Laser flash photolysis of hydrogen peroxide to oxidize protein solvent-accessible residues on the microsecond timescale. - Wikidata - wikimedia - TriplyDB

Laser flash photolysis of hydrogen peroxide to oxidize protein solvent-accessible residues on the microsecond timescale.

Laser flash photolysis of hydrogen peroxide to oxidize protein solvent-accessible residues on the microsecond timescale.

http://www.wikidata.org/entity/Q30351743

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Dynamic Viral Glycoprotein Machines: Approaches for Probing Transient States That Drive Membrane Fusion Topological mapping methods for α-helical bacterial membrane proteins--an update and a guide Multiple Functional Roles of the Accessory I-Domain of Bacteriophage P22 Coat Protein Revealed by NMR Structure and CryoEM Modeling The diverse and expanding role of mass spectrometry in structural and molecular biology Unlocking the secrets to protein-protein interface drug targets using structural mass spectrometry techniques Protein Structural Analysis via Mass Spectrometry-Based Proteomics A Dynamic Model of pH-Induced Protein G'e Higher Order Structure Changes derived from Mass Spectrometric Analyses Elucidating in vivo structural dynamics in integral membrane protein by hydroxyl radical footprinting Improved identification and relative quantification of sites of peptide and protein oxidation for hydroxyl radical footprinting.Development of a microsecond X-ray protein footprinting facility at the Advanced Light Source.Quantitative mapping of protein structure by hydroxyl radical footprinting-mediated structural mass spectrometry: a protection factor analysis.Using hydroxyl radical footprinting to explore the free energy landscape of protein folding.Supercharging by m-NBA Improves ETD-Based Quantification of Hydroxyl Radical Protein Footprinting.Pulsed electron beam water radiolysis for submicrosecond hydroxyl radical protein footprinting Aliphatic peptidyl hydroperoxides as a source of secondary oxidation in hydroxyl radical protein footprinting.Investigating Therapeutic Protein Structure with Diethylpyrocarbonate Labeling and Mass Spectrometry.Hydroxyl Radical Dosimetry for High Flux Hydroxyl Radical Protein Footprinting Applications Using a Simple Optical Detection Method.Integrated algorithms for high-throughput examination of covalently labeled biomolecules by structural mass spectrometry.Visualizing 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.Protein Footprinting Comes of Age: Mass Spectrometry for Biophysical Structure Assessment.Diethylpyrocarbonate labeling for the structural analysis of proteins: label scrambling in solution and how to avoid it.Integrating mass spectrometry of intact protein complexes into structural proteomics Mapping molecular flexibility of proteins with site-directed spin labeling: a case study of myoglobin.Probing the paramyxovirus fusion (F) protein-refolding event from pre- to postfusion by oxidative footprinting.Fast photochemical oxidation of proteins for comparing solvent-accessibility changes accompanying protein folding: data processing and application to barstar Three-dimensional structure of cofilin bound to monomeric actin derived by structural mass spectrometry data.Synchrotron 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.Fast photochemical oxidation of proteins for comparing structures of protein-ligand complexes: the calmodulin-peptide model system.Quantitative Protein Topography Measurements by High Resolution Hydroxyl Radical Protein Footprinting Enable Accurate Molecular Model Selection Protein painting reveals solvent-excluded drug targets hidden within native protein-protein interfaces.Oxidative protein labeling in mass-spectrometry-based proteomics.Conversion of methionine into homocysteic acid in heavily oxidized proteomics samples.Sulfate radical anion as a new reagent for fast photochemical oxidation of proteins.Temperature jump and fast photochemical oxidation probe submillisecond protein folding.

P2860

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P2860

Laser flash photolysis of hydrogen peroxide to oxidize protein solvent-accessible residues on the microsecond timescale.

http://www.wikidata.org/entity/Q30351743

description

2005 nî lūn-bûn

@nan

2005 թուականի Նոյեմբերին հրատարակուած գիտական յօդուած

@hyw

2005 թվականի նոյեմբերին հրատարակված գիտական հոդված

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2005年の論文

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2005年学术文章

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2005年学术文章

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2005年学术文章

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2005年学术文章

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2005年学术文章

@zh-sg

2005年學術文章

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name

Laser flash photolysis of hydr ...... on the microsecond timescale.

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Laser flash photolysis of hydr ...... on the microsecond timescale.

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type

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Laser flash photolysis of hydr ...... on the microsecond timescale.

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Laser flash photolysis of hydr ...... on the microsecond timescale.

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prefLabel

Laser flash photolysis of hydr ...... on the microsecond timescale.

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Laser flash photolysis of hydr ...... on the microsecond timescale.

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J.JASMS.2005.09.008

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Journal of the American Society for Mass Spectrometry

P1476

Laser flash photolysis of hydr ...... on the microsecond timescale.

@en

P2093

David M Hambly

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Michael L Gross

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P2860

Electrospray-assisted modification of proteins: a radical probe of protein structure.

Determination of macromolecular folding and structure by synchrotron x-ray radiolysis techniques.

Hydroxyl radical probe of protein surfaces using synchrotron X-ray radiolysis and mass spectrometry.

Radiolytic modification of basic amino acid residues in peptides: probes for examining protein-protein interactions.

Quantification of protein-ligand interactions by mass spectrometry, titration, and H/D exchange: PLIMSTEX.

Probing the folding and unfolding dynamics of secondary and tertiary structures in a three-helix bundle protein.

Nanosecond laser-induced photochemical oxidation method for protein surface mapping with mass spectrometry.

Photochemical and electrophysical production of radicals on millisecond timescales to probe the structure, dynamics and interactions of proteins.

Fast events in protein folding: relaxation dynamics of secondary and tertiary structure in native apomyoglobin.

Fast events in protein folding: helix melting and formation in a small peptide.

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j.jasms.2005.09.008

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