ArticleJournal of the American Society for Mass Spectrometry2009
Gas-phase H/D exchange and collision cross sections of hemoglobin monomers, dimers, and tetramers.
Article in Journal of the American Society for Mass Spectrometry, 2009. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 6 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
6 citing papers in PubMed, 13 citations in OpenAlex.
- Probing the Dissociation of Protein Complexes by Means of Gas-Phase H/D Exchange Mass Spectrometry.Journal of the American Society for Mass Spectrometry · 2019Article
- Design of a TW-SLIM Module for Dual Polarity Confinement, Transport, and Reactions.Journal of the American Society for Mass Spectrometry · 2017Article
- Electron-capture dissociation and ion mobility mass spectrometry for characterization of the hemoglobin protein assembly.Protein science : a publication of the Protein Society · 2015Article
- Two decades of studying non-covalent biomolecular assemblies by means of electrospray ionization mass spectrometry.Journal of the Royal Society, Interface · 2012Review
- Gas-phase ions of human hemoglobin A, F, and S.Journal of the American Society for Mass Spectrometry · 2011Article
- Mass spectra and ion collision cross sections of hemoglobin.Journal of the American Society for Mass Spectrometry · 2011Article
Corrections and comments
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Authors and funding
2 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
The conformations of gas-phase ions of hemoglobin, and its dimer and monomer subunits have been studied with H/D exchange and cross section measurements. During the H/D exchange measurements, tetramers undergo slow dissociation to dimers, and dimers to monomers, but this did not prevent drawing conclusions about the relative exchange levels of monomers, dimers, and tetramers. Assembly of the monomers into tetramers, hexamers, and octamers causes the monomers to exchange a greater fraction of their hydrogens. Dimer ions, however, exchange a lower fraction of their hydrogens than monomers or tetramers. Solvation of tetramers affects the exchange kinetics. Solvation molecules do not appear to exchange, and solvation lowers the overall exchange level of the tetramers. Cross section measurements show that monomer ions in low charge states, and tetramer ions have compact structures, comparable in size to the native conformations in solution. Dimers have remarkably compact structures, considerably smaller than the native conformation in solution and smaller than might be expected from the monomer or tetramer cross sections. This is consistent with the relatively low level of exchange of the dimers.
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Registered trials
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