Radiolytic modification of sulfur-containing amino acid residues in model peptides: fundamental studies for protein footprinting.
about
Chemical approaches to detect and analyze protein sulfenic acidsCharacterizing monoclonal antibody structure by carbodiimide/GEE footprintingQuantitative mapping of protein structure by hydroxyl radical footprinting-mediated structural mass spectrometry: a protection factor analysis.The effect of radiation-induced reactive oxygen species (ROS) on the structural and functional properties of yeast alcohol dehydrogenase (YADH).Visualizing water molecules in transmembrane proteins using radiolytic labeling methods.Future directions of structural mass spectrometry using hydroxyl radical footprinting.Electrostatics of cysteine residues in proteins: parameterization and validation of a simple model.Fast photochemical oxidation of proteins for comparing solvent-accessibility changes accompanying protein folding: data processing and application to barstarQuantifying protein interface footprinting by hydroxyl radical oxidation and molecular dynamics simulation: application to galectin-1.Fast photochemical oxidation of protein footprints faster than protein unfolding.Quantitative Protein Topography Measurements by High Resolution Hydroxyl Radical Protein Footprinting Enable Accurate Molecular Model SelectionConversion of methionine into homocysteic acid in heavily oxidized proteomics samples.Detailed map of oxidative post-translational modifications of human p21ras using Fourier transform mass spectrometry.Mass spectrometry-based protein footprinting characterizes the structures of oligomeric apolipoprotein E2, E3, and E4.Analysis of the oxidative damage-induced conformational changes of apo- and holocalmodulin by dose-dependent protein oxidative surface mapping.Conformational dynamics of activation for the pentameric complex of dimeric G protein-coupled receptor and heterotrimeric G protein.Probing structures of large protein complexes using zero-length cross-linking.Functional site profiling and electrostatic analysis of cysteines modifiable to cysteine sulfenic acid.Radiofluorination using aluminum-fluoride (Al18F)Protein oxidation: role in signalling and detection by mass spectrometry.High-resolution MS for structural characterization of protein therapeutics: advances and future directions.Comparative study of the oxidation behavior of sulfur-containing amino acids and glutathione by electrochemistry-mass spectrometry in the presence and absence of cisplatin.Cyclic voltammetry: a new strategy for the evaluation of oxidative damage to bovine insulin.Studies toward the analysis of S-nitrosoproteins.Radiation chemical studies of Gly-Met-Gly in aqueous solution.Potential allergenicity response to structural modification of irradiated bovine α-lactalbumin.Characterization of an alternative low energy fold for bovine α-lactalbumin formed by disulfide bond shuffling.
P2860
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P2860
Radiolytic modification of sulfur-containing amino acid residues in model peptides: fundamental studies for protein footprinting.
description
2005 nî lūn-bûn
@nan
2005 թուականի Ապրիլին հրատարակուած գիտական յօդուած
@hyw
2005 թվականի ապրիլին հրատարակված գիտական հոդված
@hy
2005年の論文
@ja
2005年論文
@yue
2005年論文
@zh-hant
2005年論文
@zh-hk
2005年論文
@zh-mo
2005年論文
@zh-tw
2005年论文
@wuu
name
Radiolytic modification of sul ...... dies for protein footprinting.
@ast
Radiolytic modification of sul ...... dies for protein footprinting.
@en
type
label
Radiolytic modification of sul ...... dies for protein footprinting.
@ast
Radiolytic modification of sul ...... dies for protein footprinting.
@en
prefLabel
Radiolytic modification of sul ...... dies for protein footprinting.
@ast
Radiolytic modification of sul ...... dies for protein footprinting.
@en
P356
P1433
P1476
Radiolytic modification of sul ...... dies for protein footprinting.
@en
P2093
Guozhong Xu
Mark R Chance
P304
P356
10.1021/AC0484629
P407
P577
2005-04-01T00:00:00Z