Nanosecond laser-induced photochemical oxidation method for protein surface mapping with mass spectrometry.
about
The diverse and expanding role of mass spectrometry in structural and molecular biologyMultiple proteases to localize oxidation sitesElucidating in vivo structural dynamics in integral membrane protein by hydroxyl radical footprintingLaser flash photolysis of hydrogen peroxide to oxidize protein solvent-accessible residues on the microsecond timescale.Development of a microsecond X-ray protein footprinting facility at the Advanced Light Source.Pulsed electron beam water radiolysis for submicrosecond hydroxyl radical protein footprintingVisualizing water molecules in transmembrane proteins using radiolytic labeling methods.Probing the Time Scale of FPOP (Fast Photochemical Oxidation of Proteins): Radical Reactions Extend Over Tens of Milliseconds.Future directions of structural mass spectrometry using hydroxyl radical footprinting.Effects of Fe(II)/H2O2 oxidation on ubiquitin conformers measured by ion mobility-mass spectrometry.Fast photochemical oxidation of proteins for comparing solvent-accessibility changes accompanying protein folding: data processing and application to barstarComparative informatics analysis to evaluate site-specific protein oxidation in multidimensional LC-MS/MS dataSynchrotron X-ray footprinting as a method to visualize water in proteins.Quantifying 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.Structural characterization of semen coagulum-derived SEM1(86-107) amyloid fibrils that enhance HIV-1 infection.Cold chemical oxidation of proteins.Oxidative protein labeling in mass-spectrometry-based proteomics.Fast Fenton footprinting: a laboratory-based method for the time-resolved analysis of DNA, RNA and proteinsStructural NMR of protein oligomers using hybrid methods.Modeling of the DNA-binding site of yeast Pms1 by mass spectrometry.In vitro oxidative footprinting provides insight into apolipoprotein B-100 structure in low-density lipoprotein.Advances in radical probe mass spectrometry for protein footprinting in chemical biology applications.Mass spectrometry-based protein footprinting characterizes the structures of oligomeric apolipoprotein E2, E3, and E4.Fast photochemical oxidation of proteins for epitope mappingHigh structural resolution hydroxyl radical protein footprinting reveals an extended Robo1-heparin binding interface.Analysis of the oxidative damage-induced conformational changes of apo- and holocalmodulin by dose-dependent protein oxidative surface mapping.Elucidating the higher-order structure of biopolymers by structural probing and mass spectrometry: MS3DProbing the pH-dependent prepore to pore transition of Bacillus anthracis protective antigen with differential oxidative protein footprintingComplementing global measures of RNA folding with local reports of backbone solvent accessibility by time resolved hydroxyl radical footprinting.Carbene footprinting accurately maps binding sites in protein-ligand and protein-protein interactions.Mass spectrometry for the biophysical characterization of therapeutic monoclonal antibodiesStructural Analysis of the Glycosylated Intact HIV-1 gp120-b12 Antibody Complex Using Hydroxyl Radical Protein Footprinting.The impact of mass spectrometry on the study of intact antibodies: from post-translational modifications to structural analysis.High-resolution MS for structural characterization of protein therapeutics: advances and future directions.Painting proteins with covalent labels: what's in the picture?Fast photochemical oxidation of proteins (FPOP) maps the epitope of EGFR binding to adnectin.Modifications generated by fast photochemical oxidation of proteins reflect the native conformations of proteins.Covalent labeling-mass spectrometry with non-specific reagents for studying protein structure and interactionsVariation in FPOP Measurements Is Primarily Caused by Poor Peptide Signal Intensity
P2860
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P2860
Nanosecond laser-induced photochemical oxidation method for protein surface mapping with mass spectrometry.
description
2005 nî lūn-bûn
@nan
2005 թուականի Սեպտեմբերին հրատարակուած գիտական յօդուած
@hyw
2005 թվականի սեպտեմբերին 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
Nanosecond laser-induced photo ...... apping with mass spectrometry.
@ast
Nanosecond laser-induced photo ...... apping with mass spectrometry.
@en
type
label
Nanosecond laser-induced photo ...... apping with mass spectrometry.
@ast
Nanosecond laser-induced photo ...... apping with mass spectrometry.
@en
prefLabel
Nanosecond laser-induced photo ...... apping with mass spectrometry.
@ast
Nanosecond laser-induced photo ...... apping with mass spectrometry.
@en
P356
P1433
P1476
Nanosecond laser-induced photo ...... apping with mass spectrometry.
@en
P2093
Siu Kwan Sze
Thin Thin Aye
P304
P356
10.1021/AC050353M
P407
P50
P577
2005-09-01T00:00:00Z