ArticleAnalytical chemistry2026
Characterization of Gas-Phase Native(-like) Proteins Using Structures for Lossless Ion Manipulations.
Article in Analytical chemistry, 2026. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 2 papers.
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Who cites it
2 citing papers in PubMed.
- Resolving Isomeric Structures in Natural Complex Carbohydrates: A Comparative Study of SLIM and Cyclic Ion Mobility Platforms.Rapid communications in mass spectrometry : RCM · 2026Article
- SLIMPHONY: A SLIM-Based Instrument That Orchestrates Complex Ion Mobility-Mass Spectrometry Experiments.Journal of the American Society for Mass Spectrometry · 2026Article
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Authors and funding
13 authors.
Funding
Abstract
High-resolution mobility-based ion separations in Structures for Lossless Ion Manipulations (SLIM) have been useful for ion mobility separations for a variety of molecular classes in the gas phase. Here, we present multipass SLIM separations for gas-phase proteins in their near-native state exhibiting charge-state-dependent arrival time distributions using carbonic anhydrase (29 kDa), alcohol dehydrogenase (148 kDa), and apo-transferrin (79 kDa). The experimental CCS values were obtained from calibration curves for the arrival times of Agilent Tune Mix ions. For multipass separations, the ATDs were converted to CCS values by deconvoluting the multipass arrival times into accurate single-pass values amenable to the single-pass calibration curves. Mass spectra of carbonic anhydrase (CA) showed three different charge states (
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