ArticleJournal of the American Society for Mass Spectrometry2020
Rapid Determination of Activation Energies for Gas-Phase Protein Unfolding and Dissociation in a Q-IM-ToF Mass Spectrometer.
Article in Journal of the American Society for Mass Spectrometry, 2020. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 20 papers.
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Who cites it
20 citing papers in PubMed.
- Determination of Thermochemical Barriers in Multiple-Collision-Induced Dissociation Experiments on Gas-Phase Protein Complexes.Journal of the American Chemical Society · 2025Article
- The mass spectrometric intact transition epitope mapping method supports protein engineering of foldon trimer variants.Scientific reports · 2025Article
- Dissecting Interactions between RNA and Coronavirus Nucleocapsid Proteins Using Native Mass Spectrometry.Journal of the American Society for Mass Spectrometry · 2025Article
- Computed Vibrational Heat Capacities for Gas-Phase Biomolecular Ions.Journal of the American Society for Mass Spectrometry · 2025Article
- Deciphering the safeguarding role of cysteine residues in p53 against HCommunications chemistry · 2025Article
- Modeling collisional kinetic energy damping, heating, and cooling of ions in mass spectrometers: a tutorial perspective.International journal of mass spectrometry · 2024Article
- Revealing the Fates of Proteins in the Gas Phase.International journal of mass spectrometry · 2024Article
- Effects of Nano-Electrospray Ionization Emitter Position on Unintentional In-Source Activation of Peptide and Protein Ions.Journal of the American Society for Mass Spectrometry · 2024Article
- Fragment Ion Abundance Reveals Information about Structure and Charge Localization in Highly Charged Proteins.Journal of the American Society for Mass Spectrometry · 2023Article
- Application of Multiple Length Cross-linkers to the Characterization of Gaseous Protein Structure.Analytical chemistry · 2022Article
- Gas-Phase Covalent Bond Formation via Nucleophilic Substitution: A Dissociation Kinetics Study of Leaving Groups, Isomeric R Groups, and Nucleophilic Sites.Journal of the American Society for Mass Spectrometry · 2022Article
- Comparing Selected-Ion Collision Induced Unfolding with All Ion Unfolding Methods for Comprehensive Protein Conformational Characterization.Journal of the American Society for Mass Spectrometry · 2022Article
- Approaches to Heterogeneity in Native Mass Spectrometry.Chemical reviews · 2022Review
- Mass Spectrometry Methods for Measuring Protein Stability.Chemical reviews · 2022Review
- Investigation of Charge-State-Dependent Compaction of Protein Ions with Native Ion Mobility-Mass Spectrometry and Theory.Journal of the American Society for Mass Spectrometry · 2022Article
- Lipid Head Group Adduction to Soluble Proteins Follows Gas-Phase Basicity Predictions: Dissociation Barriers and Charge Abstraction.International journal of mass spectrometry · 2021Article
- 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
- THE IMS PARADOX: A PERSPECTIVE ON STRUCTURAL ION MOBILITY-MASS SPECTROMETRY.Mass spectrometry reviews · 2021Review
- Mass Spectrometric Analysis of Antibody-Epitope Peptide Complex Dissociation: Theoretical Concept and Practical Procedure of Binding Strength Characterization.Molecules (Basel, Switzerland) · 2020Article
- Thermometer Ions, Internal Energies, and In-Source Fragmentation in Ambient Ionization.Mass spectrometry reviewsReview
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Authors and funding
3 authors.
Funding
Abstract
Ion mobility-mass spectrometry has emerged as a powerful tool for interrogating a wide variety of chemical systems. Collision-induced unfolding (CIU), typically performed in time-of-flight instruments, has been utilized to obtain valuable qualitative insight into protein structure and illuminate subtle differences between related species. CIU experiments can be performed relatively quickly, but unfolding energy information obtained from them has not yet been interpreted quantitatively. While several methods can determine quantitative dissociation energetics for small molecules, clusters, and peptides, these methods have rarely been applied to proteins, and never to study unfolding. Here, we present a method to rapidly determine activation energies for protein unfolding and dissociation, built on a model for energy deposition during collisional activation. The method is validated by comparing activation energies for dissociation of three complexes with those obtained using blackbody infrared radiative dissociation (BIRD); values from the two methods are in agreement. Several protein monomers were unfolded using CIU, including multiple charge states of both cations and anions, and activation energies determined. Δ
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