ArticleJournal of the American Society for Mass Spectrometry2009
Probing hemoglobin structure by means of traveling-wave ion mobility mass spectrometry.
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 27 papers.
What it found
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The trial behind it
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
27 citing papers in PubMed.
- Four IgG Antibodies and Protein G Are Shapeshifters.International journal of molecular sciences · 2026Article
- Resolving Hidden Solution Conformations of Hemoglobin Using IMS-IMS on a Cyclic Instrument.Journal of the American Society for Mass Spectrometry · 2023Article
- Separation and Collision Cross Section Measurements of Protein Complexes Afforded by a Modular Drift Tube Coupled to an Orbitrap Mass Spectrometer.Analytical chemistry · 2022Article
- High-Field Asymmetric Waveform Ion Mobility Spectrometry and Native Mass Spectrometry: Analysis of Intact Protein Assemblies and Protein Complexes.Analytical chemistry · 2020Article
- Native LESA TWIMS-MSI: Spatial, Conformational, and Mass Analysis of Proteins and Protein Complexes.Journal of the American Society for Mass Spectrometry · 2020Article
- Structural Heterogeneity in the Preamyloid Oligomers of β-2-Microglobulin.Journal of molecular biology · 2020Article
- In-Source Reduction of Disulfide-Bonded Peptides Monitored by Ion Mobility Mass Spectrometry.Journal of the American Society for Mass Spectrometry · 2018Article
- Addressing a Common Misconception: Ammonium Acetate as Neutral pH "Buffer" for Native Electrospray Mass Spectrometry.Journal of the American Society for Mass Spectrometry · 2017Article
- Small molecule-mediated inhibition of β-2-microglobulin-based amyloid fibril formation.The Journal of biological chemistry · 2017Article
- Imaging proteins at the single-molecule level.Proceedings of the National Academy of Sciences of the United States of America · 2017Article
- Salt Bridge Rearrangement (SaBRe) Explains the Dissociation Behavior of Noncovalent Complexes.Journal of the American Society for Mass Spectrometry · 2016Article
- Protein Structural Studies by Traveling Wave Ion Mobility Spectrometry: A Critical Look at Electrospray Sources and Calibration Issues.Journal of the American Society for Mass Spectrometry · 2016Article
- Electron-capture dissociation and ion mobility mass spectrometry for characterization of the hemoglobin protein assembly.Protein science : a publication of the Protein Society · 2015Article
- Experimental evaluation and optimization of structures for lossless ion manipulations for ion mobility spectrometry with time-of-flight mass spectrometry.Analytical chemistry · 2014Article
- Cation-induced stabilization of protein complexes in the gas phase: mechanistic insights from hemoglobin dissociation studies.Journal of the American Society for Mass Spectrometry · 2014Article
- Comparative analysis of oxy-hemoglobin and aquomet-hemoglobin by hydrogen/deuterium exchange mass spectrometry.Journal of the American Society for Mass Spectrometry · 2013Article
- Amphitrite: A program for processing travelling wave ion mobility mass spectrometry data.International journal of mass spectrometry · 2013Article
- Traveling-wave Ion Mobility-Mass Spectrometry Reveals Additional Mechanistic Details in the Stabilization of Protein Complex Ions through Tuned Salt Additives.International journal for ion mobility spectrometry : official publication of the International Society for Ion Mobility Spectrometry · 2013Article
- Resolving structural isomers of monosaccharide methyl glycosides using drift tube and traveling wave ion mobility mass spectrometry.Analytical chemistry · 2012Article
- Gas-phase ions of human hemoglobin A, F, and S.Journal of the American Society for Mass Spectrometry · 2011Article
Corrections and comments
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Authors and funding
4 authors.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Hemoglobin (Hb) is a tetrameric noncovalent complex consisting of two alpha- and two beta-globin chains each associated with a heme group. Its exact assembly pathway is a matter of debate. Disorders of hemoglobin are the most common inherited disorders and subsequently the molecule has been extensively studied. This work attempts to further elucidate the structural properties of the hemoglobin tetramer and its components. Gas-phase conformations of hemoglobin tetramers and their constituents were investigated by means of traveling-wave ion mobility mass spectrometry. Sickle (HbS) and normal (HbA) hemoglobin molecules were analyzed to determine whether conformational differences in their quaternary structure could be observed. Rotationally averaged collision cross sections were estimated for tetramer, dimer, apo-, and holo-monomers with reference to a protein standard with known cross sections. Estimates of cross section obtained for the tetramers were compared to values calculated from X-ray crystallographic structures. HbS was consistently estimated to have a larger cross section than that of HbA, comparable with values obtained from X-ray crystallographic structures. Nontetrameric species observed included apo- and holo- forms of alpha- and beta-monomers and heterodimers; alpha- and beta-monomers in both apo- and holo- forms were found to have similar cross sections, suggesting they maintain a similar fold in the gas phase in both the presence and the absence of heme. Heme-deficient dimer, observed in the spectrum when analyzing commercially prepared Hb, was not observed when analyzing fresh blood. This implies that holo-alpha-apo-beta is not an essential intermediate within the Hb assembly pathway, as previously proposed.
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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.