q exactive mass spectrometer Search Results


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  • 99
    Thermo Fisher q exactive hf orbitrap mass spectrometer
    Ser 139 , Thr 206 , and Ser 213 are PKCβ-regulatory sites. A , for <t>mass</t> spectrometry, an in vitro kinase assay was performed with recombinant kinases and p66 as substrate and subjected to SDS-PAGE. The gel was stained with Coomassie or immunoblotted for p66 Ser 36 . B , the protein bands were excised from Coomassie-stained gel and digested with trypsin or Lys C. Both Tryptic ( C ) and Lys C ( D ) digests were analyzed by nano-HPLC coupled via an electrospray ionization interface to a <t>Q</t> <t>Exactive</t> <t>HF</t> mass <t>spectrometer.</t> Data analysis and peak area calculation were performed using Proteome Discoverer 1.4.1.14.
    Q Exactive Hf Orbitrap Mass Spectrometer, supplied by Thermo Fisher, used in various techniques. Bioz Stars score: 99/100, based on 546 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    Thermo Fisher q exactive mass spectrometer
    Workflow of TMT quantitative shotgun proteomic analysis. Proteins extracted from rice leaves were reduced, alkylased, precipitated and digested before being labelled with Tandem Mass Tags. Labelled samples were pooled, fractionated by SCX and then analysed on a Q Exactive <t>Orbitrap</t> mass spectrometer. Raw data generated from the mass spectrometer were processed using Proteome Discover v1.4 and Mascot. The search results were further analysed by the TMTPrePro software package.
    Q Exactive Mass Spectrometer, supplied by Thermo Fisher, used in various techniques. Bioz Stars score: 99/100, based on 10404 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    Waters Corporation q exactive mass spectrometer
    Workflow of TMT quantitative shotgun proteomic analysis. Proteins extracted from rice leaves were reduced, alkylased, precipitated and digested before being labelled with Tandem Mass Tags. Labelled samples were pooled, fractionated by SCX and then analysed on a Q Exactive <t>Orbitrap</t> mass spectrometer. Raw data generated from the mass spectrometer were processed using Proteome Discover v1.4 and Mascot. The search results were further analysed by the TMTPrePro software package.
    Q Exactive Mass Spectrometer, supplied by Waters Corporation, used in various techniques. Bioz Stars score: 88/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    Thermal Scientific q exactive mass spectrometer
    Workflow of TMT quantitative shotgun proteomic analysis. Proteins extracted from rice leaves were reduced, alkylased, precipitated and digested before being labelled with Tandem Mass Tags. Labelled samples were pooled, fractionated by SCX and then analysed on a Q Exactive <t>Orbitrap</t> mass spectrometer. Raw data generated from the mass spectrometer were processed using Proteome Discover v1.4 and Mascot. The search results were further analysed by the TMTPrePro software package.
    Q Exactive Mass Spectrometer, supplied by Thermal Scientific, used in various techniques. Bioz Stars score: 98/100, based on 11 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    Thermo Fisher q exactive tandem mass spectrometer
    Workflow of TMT quantitative shotgun proteomic analysis. Proteins extracted from rice leaves were reduced, alkylased, precipitated and digested before being labelled with Tandem Mass Tags. Labelled samples were pooled, fractionated by SCX and then analysed on a Q Exactive <t>Orbitrap</t> mass spectrometer. Raw data generated from the mass spectrometer were processed using Proteome Discover v1.4 and Mascot. The search results were further analysed by the TMTPrePro software package.
    Q Exactive Tandem Mass Spectrometer, supplied by Thermo Fisher, used in various techniques. Bioz Stars score: 99/100, based on 115 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    Thermo Fisher q exactive biotech mass spectrometer
    Total ion chromatograms for a) AmB resistant (R) and b) wild type (WT). Extracted sterols were analysed by high resolution accurate <t>mass</t> <t>Q-Exactive</t> <t>GC</t> Orbitrap. Nine unique sterols were identified in the retention time region from 17 to 18.4 min. The identification of these sterols is listed in Table 2 . Asterisks denote polysiloxane contaminant peaks that co-elute with sterol peaks. Three replicates of each extraction show high reproducibility with regard to peak height.
    Q Exactive Biotech Mass Spectrometer, supplied by Thermo Fisher, used in various techniques. Bioz Stars score: 94/100, based on 878 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    Thermo Fisher q exactive quadrupoleorbitrap mass spectrometer
    Orthogonal partial least squares-discriminate analysis (OPLS-DA) of seven Chinese kale cultivars analysed by <t>UHPLC-Quadrupole-Orbitrap</t> MS/MS (the number after the cultivar name stands for the six independent biological replicates of each cultivar). ( a ) Score plot; ( b ) Loading plot.
    Q Exactive Quadrupoleorbitrap Mass Spectrometer, supplied by Thermo Fisher, used in various techniques. Bioz Stars score: 99/100, based on 494 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    Thermo Fisher generation q exactive mass spectrometer
    Orthogonal partial least squares-discriminate analysis (OPLS-DA) of seven Chinese kale cultivars analysed by <t>UHPLC-Quadrupole-Orbitrap</t> MS/MS (the number after the cultivar name stands for the six independent biological replicates of each cultivar). ( a ) Score plot; ( b ) Loading plot.
    Generation Q Exactive Mass Spectrometer, supplied by Thermo Fisher, used in various techniques. Bioz Stars score: 81/100, based on 6 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    Thermo Fisher electrospray q exactive mass spectrometer
    Orthogonal partial least squares-discriminate analysis (OPLS-DA) of seven Chinese kale cultivars analysed by <t>UHPLC-Quadrupole-Orbitrap</t> MS/MS (the number after the cultivar name stands for the six independent biological replicates of each cultivar). ( a ) Score plot; ( b ) Loading plot.
    Electrospray Q Exactive Mass Spectrometer, supplied by Thermo Fisher, used in various techniques. Bioz Stars score: 89/100, based on 10 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    Thermo Fisher q exactive focus mass spectrometer
    Orthogonal partial least squares-discriminate analysis (OPLS-DA) of seven Chinese kale cultivars analysed by <t>UHPLC-Quadrupole-Orbitrap</t> MS/MS (the number after the cultivar name stands for the six independent biological replicates of each cultivar). ( a ) Score plot; ( b ) Loading plot.
    Q Exactive Focus Mass Spectrometer, supplied by Thermo Fisher, used in various techniques. Bioz Stars score: 99/100, based on 169 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    Thermo Fisher q exactive mass spectrometer system
    Orthogonal partial least squares-discriminate analysis (OPLS-DA) of seven Chinese kale cultivars analysed by <t>UHPLC-Quadrupole-Orbitrap</t> MS/MS (the number after the cultivar name stands for the six independent biological replicates of each cultivar). ( a ) Score plot; ( b ) Loading plot.
    Q Exactive Mass Spectrometer System, supplied by Thermo Fisher, used in various techniques. Bioz Stars score: 99/100, based on 44 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    Thermo Fisher uhplc q exactive mass spectrometer
    Orthogonal partial least squares-discriminate analysis (OPLS-DA) of seven Chinese kale cultivars analysed by <t>UHPLC-Quadrupole-Orbitrap</t> MS/MS (the number after the cultivar name stands for the six independent biological replicates of each cultivar). ( a ) Score plot; ( b ) Loading plot.
    Uhplc Q Exactive Mass Spectrometer, supplied by Thermo Fisher, used in various techniques. Bioz Stars score: 80/100, based on 3 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    Thermo Fisher q exactive proteomic mass spectrometer
    Orthogonal partial least squares-discriminate analysis (OPLS-DA) of seven Chinese kale cultivars analysed by <t>UHPLC-Quadrupole-Orbitrap</t> MS/MS (the number after the cultivar name stands for the six independent biological replicates of each cultivar). ( a ) Score plot; ( b ) Loading plot.
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    Thermo Fisher autosampler q exactive q orbitrap mass spectrometer
    Orthogonal partial least squares-discriminate analysis (OPLS-DA) of seven Chinese kale cultivars analysed by <t>UHPLC-Quadrupole-Orbitrap</t> MS/MS (the number after the cultivar name stands for the six independent biological replicates of each cultivar). ( a ) Score plot; ( b ) Loading plot.
    Autosampler Q Exactive Q Orbitrap Mass Spectrometer, supplied by Thermo Fisher, used in various techniques. Bioz Stars score: 88/100, based on 8 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    Image Search Results


    Ser 139 , Thr 206 , and Ser 213 are PKCβ-regulatory sites. A , for mass spectrometry, an in vitro kinase assay was performed with recombinant kinases and p66 as substrate and subjected to SDS-PAGE. The gel was stained with Coomassie or immunoblotted for p66 Ser 36 . B , the protein bands were excised from Coomassie-stained gel and digested with trypsin or Lys C. Both Tryptic ( C ) and Lys C ( D ) digests were analyzed by nano-HPLC coupled via an electrospray ionization interface to a Q Exactive HF mass spectrometer. Data analysis and peak area calculation were performed using Proteome Discoverer 1.4.1.14.

    Journal: The Journal of Biological Chemistry

    Article Title: Novel Insights into the PKCβ-dependent Regulation of the Oxidoreductase p66Shc *

    doi: 10.1074/jbc.M116.752766

    Figure Lengend Snippet: Ser 139 , Thr 206 , and Ser 213 are PKCβ-regulatory sites. A , for mass spectrometry, an in vitro kinase assay was performed with recombinant kinases and p66 as substrate and subjected to SDS-PAGE. The gel was stained with Coomassie or immunoblotted for p66 Ser 36 . B , the protein bands were excised from Coomassie-stained gel and digested with trypsin or Lys C. Both Tryptic ( C ) and Lys C ( D ) digests were analyzed by nano-HPLC coupled via an electrospray ionization interface to a Q Exactive HF mass spectrometer. Data analysis and peak area calculation were performed using Proteome Discoverer 1.4.1.14.

    Article Snippet: Tryptic digests were analyzed using an UltiMate 3000 nano-HPLC system (Thermo Scientific, Bremen, Germany) coupled to a Q Exactive Plus or Q Exactive HF mass spectrometer (Thermo Scientific) equipped with a Nanospray Flex ionization source.

    Techniques: Mass Spectrometry, In Vitro, Kinase Assay, Recombinant, SDS Page, Staining, High Performance Liquid Chromatography

    Workflow of TMT quantitative shotgun proteomic analysis. Proteins extracted from rice leaves were reduced, alkylased, precipitated and digested before being labelled with Tandem Mass Tags. Labelled samples were pooled, fractionated by SCX and then analysed on a Q Exactive Orbitrap mass spectrometer. Raw data generated from the mass spectrometer were processed using Proteome Discover v1.4 and Mascot. The search results were further analysed by the TMTPrePro software package.

    Journal: Data in Brief

    Article Title: Label-free and isobaric tandem mass tag (TMT) multiplexed quantitative proteomic data of two contrasting rice cultivars exposed to drought stress and recovery

    doi: 10.1016/j.dib.2018.12.041

    Figure Lengend Snippet: Workflow of TMT quantitative shotgun proteomic analysis. Proteins extracted from rice leaves were reduced, alkylased, precipitated and digested before being labelled with Tandem Mass Tags. Labelled samples were pooled, fractionated by SCX and then analysed on a Q Exactive Orbitrap mass spectrometer. Raw data generated from the mass spectrometer were processed using Proteome Discover v1.4 and Mascot. The search results were further analysed by the TMTPrePro software package.

    Article Snippet: These fractions were desalted using C18 OMIX® tips (Agilent) and analysed on a Q Exactive Orbitrap mass spectrometer (Thermo Scientific) coupled to an EASY-nLC1000 (Thermo Scientific).

    Techniques: Mass Spectrometry, Generated, Software

    Identification of processed POMC peptides by LC-MS/MS. A) Schematic workflow for the quantification of POMC-derived peptides from hPSC-derived hypothalamic neurons. B) Liquid chromatographs of samples from hPSC-derived hypothalamic neurons (top), compared with stable isotope-labelled synthetic d-α-MSH(1-13), β-MSH(1-18) and β-EP (1-31) (bottom). Note that heavy isotope-labelled reference peptides have identical retention times as endogenous peptides but have slightly higher mass-to-charge (m/z) ratios, and that m/z values measured from Orbitrap and triple quadrupole mass spectrometers may differ. C) Schematic of human POMC protein and relevant dibasic cleavage sites (blue), expected POMC-derived peptides, and those peptides detected in hPSC-derived hypothalamic cultures by LC-MS/MS. Detected peptides included γ 1 -MSH (Lys- γ 1 -MSH), d-α-MSH(1-13), β-MSH(1-18) and β-EP (1-31). Quantified peptides are indicated in green. D) Summary of POMC-derived peptides detected by LC-MS/MS, where the colour intensity represents the relative abundance of each peptide species. Repl., replicates. Other abbreviations are as in Figure 1 .

    Journal: Molecular Metabolism

    Article Title: Quantitative mass spectrometry for human melanocortin peptides in vitro and in vivo suggests prominent roles for β-MSH and desacetyl α-MSH in energy homeostasis

    doi: 10.1016/j.molmet.2018.08.006

    Figure Lengend Snippet: Identification of processed POMC peptides by LC-MS/MS. A) Schematic workflow for the quantification of POMC-derived peptides from hPSC-derived hypothalamic neurons. B) Liquid chromatographs of samples from hPSC-derived hypothalamic neurons (top), compared with stable isotope-labelled synthetic d-α-MSH(1-13), β-MSH(1-18) and β-EP (1-31) (bottom). Note that heavy isotope-labelled reference peptides have identical retention times as endogenous peptides but have slightly higher mass-to-charge (m/z) ratios, and that m/z values measured from Orbitrap and triple quadrupole mass spectrometers may differ. C) Schematic of human POMC protein and relevant dibasic cleavage sites (blue), expected POMC-derived peptides, and those peptides detected in hPSC-derived hypothalamic cultures by LC-MS/MS. Detected peptides included γ 1 -MSH (Lys- γ 1 -MSH), d-α-MSH(1-13), β-MSH(1-18) and β-EP (1-31). Quantified peptides are indicated in green. D) Summary of POMC-derived peptides detected by LC-MS/MS, where the colour intensity represents the relative abundance of each peptide species. Repl., replicates. Other abbreviations are as in Figure 1 .

    Article Snippet: 2.9 Peptide discovery by LC-MS/MS Peptide extracts were run using nano-flow-based separation and electrospray approaches on a Thermo Fisher Ultimate 3000 nano-LC system coupled to a Q Exactive Plus Orbitrap mass spectrometer (ThermoScientific, San Jose, USA) as described previously .

    Techniques: Liquid Chromatography with Mass Spectroscopy, Mass Spectrometry, Derivative Assay

    Comparison of mean alkaloid concentrations (parts per million, ppm; mg/kg) in eight different glasshouse-grown ryegrass–endophyte associations using the Thermo Q Exactive Plus (QE) and Agilent 6460C Triple Quadruple (QQQ) mass spectrometers, and the Agilent 1100 fluorescence detector (FLD): ( a ) peramine, ( b ) ergovaline and ( c ) lolitrem B. No alkaloids were detected in Trojan-WE (omitted). Bars represent the standard error of the mean (SEM). Bars with different letters are significantly different when compared to the QE ( t -test, p

    Journal: Toxins

    Article Title: A Simple LC–MS Method for the Quantitation of Alkaloids in Endophyte-Infected Perennial Ryegrass

    doi: 10.3390/toxins11110649

    Figure Lengend Snippet: Comparison of mean alkaloid concentrations (parts per million, ppm; mg/kg) in eight different glasshouse-grown ryegrass–endophyte associations using the Thermo Q Exactive Plus (QE) and Agilent 6460C Triple Quadruple (QQQ) mass spectrometers, and the Agilent 1100 fluorescence detector (FLD): ( a ) peramine, ( b ) ergovaline and ( c ) lolitrem B. No alkaloids were detected in Trojan-WE (omitted). Bars represent the standard error of the mean (SEM). Bars with different letters are significantly different when compared to the QE ( t -test, p

    Article Snippet: Analytical Instruments and Conditions All ryegrass samples, including those used for the validation tests, were analyzed using a Thermo Scientific Vanquish ultra-high-performance liquid chromatography (UHPLC) system (Thermo Fischer Scientific, Bremen, Germany) coupled to a Thermo Fisher Q Exactive Plus mass spectrometer (QE MS) (Waltham, MA, USA; Thermo, Bremen, Germany).

    Techniques: Fluorescence

    Total ion chromatograms for a) AmB resistant (R) and b) wild type (WT). Extracted sterols were analysed by high resolution accurate mass Q-Exactive GC Orbitrap. Nine unique sterols were identified in the retention time region from 17 to 18.4 min. The identification of these sterols is listed in Table 2 . Asterisks denote polysiloxane contaminant peaks that co-elute with sterol peaks. Three replicates of each extraction show high reproducibility with regard to peak height.

    Journal: PLoS Neglected Tropical Diseases

    Article Title: Sterol 14α-demethylase mutation leads to amphotericin B resistance in Leishmania mexicana

    doi: 10.1371/journal.pntd.0005649

    Figure Lengend Snippet: Total ion chromatograms for a) AmB resistant (R) and b) wild type (WT). Extracted sterols were analysed by high resolution accurate mass Q-Exactive GC Orbitrap. Nine unique sterols were identified in the retention time region from 17 to 18.4 min. The identification of these sterols is listed in Table 2 . Asterisks denote polysiloxane contaminant peaks that co-elute with sterol peaks. Three replicates of each extraction show high reproducibility with regard to peak height.

    Article Snippet: Eluting peaks were transferred through an auxiliary transfer temperature of 275°C into a Q-Exactive GC mass spectrometer (Thermo Scientific).

    Techniques:

    Orthogonal partial least squares-discriminate analysis (OPLS-DA) of seven Chinese kale cultivars analysed by UHPLC-Quadrupole-Orbitrap MS/MS (the number after the cultivar name stands for the six independent biological replicates of each cultivar). ( a ) Score plot; ( b ) Loading plot.

    Journal: Molecules : A Journal of Synthetic Chemistry and Natural Product Chemistry

    Article Title: Evaluation of the Nutritional Quality of Chinese Kale (Brassica alboglabra Bailey) Using UHPLC-Quadrupole-Orbitrap MS/MS-Based Metabolomics

    doi: 10.3390/molecules22081262

    Figure Lengend Snippet: Orthogonal partial least squares-discriminate analysis (OPLS-DA) of seven Chinese kale cultivars analysed by UHPLC-Quadrupole-Orbitrap MS/MS (the number after the cultivar name stands for the six independent biological replicates of each cultivar). ( a ) Score plot; ( b ) Loading plot.

    Article Snippet: Mass spectrometry analysis was performed on a Q Exactive Quadrupole-Orbitrap mass spectrometer (Thermo Fisher Scientific, Bremen, Germany), which was equipped with a heated electrospray ionization source II (HESI-II) operating in negative ionization mode.

    Techniques: Mass Spectrometry

    Principles of discovery and targeted proteomics approaches. Major steps of discovery and targeted mass spectrometry analyses are schematized. Discovery proteomics (top panel) characterizes the global composition of a protein sample. With the quadrupole-orbitrap technology, peptide ions within a small window of mass-to-charge (m/z) ratio are isolated in the first quadrupole (Q1) and then fragmented in a collision cell; all ion fragments are finally monitored in the orbitrap analyzer. The processing of resulting MS/MS spectra allows identifying the proteins initially present in the samples (not shown). Targeted proteomics (bottom panel) precisely quantifies a predefined set of proteins. The SRM methodology first selects peptide ions representative of the proteins of interest in the first quadrupole (Q1); they are fragmented in the second quadrupole (Q2); finally, predefined representative ion fragments (F1, F2 and F3) are recorded in the last quadrupole (Q3). The reconstitution of each peptide elution profile, named SRM trace, allows for the integration and quantification of its abundance. The PRM methodology is similar to the SRM pipeline but the last quantification step is not restricted to a predefined set of fragment ions and can consider all of them, recorded in the Orbitrap analyzer

    Journal: Epigenetics & Chromatin

    Article Title: Systematic quantitative analysis of H2A and H2B variants by targeted proteomics

    doi: 10.1186/s13072-017-0172-y

    Figure Lengend Snippet: Principles of discovery and targeted proteomics approaches. Major steps of discovery and targeted mass spectrometry analyses are schematized. Discovery proteomics (top panel) characterizes the global composition of a protein sample. With the quadrupole-orbitrap technology, peptide ions within a small window of mass-to-charge (m/z) ratio are isolated in the first quadrupole (Q1) and then fragmented in a collision cell; all ion fragments are finally monitored in the orbitrap analyzer. The processing of resulting MS/MS spectra allows identifying the proteins initially present in the samples (not shown). Targeted proteomics (bottom panel) precisely quantifies a predefined set of proteins. The SRM methodology first selects peptide ions representative of the proteins of interest in the first quadrupole (Q1); they are fragmented in the second quadrupole (Q2); finally, predefined representative ion fragments (F1, F2 and F3) are recorded in the last quadrupole (Q3). The reconstitution of each peptide elution profile, named SRM trace, allows for the integration and quantification of its abundance. The PRM methodology is similar to the SRM pipeline but the last quantification step is not restricted to a predefined set of fragment ions and can consider all of them, recorded in the Orbitrap analyzer

    Article Snippet: PRM analyses of histones on a Q-Exactive Instrument PRM analyses were performed using a Q-Exactive hybrid quadrupole-orbitrap mass spectrometer (Thermo Fisher Scientific).

    Techniques: Mass Spectrometry, Isolation

    Signature peptides used to quantify H2A and H2B variants by targeted proteomics. a Strategy used to select the signature peptides and validate their compatibility with targeted proteomic analysis. The sequences of 22 H2A and 3 H2B variants were obtained from our recently published list of mouse histone variants (MS_histone_DB, [ 8 ]). In silico digestion of these sequences produced a theoretical list of peptides, which were ranked according to their computed ESPP score, predictive of their compatibility with MS analysis [ 41 ]. Fifty-five peptides were selected and further analyzed to monitor the potential presence of post-translational modifications, which could interfere with their analysis by targeted proteomics. This analysis excluded seven of them (see Table 1 ). Then, heavy standard peptides, 13 C, 15 N-labeled, were synthesized and analyzed on different MS instruments (LTQ-Orbitrap Velos, QTRAP 5500) to acquire full MS/MS spectra and create spectral libraries. They were used to select up to five more intense SRM transitions for each peptide. b Selected signature peptides presented on their corresponding histone variants. They are presented as black bars and numbered according to Table 1 . Histone fold domains, also called globular domains, are presented as a rectangle for each histone, surrounded by N- and C-terminal tails. H2A (orange), H2B (red), H4 (green)

    Journal: Epigenetics & Chromatin

    Article Title: Systematic quantitative analysis of H2A and H2B variants by targeted proteomics

    doi: 10.1186/s13072-017-0172-y

    Figure Lengend Snippet: Signature peptides used to quantify H2A and H2B variants by targeted proteomics. a Strategy used to select the signature peptides and validate their compatibility with targeted proteomic analysis. The sequences of 22 H2A and 3 H2B variants were obtained from our recently published list of mouse histone variants (MS_histone_DB, [ 8 ]). In silico digestion of these sequences produced a theoretical list of peptides, which were ranked according to their computed ESPP score, predictive of their compatibility with MS analysis [ 41 ]. Fifty-five peptides were selected and further analyzed to monitor the potential presence of post-translational modifications, which could interfere with their analysis by targeted proteomics. This analysis excluded seven of them (see Table 1 ). Then, heavy standard peptides, 13 C, 15 N-labeled, were synthesized and analyzed on different MS instruments (LTQ-Orbitrap Velos, QTRAP 5500) to acquire full MS/MS spectra and create spectral libraries. They were used to select up to five more intense SRM transitions for each peptide. b Selected signature peptides presented on their corresponding histone variants. They are presented as black bars and numbered according to Table 1 . Histone fold domains, also called globular domains, are presented as a rectangle for each histone, surrounded by N- and C-terminal tails. H2A (orange), H2B (red), H4 (green)

    Article Snippet: PRM analyses of histones on a Q-Exactive Instrument PRM analyses were performed using a Q-Exactive hybrid quadrupole-orbitrap mass spectrometer (Thermo Fisher Scientific).

    Techniques: Mass Spectrometry, In Silico, Produced, Labeling, Synthesized