Radiolytic modification of basic amino acid residues in peptides: probes for examining protein-protein interactions.
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Protein Structural Analysis via Mass Spectrometry-Based ProteomicsStructural analysis of gelsolin using synchrotron protein footprinting.Laser flash photolysis of hydrogen peroxide to oxidize protein solvent-accessible residues on the microsecond timescale.Improved identification and relative quantification of sites of peptide and protein oxidation for hydroxyl radical footprinting.Characterizing monoclonal antibody structure by carbodiimide/GEE footprintingIntegrated algorithms for high-throughput examination of covalently labeled biomolecules by structural mass spectrometry.Visualizing water molecules in transmembrane proteins using radiolytic labeling methods.Future directions of structural mass spectrometry using hydroxyl radical footprinting.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.Quantitative Protein Topography Measurements by High Resolution Hydroxyl Radical Protein Footprinting Enable Accurate Molecular Model SelectionEconomical evolution: microbes reduce the synthetic cost of extracellular proteins.Complex pathways in folding of protein G explored by simulation and experiment.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.SOLEIL shining on the solution-state structure of biomacromolecules by synchrotron X-ray footprinting at the Metrology beamline.Structural glycobiology: a game of snakes and ladders.Selenocysteine confers resistance to inactivation by oxidation in thioredoxin reductase: comparison of selenium and sulfur enzymesReliable determination of site-specific in vivo protein N-glycosylation based on collision-induced MS/MS and chromatographic retention time.Painting proteins with covalent labels: what's in the picture?Effect of gamma radiation on the structural and biological properties of angiotensin II.Similarities and differences in radiation damage at 100 K versus 160 K in a crystal of thermolysin.A new label-free approach for the determination of reaction rates in oxidative footprinting experiments.Influence of cavitation and high shear stress on HSA aggregation behavior.
P2860
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P2860
Radiolytic modification of basic amino acid residues in peptides: probes for examining protein-protein interactions.
description
2003 nî lūn-bûn
@nan
2003 թուականի Դեկտեմբերին հրատարակուած գիտական յօդուած
@hyw
2003 թվականի դեկտեմբերին հրատարակված գիտական հոդված
@hy
2003年の論文
@ja
2003年論文
@yue
2003年論文
@zh-hant
2003年論文
@zh-hk
2003年論文
@zh-mo
2003年論文
@zh-tw
2003年论文
@wuu
name
Radiolytic modification of bas ...... protein-protein interactions.
@ast
Radiolytic modification of bas ...... protein-protein interactions.
@en
type
label
Radiolytic modification of bas ...... protein-protein interactions.
@ast
Radiolytic modification of bas ...... protein-protein interactions.
@en
prefLabel
Radiolytic modification of bas ...... protein-protein interactions.
@ast
Radiolytic modification of bas ...... protein-protein interactions.
@en
P2093
P356
P1433
P1476
Radiolytic modification of bas ...... protein-protein interactions.
@en
P2093
Guozhong Xu
Keiji Takamoto
Mark R Chance
P304
P356
10.1021/AC035104H
P407
P577
2003-12-01T00:00:00Z