ArticleInternational journal of mass spectrometry2018
Conformational Landscapes of Ubiquitin, Cytochrome c, and Myoglobin: Uniform Field Ion Mobility Measurements in Helium and Nitrogen Drift Gas.
Article in International journal of mass spectrometry, 2018. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 44 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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Who cites it
44 citing papers in PubMed, 95 citations in OpenAlex.
- Four IgG Antibodies and Protein G Are Shapeshifters.International journal of molecular sciences · 2026Article
- Native-Like Protein Structures in Vacuo: Steric Cooperativity as a Kinetic Barrier to Denaturation.JACS Au · 2026Article
- Deconvolution of High-Dimensional Ion Mobility Data Using Reversible-Jump Markov Chain Monte Carlo.Analytical chemistry · 2026Article
- The mass spectrometric intact transition epitope mapping method supports protein engineering of foldon trimer variants.Scientific reports · 2025Article
- Improving the Quadrupole to Ion Mobility Region in a Digital Quadrupole/Ion Mobility/Orbitrap Mass Spectrometer.Journal of the American Society for Mass Spectrometry · 2025Article
- Performance Evaluation of Constant Field and Traveling Wave-Based Structures for Lossless Ion Manipulations Devices Coupled to Mass Spectrometry.Journal of the American Society for Mass Spectrometry · 2025Article
- Mass spectrometry structural analysis of intrinsically disordered phosphoproteins.International journal of mass spectrometry · 2025Article
- Nanobubbles in Electrospray Ionization Mass Spectrometry.Analytical chemistry · 2025Article
- Structural differentiation of protein charge state conformers via gas-phase ion/ion cross-linking mass spectrometry.International journal of mass spectrometry · 2025Article
- Roughhousing with Ions: Surface-Induced Dissociation and Electron Capture Dissociation as Diagnostics of Q-Cyclic IMS-TOF Instrument Tuning Gentleness.Journal of the American Society for Mass Spectrometry · 2025Article
- Top-Down Structural Characterization of Native Ubiquitin Combining Solution-Stable Isotope Labeling, Trapped Ion Mobility Spectrometry, and Tandem Electron Capture Dissociation Mass Spectrometry.Analytical chemistry · 2024Article
- Evaluation of a Commercial TIMS-Q-TOF Platform for Native Mass Spectrometry.Journal of the American Society for Mass Spectrometry · 2024Article
- Structural Elucidation of Ubiquitin via Gas-Phase Ion/Ion Cross-Linking Reactions Using Sodium-Cationized Reagents Coupled with Infrared Multiphoton Dissociation.Analytical chemistry · 2024Article
- Towards IMInternational journal of mass spectrometry · 2024Article
- The role of solvation on the conformational landscape of α-synuclein.The Analyst · 2023Article
- Determining Collisional Cross Sections from Ion Decay with Individual Ion Mass Spectrometry.Journal of the American Society for Mass Spectrometry · 2023Article
- Article
- Mass spectrometric insights into protein aggregation.Essays in biochemistry · 2023Review
- Article
- Perspective on the potential of tandem-ion mobility /mass spectrometry methods for structural proteomics applications.Frontiers in analytical science · 2023Article
Corrections and comments
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Authors and funding
6 authors at 4 institutions in 2 countries.
Funding
Abstract
In this study, a commercial uniform field drift tube ion mobility-mass spectrometer (IM-MS) was utilized to measure the gas-phase conformational populations of three well-studied proteins: ubiquitin (8566 Da), cytochrome c (12,359 Da), and myoglobin in both apo and holo forms (16,951 and 17,567 Da, respectively) in order to evaluate the use of this technology for broadscale structural proteomics applications. Proteins were electrosprayed from either acidic organic (pH ~3) or aqueous buffered (pH ~6.6) solution phase conditions, which generated a wide range of cation charge states corresponding to both extended (unfolded) and compact (folded) gas-phase conformational populations. Corresponding collision cross section (CCS) measurements were compiled for significant ion mobility peak features observed at each charge state in order to map the conformational landscapes of these proteins in both helium and nitrogen drift gases. It was observed that the conformational landscapes were similar in both drift gases, with differences being attributed primarily to ion heating during helium operation due to the necessity of operating the instrument with higher pressure differentials. Higher resolving powers were observed in nitrogen, which allowed for slightly better structural resolution of closely-spaced conformer populations. The instrumentation was found to be particularly adept at measuring low abundance conformers which are only present under gentle conditions which minimize ion heating. This work represents the single largest ion mobility CCS survey published to date for these three proteins with 266 CCS values and 117 ion mobility spectra, many of which have not been previously reported.
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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.