[go: up one dir, main page]

Anderson et al., 2016 - Google Patents

Analyses of histone proteoforms using front-end electron transfer dissociation-enabled orbitrap instruments

Anderson et al., 2016

View HTML
Document ID
13714832555381126252
Author
Anderson L
Karch K
Ugrin S
Coradin M
English A
Sidoli S
Shabanowitz J
Garcia B
Hunt D
Publication year
Publication venue
Molecular & Cellular Proteomics

External Links

Snippet

Histones represent a class of proteins ideally suited to analyses by top-down mass spectrometry due to their relatively small size, the high electron transfer dissociation- compatible charge states they exhibit, and the potential to gain valuable information …
Continue reading at www.sciencedirect.com (HTML) (other versions)

Classifications

    • GPHYSICS
    • G01MEASURING; TESTING
    • G01NINVESTIGATING OR ANALYSING MATERIALS BY DETERMINING THEIR CHEMICAL OR PHYSICAL PROPERTIES
    • G01N33/00Investigating or analysing materials by specific methods not covered by the preceding groups
    • G01N33/48Investigating or analysing materials by specific methods not covered by the preceding groups biological material, e.g. blood, urine; Haemocytometers
    • G01N33/50Chemical analysis of biological material, e.g. blood, urine; Testing involving biospecific ligand binding methods; Immunological testing
    • G01N33/68Chemical analysis of biological material, e.g. blood, urine; Testing involving biospecific ligand binding methods; Immunological testing involving proteins, peptides or amino acids
    • G01N33/6803General methods of protein analysis not limited to specific proteins or families of proteins
    • G01N33/6848Methods of protein analysis involving mass spectrometry
    • GPHYSICS
    • G01MEASURING; TESTING
    • G01NINVESTIGATING OR ANALYSING MATERIALS BY DETERMINING THEIR CHEMICAL OR PHYSICAL PROPERTIES
    • G01N33/00Investigating or analysing materials by specific methods not covered by the preceding groups
    • G01N33/48Investigating or analysing materials by specific methods not covered by the preceding groups biological material, e.g. blood, urine; Haemocytometers
    • G01N33/50Chemical analysis of biological material, e.g. blood, urine; Testing involving biospecific ligand binding methods; Immunological testing
    • G01N33/68Chemical analysis of biological material, e.g. blood, urine; Testing involving biospecific ligand binding methods; Immunological testing involving proteins, peptides or amino acids
    • G01N33/6803General methods of protein analysis not limited to specific proteins or families of proteins
    • G01N33/6842Proteomic analysis of subsets of protein mixtures with reduced complexity, e.g. membrane proteins, phosphoproteins, organelle proteins
    • GPHYSICS
    • G01MEASURING; TESTING
    • G01NINVESTIGATING OR ANALYSING MATERIALS BY DETERMINING THEIR CHEMICAL OR PHYSICAL PROPERTIES
    • G01N33/00Investigating or analysing materials by specific methods not covered by the preceding groups
    • G01N33/48Investigating or analysing materials by specific methods not covered by the preceding groups biological material, e.g. blood, urine; Haemocytometers
    • G01N33/50Chemical analysis of biological material, e.g. blood, urine; Testing involving biospecific ligand binding methods; Immunological testing
    • G01N33/53Immunoassay; Biospecific binding assay
    • GPHYSICS
    • G01MEASURING; TESTING
    • G01NINVESTIGATING OR ANALYSING MATERIALS BY DETERMINING THEIR CHEMICAL OR PHYSICAL PROPERTIES
    • G01N30/00Investigating or analysing materials by separation into components using adsorption, absorption or similar phenomena or using ion-exchange, e.g. chromatography or field flow fractionation
    • G01N30/02Column chromatography
    • G01N30/62Detectors specially adapted therefor
    • G01N30/72Mass spectrometers
    • G01N30/7233Mass spectrometers interfaced to liquid or superfluid chromatograph
    • GPHYSICS
    • G01MEASURING; TESTING
    • G01NINVESTIGATING OR ANALYSING MATERIALS BY DETERMINING THEIR CHEMICAL OR PHYSICAL PROPERTIES
    • G01N2333/00Assays involving biological materials from specific organisms or of a specific nature
    • G01N2333/90Enzymes; Proenzymes
    • G01N2333/914Hydrolases (3)
    • G01N2333/978Hydrolases (3) acting on carbon to nitrogen bonds other than peptide bonds (3.5)

Similar Documents

Publication Publication Date Title
Anderson et al. Analyses of histone proteoforms using front-end electron transfer dissociation-enabled orbitrap instruments
US20210311072A1 (en) Absolute Quantitation of Proteins and Protein Modifications by Mass Spectrometry with Multiplexed Internal Standards
Zolg et al. ProteomeTools: Systematic characterization of 21 post-translational protein modifications by liquid chromatography tandem mass spectrometry (LC-MS/MS) using synthetic peptides
Zhou et al. Advancements in top-down proteomics
CN102395886B (en) Method for quantifying modified peptides
Garcia What does the future hold for top down mass spectrometry?
Garcia et al. Analysis of protein phosphorylation by mass spectrometry
Cox et al. Multiple reaction monitoring as a method for identifying protein posttranslational modifications
Karch et al. Identification and quantification of histone PTMs using high-resolution mass spectrometry
Tolonen et al. Quantitative proteomics using reductive dimethylation for stable isotope labeling
Bonet-Costa et al. Combined bottom-up and top-down mass spectrometry analyses of the pattern of post-translational modifications of Drosophila melanogaster linker histone H1
EP2455751B1 (en) Method for quantifying protein
Sachon et al. Phosphopeptide quantitation using amine‐reactive isobaric tagging reagents and tandem mass spectrometry: application to proteins isolated by gel electrophoresis
JP2016525677A (en) Mass label
Garcia et al. Comprehensive phosphoprotein analysis of linker histone H1 from Tetrahymena thermophila
Chen et al. Quantitative mass spectrometry reveals that intact histone H1 phosphorylations are variant specific and exhibit single molecule hierarchical dependence
Tichy et al. Phosphoproteomics: Searching for a needle in a haystack
Mo et al. Analytical aspects of mass spectrometry and proteomics
WO2013148178A1 (en) Quantification of post-translational modifications on histone proteins with mass spectrometry
Nakazawa et al. Terminal proteomics: N‐and C‐terminal analyses for high‐fidelity identification of proteins using MS
Wang et al. Phosphopeptide detection using automated online IMAC‐capillary LC‐ESI‐MS/MS
Bons et al. Localization and quantification of post-translational modifications of proteins using electron activated dissociation fragmentation on a fast-acquisition time-of-flight mass spectrometer
Stensland et al. Targeted analysis of protein citrullination using chemical modification and tandem mass spectrometry
Liu et al. Approach for identification and quantification of C-terminal peptides: incorporation of isotopic arginine labeling based on oxazolone chemistry
Bensaddek et al. Evaluating the use of HILIC in large-scale, multi dimensional proteomics: Horses for courses?