ArticleJournal of the American Chemical Society2017
Chemical Probes and Engineered Constructs Reveal a Detailed Unfolding Mechanism for a Solvent-Free Multidomain Protein.
Article in Journal of the American Chemical Society, 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 27 papers.
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Who cites it
27 citing papers in PubMed.
- Revealing Anisotropic Growth of Liraglutide Oligomers by Native Ion Mobility Mass Spectrometry and Molecular Dynamics Simulation.ACS central science · 2025Article
- The sheet-to-helix transition is a potential gas-phase unfolding pathway for a multidomain protein CRMChinese chemical letters = Zhongguo hua xue kuai bao · 2025Article
- Computed Vibrational Heat Capacities for Gas-Phase Biomolecular Ions.Journal of the American Society for Mass Spectrometry · 2025Article
- Ion Mobility-Mass Spectrometry Captures the Structural Consequences of Lipid Nanoparticle Encapsulation on Ribonucleic Acid Cargo.Journal of the American Chemical Society · 2024Article
- Understanding the structural dynamics of human islet amyloid polypeptide: Advancements in and applications of ion-mobility mass spectrometry.Biophysical chemistry · 2024Review
- Cyclic Ion Mobility-Mass Spectrometry and Tandem Collision Induced Unfolding for Quantification of Elusive Protein Biomarkers.Analytical chemistry · 2024Article
- Collision-Induced Unfolding Reveals Disease-Associated Stability Shifts in Mitochondrial Transfer Ribonucleic Acids.Journal of the American Chemical Society · 2024Article
- Collision Induced Unfolding Enables the Quantitation of Isomass Biotherapeutics in Complex Biological Matrices.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
- Perspective on the potential of tandem-ion mobility /mass spectrometry methods for structural proteomics applications.Frontiers in analytical science · 2023Article
- Gas-Phase Unfolding of Protein Complexes Distinguishes Conformational Isomers.Journal of the American Chemical Society · 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
- Collision Cross Sections for Native Proteomics: Challenges and Opportunities.Journal of proteome research · 2022Article
- Recent technological developments for native mass spectrometry.Biochimica et biophysica acta. Proteins and proteomics · 2022Review
- Rapid structural discrimination of IgG antibodies by multicharge-state collision-induced unfolding.RSC advances · 2021Article
- Native mass spectrometry and gas-phase fragmentation provide rapid and in-depth topological characterization of a PROTAC ternary complex.Cell chemical biology · 2021Article
- Enhanced Collision Induced Unfolding and Electron Capture Dissociation of Native-like Protein Ions.Analytical chemistry · 2020Article
- Structural Analysis of the Effect of a Dual-FLAG Tag on Transthyretin.Biochemistry · 2020Article
- Molecular basis for chirality-regulated Aβ self-assembly and receptor recognition revealed by ion mobility-mass spectrometry.Nature communications · 2019Article
- Solution thermochemistry of concanavalin A tetramer conformers measured by variable-temperature ESI-IMS-MS.International journal of mass spectrometry · 2019Article
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Authors and funding
3 authors.
Funding
Abstract
Despite the growing application of gas-phase measurements in structural biology and drug discovery, the factors that govern protein stabilities and structures in a solvent-free environment are still poorly understood. Here, we examine the solvent-free unfolding pathway for a group of homologous serum albumins. Utilizing a combination of chemical probes and noncovalent reconstructions, we draw new specific conclusions regarding the unfolding of albumins in the gas phase, as well as more general inferences regarding the sensitivity of collision induced unfolding to changes in protein primary and tertiary structure. Our findings suggest that the general unfolding pathway of low charge state albumin ions is largely unaffected by changes in primary structure; however, the stabilities of intermediates along these pathways vary widely as sequences diverge. Additionally, we find that human albumin follows a domain associated unfolding pathway, and we are able to assign each unfolded form observed in our gas-phase data set to the disruption of specific domains within the protein. The totality of our data informs the first detailed mechanism for multidomain protein unfolding in the gas phase, and highlights key similarities and differences from the known solution-phase pathway.
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