Protein surface topology-probing by selective chemical modification and mass spectrometric peptide mapping.
about
Conformational changes in the NS3 protease from hepatitis C virus strain Bk monitored by limited proteolysis and mass spectrometryStructural elucidation of critical residues involved in binding of human monoclonal antibodies to hepatitis C virus E2 envelope glycoproteinStructural characterization of the conformational change in calbindin-D28k upon calcium binding using differential surface modification analyzed by mass spectrometryProtein structure information from mass spectrometry? Selective titration of arginine residues by sulfonates.Protein compatibility of selected cross-linking reactions for hydrogels.Adsorption-induced changes in ribonuclease A structure and enzymatic activity on solid surfaces.Probing protein structure by amino acid-specific covalent labeling and mass spectrometry.Integrated algorithms for high-throughput examination of covalently labeled biomolecules by structural mass spectrometry.Kinetic study of beta-amyloid residue accessibility using reductive alkylation and mass spectrometry.Characterisation of combinatorial libraries of mucin-2 antigen peptides by high-resolution mass spectrometry.Characterization of a discontinuous epitope of the human immunodeficiency virus (HIV) core protein p24 by epitope excision and differential chemical modification followed by mass spectrometric peptide mapping analysisIdentification of specific HIV-1 reverse transcriptase contacts to the viral RNA:tRNA complex by mass spectrometry and a primary amine selective reagentReaction of hen egg white lysozyme with Fischer-type metallocarbene complexes. Characterization of the conjugates and determination of the metal complex binding sites.Solution- and crystal-phase covalent modification of lysozyme by a purpose-designed organoruthenium complex. A MALDI-TOF MS study of its metal binding sites.Modulation of replication protein A function by its hyperphosphorylation-induced conformational change involving DNA binding domain B.Analysis of protein-protein interaction surfaces using a combination of efficient lysine acetylation and nanoLC-MALDI-MS/MS applied to the E9:Im9 bacteriotoxin--immunity protein complex.Development of indole chemistry to label tryptophan residues in protein for determination of tryptophan surface accessibility.Solution insights into the structure of the Efb/C3 complement inhibitory complex as revealed by lysine acetylation and mass spectrometry.'Fixed charge' chemical derivatization and data dependant multistage tandem mass spectrometry for mapping protein surface residue accessibility.Mapping surface accessibility of the C1r/C1s tetramer by chemical modification and mass spectrometry provides new insights into assembly of the human C1 complex.Contributions of mass spectrometry to structural immunology.New inhibitors of VEGFR-2 targeting the extracellular domain dimerization process.Characterization of a discontinuous epitope of the HIV envelope protein gp120 recognized by a human monoclonal antibody using chemical modification and mass spectrometric analysis.Analysis of the native structure, stability and aggregation of biotinylated human lysozyme.Protein surface mapping using diethylpyrocarbonate with mass spectrometric detectionStudies of biomolecular conformations and conformational dynamics by mass spectrometry.Divergent synthesis and chemical reactivity of bicyclic lactone fragments of complex rearranged spongian diterpenes.Preferential Interactions and the Effect of Protein PEGylation.Förster resonance energy transfer evidence for lysozyme oligomerization in lipid environmentBinding of lysozyme to phospholipid bilayers: evidence for protein aggregation upon membrane associationMapping protein surface accessibility via an electron transfer dissociation selectively cleavable hydrazone probeElucidating the higher-order structure of biopolymers by structural probing and mass spectrometry: MS3DProbing the tertiary structure of proteins by limited proteolysis and mass spectrometry: the case of Minibody.Histone H4 N-terminal acetylation in Kasumi-1 cells treated with depsipeptide determined by acetic acid-urea polyacrylamide gel electrophoresis, amino acid coded mass tagging, and mass spectrometry.Mass spectrometry-based structural proteomics.Characterizing TDP-43 interaction with its RNA targets.Ionic liquid induced dehydration and domain closure in lysozyme: FCS and MD simulation.Pinched multilamellar structure of aggregates of lysozyme and phosphatidylserine-containing membranes revealed by FRET.Surface topology of Minibody by selective chemical modifications and mass spectrometry.Mass spectrometric mapping of fibrinogen conformations at poly(ethylene terephthalate) interfaces.
P2860
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P2860
Protein surface topology-probing by selective chemical modification and mass spectrometric peptide mapping.
description
article científic
@ca
article scientifique
@fr
articolo scientifico
@it
artigo científico
@pt
bilimsel makale
@tr
scientific article published on June 1992
@en
vedecký článok
@sk
vetenskaplig artikel
@sv
videnskabelig artikel
@da
vědecký článek
@cs
name
Protein surface topology-probi ...... spectrometric peptide mapping.
@en
Protein surface topology-probi ...... spectrometric peptide mapping.
@nl
type
label
Protein surface topology-probi ...... spectrometric peptide mapping.
@en
Protein surface topology-probi ...... spectrometric peptide mapping.
@nl
prefLabel
Protein surface topology-probi ...... spectrometric peptide mapping.
@en
Protein surface topology-probi ...... spectrometric peptide mapping.
@nl
P2860
P356
P1476
Protein surface topology-probi ...... spectrometric peptide mapping
@en
P2093
P2860
P304
P356
10.1073/PNAS.89.12.5630
P407
P577
1992-06-01T00:00:00Z