Electron transfer dissociation facilitates the measurement of deuterium incorporation into selectively labeled peptides with single residue resolution
about
Applications of hydrogen deuterium exchange (HDX) for the characterization of conformational dynamics in light-activated photoreceptorsHydrogen/deuterium exchange mass spectrometry applied to IL-23 interaction characteristics: potential impact for therapeuticsThe diverse and expanding role of mass spectrometry in structural and molecular biologyHydrogen exchange mass spectrometry: are we out of the quicksand?Glucagon-like peptide-1 receptor ligand interactions: structural cross talk between ligands and the extracellular domainPartial cooperative unfolding in proteins as observed by hydrogen exchange mass spectrometry.Investigating solution-phase protein structure and dynamics by hydrogen exchange mass spectrometry.Hydrogen Exchange Mass Spectrometry.Controlling hydrogen scrambling in multiply charged protein ions during collisional activation: implications for top-down hydrogen/deuterium exchange MS utilizing collisional activation in the gas phase.Probing the Gaseous Structure of a β-Hairpin Peptide with H/D Exchange and Electron Capture Dissociation.The utility of hydrogen/deuterium exchange mass spectrometry in biopharmaceutical comparability studiesMany overlapping peptides for protein hydrogen exchange experiments by the fragment separation-mass spectrometry method.Platform dependencies in bottom-up hydrogen/deuterium exchange mass spectrometry.Peptide-column interactions and their influence on back exchange rates in hydrogen/deuterium exchange-MS.Considerations in the analysis of hydrogen exchange mass spectrometry data.H/D exchange and mass spectrometry in the studies of protein conformation and dynamics: is there a need for a top-down approach?Online, high-pressure digestion system for protein characterization by hydrogen/deuterium exchange and mass spectrometry.Hydrogen/deuterium exchange mass spectrometry for probing higher order structure of protein therapeutics: methodology and applications.Recent developments in quantitative proteomics.The influence of adnectin binding on the extracellular domain of epidermal growth factor receptor.Real-time hydrogen/deuterium exchange kinetics via supercharged electrospray ionization tandem mass spectrometry.Resolving isotopic fine structure to detect and quantify natural abundance- and hydrogen/deuterium exchange-derived isotopomers.Use of 1,5-diaminonaphthalene to combine matrix-assisted laser desorption/ionization in-source decay fragmentation with hydrogen/deuterium exchange.Investigating the interaction between the neonatal Fc receptor and monoclonal antibody variants by hydrogen/deuterium exchange mass spectrometryDifferential hydrogen/deuterium exchange mass spectrometry analysis of protein-ligand interactionsEffects of supercharging reagents on noncovalent complex structure in electrospray ionization from aqueous solutionsConformational transitions in the membrane scaffold protein of phospholipid bilayer nanodiscsFast photochemical oxidation of proteins for epitope mappingHydrogen/deuterium exchange and electron-transfer dissociation mass spectrometry determine the interface and dynamics of apolipoprotein E oligomerizationApplications of mass spectrometry to lipids and membranesETD in a traveling wave ion guide at tuned Z-spray ion source conditions allows for site-specific hydrogen/deuterium exchange measurementsSubzero temperature chromatography for reduced back-exchange and improved dynamic range in amide hydrogen/deuterium exchange mass spectrometryGas-phase structure and fragmentation pathways of singly protonated peptides with N-terminal arginine.Automated hydrogen/deuterium exchange electron transfer dissociation high resolution mass spectrometry measured at single-amide resolution.Protein hydrogen exchange at residue resolution by proteolytic fragmentation mass spectrometry analysis.A new approach to measuring protein backbone protection with high spatial resolution using H/D exchange and electron capture dissociationProtein conformations can be probed in top-down HDX MS experiments utilizing electron transfer dissociation of protein ions without hydrogen scrambling.Gas-phase hydrogen/deuterium exchange in a traveling wave ion guide for the examination of protein conformations.The use of mass spectrometry to study amyloid-β peptides.High-resolution MS for structural characterization of protein therapeutics: advances and future directions.
P2860
Q27003155-1A347AE0-2563-41F5-B0A9-AFADDBB76500Q27004640-C8008A19-D1A5-4782-9C84-E7FBB1142639Q28080243-EDCFA869-D0E7-4071-8D4F-A65640B6E3C3Q28263711-46882D3F-C012-4E8B-85BC-3BA612C8D008Q28542687-B49CCAE6-D8C5-4208-9AB6-4C29720E696CQ30009855-4C4CB88B-D4BD-4763-BCBC-58E2AB93E5A8Q30382851-113F155A-1792-428B-A5C8-437AF77931CBQ30383686-EE155EE9-5342-4BD2-9267-D1E590180687Q30384154-DC66E24A-AD0D-45F6-A5DB-9EF9AA2FC4FBQ30396317-6D236A49-E0A9-4A2D-B0C4-2925C5136ABBQ30401825-A2CBACA7-9EBD-4D04-AF4E-A8EF1E32A70CQ30407515-B07D95C7-D922-4EC9-BB8D-CF1A665EF600Q30424252-17EFFF08-6AC3-4ED5-A3DC-82CD4121599BQ30430210-C0A22505-5E25-4884-9DDC-1029FC8E007FQ30624819-43596592-BAC3-4F50-AB26-C2C35E9D395CQ33585139-9A2C8928-4EE3-46F2-B41F-D6CF72AF342AQ33676804-ECBF566A-F54B-41D8-BB1D-946BBD0893A7Q33844511-C6FEA1CD-265B-429A-9368-9B750A0C3EEBQ34307294-E4A779DA-7819-4078-977D-8CD1BCD60F00Q34474034-004877B9-5806-4DB1-A19A-F793951D9203Q34626415-567756B4-7818-43A2-AA34-6B70CEDF6E15Q34712697-94824786-BA04-4E97-9823-81F51D8D6052Q34822535-2DC05BAE-9435-4079-A571-945535EEA073Q34884133-BD24C1EE-6507-4E7F-A6D7-FA732939C120Q35040616-BE2004C8-53D5-4F88-99A8-3086339813CAQ35120265-E28D81FD-FAE8-48FB-B690-7E32270C46BEQ35264725-9D5DA2EC-1E5B-41D5-8AD8-1ADC0C5264BEQ35349699-95646378-11AF-4411-AE1C-075D91902701Q35456689-8DD0D07F-1CE1-4EDF-B858-0B697689FEB0Q36135725-D9A8B3B2-02B2-450E-B210-BEE55A16B572Q36225549-A6DEDA9A-C204-41E4-ADE0-E8CBA81D06A1Q36386531-2E24F656-4728-4795-97F5-C439AD2C9307Q36876363-6A3ECBB0-A06D-42E7-BC97-C41CCCAF8F88Q37228274-A86AD08F-F663-49C6-9592-8F5DABCBEA48Q37236489-9D6D8528-43AA-4E9B-AD76-4C60F0C2F3CAQ37240962-A73F9F31-FBAE-4475-855B-EE084BA980B0Q37301806-E24DDA7A-3609-4D3A-A0C1-AD17924F522AQ37480120-DDEB6E6B-549B-4336-9351-53407689B9B9Q37866222-E21840BB-592B-42BA-8197-07D7CE0B6850Q38110611-8E7EF826-7312-4FE2-B9E9-F2139021BD35
P2860
Electron transfer dissociation facilitates the measurement of deuterium incorporation into selectively labeled peptides with single residue resolution
description
2008 nî lūn-bûn
@nan
2008 թուականի Դեկտեմբերին հրատարակուած գիտական յօդուած
@hyw
2008 թվականի դեկտեմբերին հրատարակված գիտական հոդված
@hy
2008年の論文
@ja
2008年論文
@yue
2008年論文
@zh-hant
2008年論文
@zh-hk
2008年論文
@zh-mo
2008年論文
@zh-tw
2008年论文
@wuu
name
Electron transfer dissociation ...... with single residue resolution
@ast
Electron transfer dissociation ...... with single residue resolution
@en
Electron transfer dissociation ...... with single residue resolution
@nl
type
label
Electron transfer dissociation ...... with single residue resolution
@ast
Electron transfer dissociation ...... with single residue resolution
@en
Electron transfer dissociation ...... with single residue resolution
@nl
prefLabel
Electron transfer dissociation ...... with single residue resolution
@ast
Electron transfer dissociation ...... with single residue resolution
@en
Electron transfer dissociation ...... with single residue resolution
@nl
P50
P356
P1476
Electron transfer dissociation ...... with single residue resolution
@en
P2093
Thomas J D Jørgensen
P304
17453-17459
P356
10.1021/JA805573H
P407
P577
2008-12-01T00:00:00Z