ArticleJournal of the American Society for Mass Spectrometry2008
Conformations of gas-phase ions of ubiquitin, cytochrome c, apomyoglobin, and beta-lactoglobulin produced from two different solution conformations.
Article in Journal of the American Society for Mass Spectrometry, 2008. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 9 papers.
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Who cites it
9 citing papers in PubMed, 23 citations in OpenAlex.
- Characterization of Intramolecular Interactions of Cytochrome c Using Hydrogen-Deuterium Exchange-Trapped Ion Mobility Spectrometry-Mass Spectrometry and Molecular Dynamics.Analytical chemistry · 2017Article
- Differential Mobility Spectrometry-Hydrogen Deuterium Exchange (DMS-HDX) as a Probe of Protein Conformation in Solution.Journal of the American Society for Mass Spectrometry · 2016Article
- Supercharging with m-nitrobenzyl alcohol and propylene carbonate: forming highly charged ions with extended, near-linear conformations.Analytical chemistry · 2015Article
- Time-resolved pulsed hydrogen/deuterium exchange mass spectrometry probes gaseous proteins structural kinetics.Journal of the American Society for Mass Spectrometry · 2015Article
- Solution and gas-phase H/D exchange of protein-small-molecule complexes: Cex and its inhibitors.Journal of the American Society for Mass Spectrometry · 2012Article
- Transitions between elongated conformations of ubiquitin [M+11H]11+ enhance hydrogen/deuterium exchange.The journal of physical chemistry. B · 2011Article
- Shape changes induced by N-terminal platination of ubiquitin by cisplatin.Journal of the American Society for Mass Spectrometry · 2010Article
- Gas-phase hydrogen/deuterium exchange in a traveling wave ion guide for the examination of protein conformations.Analytical chemistry · 2009Article
- Gas-phase H/D exchange and collision cross sections of hemoglobin monomers, dimers, and tetramers.Journal of the American Society for Mass Spectrometry · 2009Article
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Authors and funding
3 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
At low pH in solutions of 50% methanol, proteins form expanded denatured states (the "H" state). In 90% methanol, proteins form expanded helical denatured states with artificial alpha-helices (the "H(c)" state). Gas-phase ions of ubiquitin, cytochrome c, apomyoglobin, and native and disulfide-reduced beta-lactoglobulin were formed by electrospray ionization (ESI) of the proteins from the H and H(c) states in solution. Both states in solution produce the same charge states in ESI. The conformations of the ions were studied with cross section measurements and gas-phase H/D exchange experiments. The cross sections show that the ions retain considerable folded structure. For a given protein and given charge state, ions produced from the H and H(c) states showed the same cross sections (within approximately 1%). Ions of cytochrome c, apomyoglobin, and native and reduced beta-lactoglobulin of a given charge state showed no differences in H/D exchange level when produced from the H or H(c) state. However, ubiquitin ions produced from the H(c) state consistently exchange fewer ( approximately 13%) hydrogens than ions produced from the H state, suggesting that in this case the gas-phase protein ions retain some memory of their solution conformations.
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