Ion-Ion Proton Transfer and Parallel Ion Parking for the Analysis of Mixtures of Intact Proteins on a Modified Orbitrap Mass Analyzer
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We have enabled parallel ion parking on a modified Orbitrap Elite™ as a way to control ion-ion proton transfer reactions via selective activation of a range of ions. The result is the concentration of the majority of ion current from multiple charge states of each precursor proteoform into a single charge state, maximizing signal intensity and increasing effective sensitivity compared to conventional MS1 spectra. These techniques were applied in an on-line HPLC, data-dependent MS/MS analysis of intact E. coli ribosomal proteins with HCD fragmentation. With one injection, all but two ribosomal proteins were selected for fragmentation and subsequently identified. The techniques described facilitate rapid identification of intact proteins in complex mixtures and an enhanced ability to observe proteins of low abundance.
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Proton transfer reaction methods recently introduced in top-down proteomics lower charge states and simplify mass spectra, which improves analysis of complex intact protein mixtures.
“Recent implementations of proton transfer reaction in top-down proteomics have allowed to reduce the charge states and simplify mass spectra, leading to significant improvements in analysis of complex intact protein mixtures.12,44,45”
From Sensitive Top-Down Proteomics Analysis of a Low Number of Mammalian Cells Using a Nanodroplet Sample Processing Platform (2020) · cites this paper as [12]
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References 26 · Cited by 44
- Authors
- Ugrin, S. A., English, A. M., Syka, J. E. P., Bai, D. L., Anderson, L. C., Shabanowitz, J., & Hunt, D. F.
- Affiliations
- University of Virginia (US)
- Thermo Fisher Scientific (United States) (US)
- National High Magnetic Field Laboratory (US)
- Corresponding author
- Hunt, Donald F.
- Venue
- Journal of the American Society for Mass Spectrometry
- Publisher
- American Chemical Society (ACS)
- Published
- 2019-08-07
- Volume
- 30
- Issue
- 10
- Pages
- 2163-2173
- ISSN
- 1044-0305 (ISSN-L)
- PMC
- PMC6805958
- OpenAlex
- W2966700924
- Cited by
- 44
- References
- 26
- Citations by year
- 2026: 4 · 2025: 5 · 2024: 7 · 2023: 4 · 2022: 8 · 2021: 6 · 2020: 6 · 2019: 4
- FWCI
- 2.40
- Type
- journal article
- Language
- en
- Open access
- green
- www.ncbi.nlm.nih.gov
- Licence
- Locations
- Journal of the American Society for Mass Spectrometry (publishedVersion)
- Europe PMC (PubMed Central) (publishedVersion, cc-by)
- PubMed Central (publishedVersion, cc-by)
- PubMed (publishedVersion)
- Funders
- National Science Foundation (DMR-1157490, DMR-1644779)
- National Institute of General Medical Sciences (GM037537)
- Topics
- Physical Sciences › Chemistry › Spectroscopy › Mass Spectrometry Techniques and Applications
- Physical Sciences › Chemistry › Spectroscopy › Advanced Proteomics Techniques and Applications
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Metabolomics and Mass Spectrometry Studies
- Keywords
- top-down proteomics, HCD fragmentation, ribosomal proteins, Escherichia coli, low-abundance proteins, proteoforms, HPLC-MS/MS
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