ArticleProtein science : a publication of the Protein Society2006
Automated extraction of backbone deuteration levels from amide H/2H mass spectrometry experiments.
Article in Protein science : a publication of the Protein Society, 2006. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 41 papers.
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Who cites it
41 citing papers in PubMed.
- Spinon Excitations in 99.9% Deuterated Single Crystals of Tomonaga-Luttinger Liquid [Cu(μ-CACS omega · 2025Article
- DGet! An open source deuteration calculator for mass spectrometry data.Journal of cheminformatics · 2024Article
- Protein turnover models for LC-MS data of heavy water metabolic labeling.Briefings in bioinformatics · 2022Article
- Computational methods in mass spectrometry-based structural proteomics for studying protein structure, dynamics, and interactions.Computational and structural biotechnology journal · 2020Review
- deMix: Decoding Deuterated Distributions from Heterogeneous Protein States via HDX-MS.Scientific reports · 2019Article
- Development of Software for the In-Depth Analysis of Protein Dynamics as Determined by MALDI Mass Spectrometry-Based Hydrogen/Deuterium Exchange.Mass spectrometry (Tokyo, Japan) · 2019Article
- Protein Footprinting Comes of Age: Mass Spectrometry for Biophysical Structure Assessment.Molecular & cellular proteomics : MCP · 2017Review
- Applications of hydrogen deuterium exchange (HDX) for the characterization of conformational dynamics in light-activated photoreceptors.Frontiers in molecular biosciences · 2015Review
- Analytical Aspects of Hydrogen Exchange Mass Spectrometry.Annual review of analytical chemistry (Palo Alto, Calif.) · 2015Review
- QUDeX-MS: hydrogen/deuterium exchange calculation for mass spectra with resolved isotopic fine structure.BMC bioinformatics · 2014Article
- Hexicon 2: automated processing of hydrogen-deuterium exchange mass spectrometry data with improved deuteration distribution estimation.Journal of the American Society for Mass Spectrometry · 2014Article
- Resolving isotopic fine structure to detect and quantify natural abundance- and hydrogen/deuterium exchange-derived isotopomers.Analytical chemistry · 2014Article
- Analysis of overlapped and noisy hydrogen/deuterium exchange mass spectra.Journal of the American Society for Mass Spectrometry · 2013Article
- H/D exchange centroid monitoring is insufficient to show differences in the behavior of protein states.Journal of the American Society for Mass Spectrometry · 2013Article
- Conformational analysis of recombinant monoclonal antibodies with hydrogen/deuterium exchange mass spectrometry.Methods in molecular biology (Clifton, N.J.) · 2013Article
- Minimizing back exchange in the hydrogen exchange-mass spectrometry experiment.Journal of the American Society for Mass Spectrometry · 2012Article
- HDX workbench: software for the analysis of H/D exchange MS data.Journal of the American Society for Mass Spectrometry · 2012Article
- Improved sequence resolution by global analysis of overlapped peptides in hydrogen/deuterium exchange mass spectrometry.Journal of the American Society for Mass Spectrometry · 2012Article
- The inner membrane histidine kinase EnvZ senses osmolality via helix-coil transitions in the cytoplasm.The EMBO journal · 2012Article
- HDXFinder: automated analysis and data reporting of deuterium/hydrogen exchange mass spectrometry.Journal of the American Society for Mass Spectrometry · 2012Article
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4 authors.
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Abstract
A Fourier deconvolution method has been developed to explicitly determine the amount of backbone amide deuterium incorporated into protein regions or segments by hydrogen/deuterium (H/D) exchange with high-resolution mass spectrometry. Determination and analysis of the level and number of backbone amide exchanging in solution provide more information about the solvent accessibility of the protein than do previous centroid methods, which only calculate the average deuterons exchanged. After exchange, a protein is digested into peptides as a way of determining the exchange within a local area of the protein. The mass of a peptide upon deuteration is a sum of the natural isotope abundance, fast exchanging side-chain hydrogens (present in MALDI-TOF H/2H data) and backbone amide exchange. Removal of the components of the isotopic distribution due to the natural isotope abundances and the fast exchanging side-chains allows for a precise quantification of the levels of backbone amide exchange, as is shown by an example from protein kinase A. The deconvoluted results are affected by overlapping peptides or inconsistent mass envelopes, and evaluation procedures for these cases are discussed. Finally, a method for determining the back exchange corrected populations is presented, and its effect on the data is discussed under various circumstances.
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