ArticleThe journal of physical chemistry. B2014
Evidence for two new solution states of ubiquitin by IMS-MS analysis.
Article in The journal of physical chemistry. B, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 39 papers.
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Who cites it
39 citing papers in PubMed, 60 citations in OpenAlex.
- Development and Modification of Ion Mobility Mass Spectrometry Instrumentation for Enhanced Analysis of Biological Molecules.Journal of the American Society for Mass Spectrometry · 2025Review
- Conformational landscapes of rigid and flexible molecules explored with variable temperature ion mobility-mass spectrometry.Nature communications · 2025Article
- Structural differentiation of protein charge state conformers via gas-phase ion/ion cross-linking mass spectrometry.International journal of mass spectrometry · 2025Article
- Accessing Different Protein Conformer Ensembles with Tunable Capillary Vibrating Sharp-Edge Spray Ionization.The journal of physical chemistry. B · 2025Article
- Revealing the Fates of Proteins in the Gas Phase.International journal of mass spectrometry · 2024Article
- Conformational and Structural Characterization of Knotted Proteins.Biochemistry · 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
- Variation of CI-2 Conformers upon Addition of Methanol to Water: An IMS-MS-Based Thermodynamic Analysis.The journal of physical chemistry. A · 2023Article
- In-droplet hydrogen-deuterium exchange to examine protein/peptide solution conformer heterogeneity.Rapid communications in mass spectrometry : RCM · 2023Article
- Resolving Hidden Solution Conformations of Hemoglobin Using IMS-IMS on a Cyclic Instrument.Journal of the American Society for Mass Spectrometry · 2023Article
- Ion Mobility Mass Spectrometry (IM-MS) for Structural Biology: Insights Gained by Measuring Mass, Charge, and Collision Cross Section.Chemical reviews · 2023Review
- Variable-Temperature Native Mass Spectrometry for Studies of Protein Folding, Stabilities, Assembly, and Molecular Interactions.Annual review of biophysics · 2022Review
- Experimental Determination of Activation Energies for Covalent Bond Formation via Ion/Ion Reactions and Competing Processes.Journal of the American Society for Mass Spectrometry · 2021Article
- Protons Are Fast and Smart; Proteins Are Slow and Dumb: On the Relationship of Electrospray Ionization Charge States and Conformations.Journal of the American Society for Mass Spectrometry · 2021Article
- Gas-Phase Ion/Ion Chemistry for Structurally Sensitive Probes of Gaseous Protein Ion Structure: Electrostatic and Electrostatic to Covalent Cross-Linking.International journal of mass spectrometry · 2021Article
- Evidence for Many Unique Solution Structures for Chymotrypsin Inhibitor 2: A Thermodynamic Perspective Derived from vT-ESI-IMS-MS Measurements.Journal of the American Chemical Society · 2020Article
- Following Structural Changes by Thermal Denaturation Using Trapped Ion Mobility Spectrometry-Mass Spectrometry.The journal of physical chemistry. B · 2020Article
- Collision-Induced Unfolding Studies of Proteins and Protein Complexes using Drift Tube Ion Mobility-Mass Spectrometer.Analytical chemistry · 2020Article
- Ion Mobility and Gas-Phase Covalent Labeling Study of the Structure and Reactivity of Gaseous Ubiquitin Ions Electrosprayed from Aqueous and Denaturing Solutions.Journal of the American Society for Mass Spectrometry · 2020Article
- Ultraviolet Photodissociation Mass Spectrometry for Analysis of Biological Molecules.Chemical reviews · 2020Review
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Authors and funding
2 authors at 1 institution in 1 country.
Funding
Abstract
Ion mobility spectrometry coupled with mass spectrometry (IMS-MS) is used to investigate the populations of different states for ubiquitin in water:methanol solutions. In these experiments, ubiquitin is electrosprayed from 20 water:methanol (100:0 to 5:95, pH = 2) solutions, ranging from native to denaturing conditions. With an increased percentage of methanol in solution, ubiquitin ions ([M + 7H](7+) to [M + 12H](12+)) show substantial variations in both charge state distributions and ion mobility distributions. Analysis of these data provides evidence for the existence of five ubiquitin states in solution: the native N state, favored in solutions of 100:0 to 70:30 water:methanol for the +7 and +8 charge states; the more helical A state and a new closely related A' state, favored in solutions of 70:30 to 5:95 water:methanol for the +9 to +12 charge states; the unfolded U state, populated in 40:60 to 5:95 water:methanol solutions for the +8 to +10 and +12 charge states; and a new low-abundance state termed the B state, observed for 100:0 to 70:30 water:methanol solutions in the +8 to +10 and +12 charge states. The relative abundances for different states in different solutions are determined. The analysis presented here provides insight into how solution structures evolve into anhydrous conformations and demonstrates the utility of IMS-MS methods as a means of characterizing populations of conformers for proteins in solution.
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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.