ArticleAnalytical chemistry2016
Low Charge and Reduced Mobility of Membrane Protein Complexes Has Implications for Calibration of Collision Cross Section Measurements.
Article in Analytical chemistry, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 15 papers.
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Who cites it
15 citing papers in PubMed.
- High-Performance Molecular Dynamics Simulations for Native Mass Spectrometry of Large Protein Complexes with the Fast Multipole Method.Analytical chemistry · 2024Article
- Ion mobility-mass spectrometry reveals the role of peripheral myelin protein dimers in peripheral neuropathy.Proceedings of the National Academy of Sciences of the United States of America · 2021Article
- Charge Reduction of Membrane Proteins in Native Mass Spectrometry Using Alkali Metal Acetate Salts.Analytical chemistry · 2020Article
- Collision Cross Sections of Charge-Reduced Proteins and Protein Complexes: A Database for Collision Cross Section Calibration.Analytical chemistry · 2020Article
- Native IM-Orbitrap MS: Resolving What Was Hidden.Trends in analytical chemistry : TRAC · 2020Article
- Interrogating Membrane Protein Structure and Lipid Interactions by Native Mass Spectrometry.Methods in molecular biology (Clifton, N.J.) · 2020Article
- Gas-Phase Collisions with Trimethylamine-N-Oxide Enable Activation-Controlled Protein Ion Charge Reduction.Journal of the American Society for Mass Spectrometry · 2019Article
- Computational Insights into Compaction of Gas-Phase Protein and Protein Complex Ions in Native Ion Mobility-Mass Spectrometry.Trends in analytical chemistry : TRAC · 2019Article
- Conditions for Analysis of Native Protein Structures Using Uniform Field Drift Tube Ion Mobility Mass Spectrometry and Characterization of Stable Calibrants for TWIM-MS.Journal of the American Society for Mass Spectrometry · 2019Article
- Allostery revealed within lipid binding events to membrane proteins.Proceedings of the National Academy of Sciences of the United States of America · 2018Article
- The application of ion-mobility mass spectrometry for structure/function investigation of protein complexes.Current opinion in chemical biology · 2018Review
- Polymers for Traveling Wave Ion Mobility Spectrometry Calibration.Journal of the American Society for Mass Spectrometry · 2017Article
- Size Exclusion Chromatography-Ion Mobility-Mass Spectrometry Coupling: a Step Toward Structural Biology.Journal of the American Society for Mass Spectrometry · 2017Article
- Integral membrane proteins: bottom-up, top-down and structural proteomics.Expert review of proteomics · 2017Review
- Integrating mass spectrometry with MD simulations reveals the role of lipids in NaNature communications · 2017Article
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4 authors.
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Abstract
Ion mobility mass spectrometry of integral membrane proteins provides valuable insights into their architecture and stability. Here we show that, due to their lower charge, the average mobility of native-like membrane protein ions is approximately 30% lower than that of soluble proteins of similar mass. This has implications for drift time measurements, made on traveling wave ion mobility mass spectrometers, which have to be calibrated to extract collision cross sections (Ω). Common calibration strategies employ unfolded or native-like soluble protein standards with masses and mobilities comparable to the protein of interest. We compare Ω values for membrane proteins, derived from standard calibration protocols using soluble proteins, to values measured using an RF-confined drift tube. Our results demonstrate that, while common calibration methods underestimate Ω for native-like or unfolded membrane protein complexes, higher mass soluble calibration standards consistently yield more accurate Ω values. These findings enable us to obtain directly structural information for highly charge-reduced complexes by traveling wave ion mobility mass spectrometry.
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