ArticleJournal of the American Society for Mass Spectrometry2011
Ion mobility measurements of nondenatured 12-150 kDa proteins and protein multimers by tandem differential mobility analysis-mass spectrometry (DMA-MS).
Article in Journal of the American Society for Mass Spectrometry, 2011. 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.
- Other Techniques.Advances in biochemical engineering/biotechnology · 2026Review
- Collision cross section measurement and prediction methods in omics.Journal of mass spectrometry : JMS · 2023Review
- Surface Activity of Amines Provides Evidence for the Combined ESI Mechanism of Charge Reduction for Protein Complexes.Analytical chemistry · 2022Article
- Aqueous Solutions of Peptides and Trialkylamines Lead to Unexpected Peptide Modification.Molecules (Basel, Switzerland) · 2021Article
- Ion Mobility Spectrometry: Fundamental Concepts, Instrumentation, Applications, and the Road Ahead.Journal of the American Society for Mass Spectrometry · 2019Article
- Resolving the Discrepancies Between Empirical and Rayleigh Charge Limiting Models for Globular Proteins.Journal of the American Society for Mass Spectrometry · 2018Article
- Towards the Analysis of High Molecular Weight Proteins and Protein complexes using TIMS-MS.International journal for ion mobility spectrometry : official publication of the International Society for Ion Mobility Spectrometry · 2016Article
- Practical Limitations of Aerosol Separation by a Tandem Differential Mobility Analyzer-Aerosol Particle Mass Analyzer.Aerosol science and technology : the journal of the American Association for Aerosol Research · 2016Article
- Enhancing bottom-up and top-down proteomic measurements with ion mobility separations.Proteomics · 2015Article
- Measuring the effect of ion-induced drift-gas polarization on the electrical mobilities of multiply-charged ionic liquid nanodrops in air.Journal of the American Society for Mass Spectrometry · 2013Article
- The collision cross sections of iodide salt cluster ions in air via differential mobility analysis-mass spectrometry.Journal of the American Society for Mass Spectrometry · 2013Article
- Why do GroEL ions exhibit two gas phase conformers?Journal of the American Society for Mass Spectrometry · 2012Article
- Two decades of studying non-covalent biomolecular assemblies by means of electrospray ionization mass spectrometry.Journal of the Royal Society, Interface · 2012Review
- Ion mobility-mass spectrometry for structural proteomics.Expert review of proteomics · 2012Review
- Extracting structural information from charge-state distributions of intrinsically disordered proteins by non-denaturing electrospray-ionization mass spectrometry.Intrinsically disordered proteinsReview
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Abstract
The mobilities of electrosprayed proteins and protein multimers with molecular weights ranging from 12.4 kDa (cytochrome C monomers) to 154 kDa (nonspecific concanavalin A hexamers) were measured in dry air by a planar differential mobility analyzer (DMA) coupled to a time-of-flight mass spectrometer (TOF-MS). The DMA determines true mobility at atmospheric pressure, without perturbing ion structure from that delivered by the electrospray. A nondenaturing aqueous 20 mM triethylammonium formate buffer yields compact ions with low charge states, moderating polarization effects on ion mobility. Conversion of mobilities into cross-sections involves a reduction factor ξ for the actual mobility relative to that associated with elastic specular collisions with smooth surfaces. ξ is known to be 1.36 in air from Millikan's oil drop experiments. A similar enhancement effect ascribed to atomic-scale surface roughness has been found in numerical simulations. Adopting Millikan's value ξ=1.36 and assuming a spherical geometry yields a gas-phase protein density ρ(p)=0.949±0.053 g cm(-3) for all our protein data. This is substantially higher than the 0.67 g cm(-3) found in recent low-resolution DMA measurements of singly charged proteins. DMA-MS can distinguish nonspecific protein aggregates formed during the electrospray process from those formed preferentially in solution. The observed charge versus diameter relation is compatible with a protein charge reduction mechanism based on the evaporation of triethylammonium ions from electrosprayed drops.
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