ArticleJournal of the American Society for Mass Spectrometry2008
Probing the gas-phase folding kinetics of peptide ions by IR activated DR-ECD.
Article in Journal of the American Society for Mass Spectrometry, 2008. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 32 papers.
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Who cites it
32 citing papers in PubMed.
- Multimodal Tandem Mass Spectrometry Techniques for the Analysis of Phosphopeptides.Journal of the American Society for Mass Spectrometry · 2022Article
- Effective discrimination of gas-phase peptide conformers using TIMS-ECD-ToF MS/MS.Analytical methods : advancing methods and applications · 2021Article
- Metal Ion Binding to the Amyloid β Monomer Studied by Native Top-Down FTICR Mass Spectrometry.Journal of the American Society for Mass Spectrometry · 2019Article
- Middle-down approach: a choice to sequence and characterize proteins/proteomes by mass spectrometry.RSC advances · 2018Review
- Radical solutions: Principles and application of electron-based dissociation in mass spectrometry-based analysis of protein structure.Mass spectrometry reviews · 2018Review
- Replacing HChemical science · 2018Article
- De Novo Glycan Sequencing by Electronic Excitation Dissociation and Fixed-Charge Derivatization.Analytical chemistry · 2018Article
- Unfolding and Folding of the Three-Helix Bundle Protein KIX in the Absence of Solvent.Journal of the American Society for Mass Spectrometry · 2016Article
- Enhancing Protein Disulfide Bond Cleavage by UV Excitation and Electron Capture Dissociation for Top-Down Mass Spectrometry.International journal of mass spectrometry · 2015Article
- Capturing Polyradical Protein Cations after an Electron Capture Event: Evidence for their Stable Distonic Structures in the Gas Phase.Journal of the American Society for Mass Spectrometry · 2015Article
- Probing Protein Structure and Folding in the Gas Phase by Electron Capture Dissociation.Journal of the American Society for Mass Spectrometry · 2015Article
- Mass spectrometric strategies to improve the identification of Pt(II)-modification sites on peptides and proteins.Journal of the American Society for Mass Spectrometry · 2014Article
- Proteins with highly similar native folds can show vastly dissimilar folding behavior when desolvated.Angewandte Chemie (International ed. in English) · 2014Article
- Gas-phase structure of amyloid-β (12-28) peptide investigated by infrared spectroscopy, electron capture dissociation and ion mobility mass spectrometry.Journal of the American Society for Mass Spectrometry · 2013Article
- Charge-site-dependent dissociation of hydrogen-rich radical peptide cations upon vacuum UV photoexcitation.Chemistry (Weinheim an der Bergstrasse, Germany) · 2012Article
- Transition metal ions: charge carriers that mediate the electron capture dissociation pathways of peptides.Journal of the American Society for Mass Spectrometry · 2011Article
- A new ion source and procedures for atmospheric pressure-electron capture dissociation of peptides.Journal of the American Society for Mass Spectrometry · 2011Article
- Topoisomer differentiation of molecular knots by FTICR MS: lessons from class II lasso peptides.Journal of the American Society for Mass Spectrometry · 2011Article
- Unusual fragmentation of β-linked peptides by ExD tandem mass spectrometry.Journal of the American Society for Mass Spectrometry · 2011Article
- Influence of charge state and amino acid composition on hydrogen transfer in electron capture dissociation of peptides.Journal of the American Society for Mass Spectrometry · 2010Article
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3 authors.
Funding
Abstract
The effect of infrared (IR) irradiation on the electron capture dissociation (ECD) fragmentation pattern of peptide ions was investigated. IR heating increases the internal energy of the precursor ion, which often amplifies secondary fragmentation, resulting in the formation of w-type ions as well as other secondary fragments. Improved sequence coverage was observed with IR irradiation before ECD, likely due to the increased conformational heterogeneity upon IR heating, rather than faster breakdown of the initially formed product ion complex, as IR heating after ECD did not have similar effect. Although the ECD fragment ion yield of peptide ions does not typically increase with IR heating, in double resonance (DR) ECD experiments, fragment ion yield may be reduced by fast resonant ejection of the charge reduced molecular species, and becomes dependent on the folding state of the precursor ion. In this work, the fragment ion yield was monitored as a function of the delay between IR irradiation and the DR-ECD event to study the gas-phase folding kinetics of the peptide ions. Furthermore, the degree of intracomplex hydrogen transfer of the ECD fragment ion pair was used to probe the folding state of the precursor ion. Both methods gave similar refolding time constants of approximately 1.5 s(-1), revealing that gaseous peptide ions often refold in less than a second, much faster than their protein counterparts. It was also found from the IR-DR-ECD study that the intramolecular H. transfer rate can be an order of magnitude higher than that of the separation of the long-lived c/z product ion complexes, explaining the common observation of c. and z type ions in ECD experiments.
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