native Mass Spectrometry Using Alkali Metal Acetate Salts.Analytical chemistry · 2020Article
- 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
- Increasing protein charge state when using laser electrospray mass spectrometry.Journal of the American Society for Mass Spectrometry · 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
- Article
- What protein charging (and supercharging) reveal about the mechanism of electrospray ionization.Journal of the American Society for Mass Spectrometry · 2014Article
- Effects of cations on protein and peptide charging in electrospray ionization from aqueous solutions.Journal of the American Society for Mass Spectrometry · 2014Article
- Effects of metal ion adduction on the gas-phase conformations of protein ions.Journal of the American Society for Mass Spectrometry · 2013Article
Corrections and comments
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Authors and funding
2 authors at 1 institution in 1 country.
Funding
Abstract
Addition of 1.0 mM LaCl(3) to aqueous ammonium acetate solutions containing proteins in their folded native forms can result in a significant increase in the molecular ion charging obtained with electrospray ionization as a result of cation adduction. In combination with m-nitrobenzyl alcohol, molecular ion charge states that are greater than the number of basic sites in the protein can be produced from these native solutions, even for lysozyme, which is conformationally constrained by four intramolecular disulfide bonds. Circular dichroism spectroscopy indicates that the conformation of ubiquitin is not measurably affected with up to 1.0 M LaCl(3), but ion mobility data indicate that the high charge states that are formed when 1.0 mM LaCl(3) is present are more unfolded than the low charge states formed without this reagent. These and other results indicate that the increased charging is a result of La(3+) preferentially adducting onto compact or more native-like conformers during ESI and the gas-phase ions subsequently unfolding as a result of increased Coulomb repulsion. Electron capture dissociation of these high charge-state ions formed from these native solutions results in comparable sequence coverage to that obtained for ions formed from denaturing solutions without supercharging reagents, making this method a potentially powerful tool for obtaining structural information in native 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.