ArticleNature communications2023
Determining the gas-phase structures of α-helical peptides from shape, microsolvation, and intramolecular distance data.
Article in Nature communications, 2023. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 5 papers.
What it found
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The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
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Who cites it
5 citing papers in PubMed.
- Evaluation of TIMS-derived peptide mobility measurements: calibration strategy and MS1/MS2 discrepancies.Analytical and bioanalytical chemistry · 2026Article
- How to Use Quantum Chemistry for Analyzing Mass Spectrometry Data.Mass spectrometry (Tokyo, Japan) · 2026Review
- Assigning Peptide Structure from Ion-Mobility Mass Spectrometry Collision Cross Section Data.Journal of the American Society for Mass Spectrometry · 2025Article
- Structure and Stabilities of Solution and Gas Phase Protein Complexes.Journal of the American Society for Mass Spectrometry · 2024Article
- Fluorescent Probes and Quenchers in Studies of Protein Folding and Protein-Lipid Interactions.Chemical record (New York, N.Y.) · 2024Review
Corrections and comments
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Authors and funding
11 authors.
Funding
Abstract
Mass spectrometry is a powerful technique for the structural and functional characterization of biomolecules. However, it remains challenging to accurately gauge the gas-phase structure of biomolecular ions and assess to what extent native-like structures are maintained. Here we propose a synergistic approach which utilizes Förster resonance energy transfer and two types of ion mobility spectrometry (i.e., traveling wave and differential) to provide multiple constraints (i.e., shape and intramolecular distance) for structure-refinement of gas-phase ions. We add microsolvation calculations to assess the interaction sites and energies between the biomolecular ions and gaseous additives. This combined strategy is employed to distinguish conformers and understand the gas-phase structures of two isomeric α-helical peptides that might differ in helicity. Our work allows more stringent structural characterization of biologically relevant molecules (e.g., peptide drugs) and large biomolecular ions than using only a single structural methodology in the gas phase.
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Registered trials
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