ArticleJournal of the American Society for Mass Spectrometry2015
HDX match software for the data analysis of top-down ECD-FTMS hydrogen/deuterium exchange experiments.
Article in Journal of the American Society for Mass Spectrometry, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 7 papers.
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Who cites it
7 citing papers in PubMed.
- Strategies for Top-Down Hydrogen Deuterium Exchange-Mass Spectrometry: A Mini Review and Perspective.Journal of mass spectrometry : JMS · 2024Review
- Advances in Hydrogen/Deuterium Exchange Mass Spectrometry and the Pursuit of Challenging Biological Systems.Chemical reviews · 2022Review
- Structure of prion β-oligomers as determined by short-distance crosslinking constraint-guided discrete molecular dynamics simulations.Proteomics · 2021Article
- Ligand-induced disorder-to-order transitions characterized by structural proteomics and molecular dynamics simulations.Journal of proteomics · 2020Article
- Conformational ensemble of native α-synuclein in solution as determined by short-distance crosslinking constraint-guided discrete molecular dynamics simulations.PLoS computational biology · 2019Article
- Top-Down Proteomics: Ready for Prime Time?Analytical chemistry · 2018Review
- Solving protein structures using short-distance cross-linking constraints as a guide for discrete molecular dynamics simulations.Science advances · 2017Article
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Authors and funding
2 authors.
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Abstract
Hydrogen/deuterium exchange (HDX) combined with mass spectrometry is a powerful technique for studying protein structure. The recently developed top-down ECD-FTMS HDX approach (Pan J. et al., JACS, 2008) allows determination of the hydrogen/deuterium exchange of a protein's amide bonds, down to the single residue resolution. One of the existing limitations of this technology has been the laborious manual analysis of the MS/MS spectra. Here we present a software program for processing the data from these experiments. This program assigns the c- and z-fragment ion series of the protein, and calculates the number of the exchanged amide protons for each fragment by fitting the theoretically predicted isotopic envelopes of the deuterated fragments to the experimental data. Graphical Abstract ᅟ.
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