ArticleJournal of the American Society for Mass Spectrometry1998
Unfolding of proteins monitored by electrospray ionization mass spectrometry: a comparison of positive and negative ion modes.
Article in Journal of the American Society for Mass Spectrometry, 1998. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 64 papers.
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Who cites it
64 citing papers in PubMed.
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- IscS Kinetics in Native Mass Spectrometry Buffers Reveal Key Physiochemical Properties that Influence Enzyme Activity.Journal of the American Society for Mass Spectrometry · 2026Article
- Stabilization of Protein Interactions through Electrospray Additives in Negative Ion Mode Native Mass Spectrometry.Analytical chemistry · 2025Article
- Protein analysis using capillary electrophoresis coupled to mass spectrometry through vibrating sharp-edge spray ionization.Electrophoresis · 2024Article
- The role of solvation on the conformational landscape of α-synuclein.The Analyst · 2023Article
- Molecular sensitised probe for amino acid recognition within peptide sequences.Nature communications · 2023Article
- Effects of Phosphorylation on the Activity, Inhibition and Stability of Carbonic Anhydrases.International journal of molecular sciences · 2023Article
- Characterisation of gas cell reactions for 70+ elements using NJournal of analytical atomic spectrometry · 2023Article
- Capillary Vibrating Sharp-Edge Spray Ionization Augments Field-Free Ionization Techniques to Promote Conformer Preservation in the Gas-Phase for Intractable Biomolecular Ions.The journal of physical chemistry. B · 2022Article
- High-Throughput Native Mass Spectrometry Screening in Drug Discovery.Frontiers in molecular biosciences · 2022Review
- Analysis of Tagged Proteins Using Tandem Affinity-Buffer Exchange Chromatography Online with Native Mass Spectrometry.Biochemistry · 2021Article
- Surface-Induced Dissociation of Anionic vs Cationic Native-Like Protein Complexes.Journal of the American Chemical Society · 2021Article
- Following Structural Changes by Thermal Denaturation Using Trapped Ion Mobility Spectrometry-Mass Spectrometry.The journal of physical chemistry. B · 2020Article
- Mass spectrometry-based methods in characterization of the higher order structure of protein therapeutics.Journal of pharmaceutical and biomedical analysis · 2020Review
- Ion Mobility and Gas-Phase Covalent Labeling Study of the Structure and Reactivity of Gaseous Ubiquitin Ions Electrosprayed from Aqueous and Denaturing Solutions.Journal of the American Society for Mass Spectrometry · 2020Article
- Collision-Induced Unfolding Is Sensitive to the Polarity of Proteins and Protein Complexes.Journal of the American Society for Mass Spectrometry · 2019Article
- Experimental and theoretical investigation of overall energy deposition in surface-induced unfolding of protein ions.Chemical science · 2019Article
- On the mechanism of protein supercharging in electrospray ionisation mass spectrometry: Effects on charging of additives with short- and long-chain alkyl constituents with carbonate and sulphite terminal groups.Analytica chimica acta: X · 2019Article
4 more citing papers are in PubMed but not listed here.
Corrections and comments
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Authors and funding
2 authors.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Electrospray ionization (ESI) mass spectrometry (MS) in both the positive and negative ion mode has been used to study protein unfolding transitions of lysozyme, cytochrome c (cyt c), and ubiquitin in solution. As expected, ESI of unfolded lysozyme leads to the formation of substantially higher charge states than the tightly folded protein in both modes of operation. Surprisingly, the acid-induced unfolding of cyt c as well as the acid and the base-induced unfolding of ubiquitin show different behavior: In these three cases protein unfolding only leads to marginal changes in the negative ion charge state distributions, whereas in the positive ion mode pronounced shifts to higher charge states are observed. This shows that ESI MS in the negative ion mode as a method for probing conformational changes of proteins in solution should be treated with caution. The data presented in this work provide further evidence that the conformation of a protein in solution not its charge state is the predominant factor for determining the ESI charge state distribution in the positive ion mode. Furthermore, these data support the hypothesis of a recent study (Konermann and Douglas, Biochemistry 1997, 36, 12,296-12,302) which suggested that ESI in the positive ion mode is not sensitive to changes in the secondary structure of proteins but only to changes in the tertiary structure.
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