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    Thermo Fisher thermo hybrid linear ion trap orbitrap mass spectrometer
    Thermo Hybrid Linear Ion Trap Orbitrap Mass Spectrometer, supplied by Thermo Fisher, used in various techniques. Bioz Stars score: 99/100, based on 9 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
    https://www.bioz.com/result/thermo hybrid linear ion trap orbitrap mass spectrometer/product/Thermo Fisher
    Average 99 stars, based on 9 article reviews
    Price from $9.99 to $1999.99
    thermo hybrid linear ion trap orbitrap mass spectrometer - by Bioz Stars, 2020-08
    99/100 stars
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    99
    Thermo Fisher hybrid linear ion trap orbitrap mass spectrometer
    Quality control after cross-link identification at a 5% link FDR. (a) Results from cross-linking HSA with sulfo-SDA acquired on an Q Exactive and an LTQ <t>Orbitrap</t> Velos mass spectrometer. The line at 25 Å indicates the distance cutoff for links classified as long distance. The inlet shows the fraction of long-distance links (LDL) in each data set. (b) Score comparison between within-distance linkzs and LDL. LDL showed no significant (ns) deviation from the within-distance links (two-sided Mann–Whitney-U-test at α = 0.05).
    Hybrid Linear Ion Trap Orbitrap Mass Spectrometer, supplied by Thermo Fisher, used in various techniques. Bioz Stars score: 99/100, based on 917 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
    https://www.bioz.com/result/hybrid linear ion trap orbitrap mass spectrometer/product/Thermo Fisher
    Average 99 stars, based on 917 article reviews
    Price from $9.99 to $1999.99
    hybrid linear ion trap orbitrap mass spectrometer - by Bioz Stars, 2020-08
    99/100 stars
      Buy from Supplier

    Image Search Results


    Quality control after cross-link identification at a 5% link FDR. (a) Results from cross-linking HSA with sulfo-SDA acquired on an Q Exactive and an LTQ Orbitrap Velos mass spectrometer. The line at 25 Å indicates the distance cutoff for links classified as long distance. The inlet shows the fraction of long-distance links (LDL) in each data set. (b) Score comparison between within-distance linkzs and LDL. LDL showed no significant (ns) deviation from the within-distance links (two-sided Mann–Whitney-U-test at α = 0.05).

    Journal: Analytical Chemistry

    Article Title: Noncovalently Associated Peptides Observed during Liquid Chromatography-Mass Spectrometry and Their Effect on Cross-Link Analyses

    doi: 10.1021/acs.analchem.8b04037

    Figure Lengend Snippet: Quality control after cross-link identification at a 5% link FDR. (a) Results from cross-linking HSA with sulfo-SDA acquired on an Q Exactive and an LTQ Orbitrap Velos mass spectrometer. The line at 25 Å indicates the distance cutoff for links classified as long distance. The inlet shows the fraction of long-distance links (LDL) in each data set. (b) Score comparison between within-distance linkzs and LDL. LDL showed no significant (ns) deviation from the within-distance links (two-sided Mann–Whitney-U-test at α = 0.05).

    Article Snippet: We observed surprising differences when comparing the identified cross-links using data acquired on two different mass spectrometers: a hybrid linear ion trap-Orbitrap mass spectrometer (LTQ Orbitrap Velos, Thermo Fisher Scientific) and a hybrid quadrupole-Orbitrap mass spectrometer (Q Exactive, Thermo Fisher Scientific).

    Techniques: Mass Spectrometry, MANN-WHITNEY

    Mass spectrometry-based identification of the Vel antigen carrier as SMIM1. A. The top panel shows the high resolution MS/MS spectrum acquired in the orbitrap mass spectrometer corresponding to the SMIM1 peptide PQESHVHY that was annotated following de novo peptide sequencing as described in the Methods Section. The bottom panel provides the corresponding calculated (calc.) and observed (obs.) m / z values of the singly charged y- and b-type ions. B. Schematic representation of the SMIM1 protein showing the predicted transmembrane domain, the peptides that were identified by mass spectrometry, and the three cysteine residues potentially involved in dimer formation.

    Journal: EMBO Molecular Medicine

    Article Title: Disruption of SMIM1 causes the Vel- blood type

    doi: 10.1002/emmm.201302466

    Figure Lengend Snippet: Mass spectrometry-based identification of the Vel antigen carrier as SMIM1. A. The top panel shows the high resolution MS/MS spectrum acquired in the orbitrap mass spectrometer corresponding to the SMIM1 peptide PQESHVHY that was annotated following de novo peptide sequencing as described in the Methods Section. The bottom panel provides the corresponding calculated (calc.) and observed (obs.) m / z values of the singly charged y- and b-type ions. B. Schematic representation of the SMIM1 protein showing the predicted transmembrane domain, the peptides that were identified by mass spectrometry, and the three cysteine residues potentially involved in dimer formation.

    Article Snippet: These procedures were performed as described previously (Ballif et al, ) except that digestion with chymotrypsin (12.5 ng/µl) occurred at room temperature for 2 h. Extracted and dried peptides were subjected to liquid chromatography tandem mass spectrometry (LC–MS/MS) analysis using a linear ion trap-orbitrap hybrid mass spectrometer (LTQ-orbitrap, Thermo-Electron, San Jose, CA) set up as described previously (Haas et al, ; Roskens et al, ).

    Techniques: Mass Spectrometry, Sequencing

    Influence of the potential applied to the ESI source on retention of UDP-sugars. Chromatogram obtained with a newly installed or regenerated PGC column ( a ); chromatogram obtained after 20-min utilization of the column connected to the ESI source of an Orbitrap mass spectrometer ( b ). Conditions: column regeneration was performed with 80 % acetonitrile in water containing 0.10 % trifluoroacetic acid for 20 min, the sample measurements were done with the gradient program described in the materials and methods section for HPLC-MS; detection, UV, 262 nm; sample. UDP-Gal (100 μmol L −1 ) and UDP-Glc (100 μmol L −1 )

    Journal: Analytical and Bioanalytical Chemistry

    Article Title: Quantitative HPLC-MS analysis of nucleotide sugars in plant cells following off-line SPE sample preparation

    doi: 10.1007/s00216-014-7746-3

    Figure Lengend Snippet: Influence of the potential applied to the ESI source on retention of UDP-sugars. Chromatogram obtained with a newly installed or regenerated PGC column ( a ); chromatogram obtained after 20-min utilization of the column connected to the ESI source of an Orbitrap mass spectrometer ( b ). Conditions: column regeneration was performed with 80 % acetonitrile in water containing 0.10 % trifluoroacetic acid for 20 min, the sample measurements were done with the gradient program described in the materials and methods section for HPLC-MS; detection, UV, 262 nm; sample. UDP-Gal (100 μmol L −1 ) and UDP-Glc (100 μmol L −1 )

    Article Snippet: Fragmentation experiments were performed on a linear ion trap–Orbitrap mass spectrometer (Model LTQ Orbitrap XL, Thermo Fisher Scientific).

    Techniques: Pyrolysis Gas Chromatography, Mass Spectrometry, High Performance Liquid Chromatography, Gas Chromatography

    (a) CID on the LTQ-Orbitrap of the crosslinked homodimer synthetic peptide (Ac-QIGKGVAR) results in the same two major cleavage events observed in MALDI at the intrinsic positive charges. (b) MS 3 of the fragment without an intrinsic positive charge produces

    Journal: Journal of the American Society for Mass Spectrometry

    Article Title: Quaternary Diamines as Mass Spectrometry Cleavable Crosslinkers for Protein Interactions

    doi: 10.1007/s13361-011-0288-4

    Figure Lengend Snippet: (a) CID on the LTQ-Orbitrap of the crosslinked homodimer synthetic peptide (Ac-QIGKGVAR) results in the same two major cleavage events observed in MALDI at the intrinsic positive charges. (b) MS 3 of the fragment without an intrinsic positive charge produces

    Article Snippet: The crosslinked standard peptides were analyzed with a hybrid linear quadrupole ion trap-Orbitrap mass spectrometer (ThermoFisher Scientific, Inc. model LTQ-Orbitrap XL; San Jose, CA, USA).

    Techniques: Mass Spectrometry

    Overview of the analytical workflow used in this study. Mixed population of T. thermophila cells was harvested and lysed in urea lysis buffer. After Lys-C/trypsin digestion, phosphopeptides were enriched by TiO 2 , loaded onto the biphasic (strong cation exchange and reverse-phase C 18 ) capillary column, and analyzed with an LTQ Orbitrap XL mass spectrometer. Mascot and MSQuant were used for phosphopeptide identification and post-translational modification (PTM) score analysis.

    Journal: Molecular & Cellular Proteomics : MCP

    Article Title: Phosphoproteomic Analysis of Protein Phosphorylation Networks in Tetrahymena thermophila, a Model Single-celled Organism *

    doi: 10.1074/mcp.M112.026575

    Figure Lengend Snippet: Overview of the analytical workflow used in this study. Mixed population of T. thermophila cells was harvested and lysed in urea lysis buffer. After Lys-C/trypsin digestion, phosphopeptides were enriched by TiO 2 , loaded onto the biphasic (strong cation exchange and reverse-phase C 18 ) capillary column, and analyzed with an LTQ Orbitrap XL mass spectrometer. Mascot and MSQuant were used for phosphopeptide identification and post-translational modification (PTM) score analysis.

    Article Snippet: After loading, the peptides were analyzed on an Eksigent HPLC system (Dublin, CA) coupled with a linear ion trap LTQ-Orbitrap XL mass spectrometer (Thermo Fisher Scientific, Waltham, MA) as described by Hou et al. ( ).

    Techniques: Lysis, Mass Spectrometry, Modification