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  • 99
    Thermo Fisher electrospray ionization source
    Schematic of the CPP method. CPP includes in vivo chemical methylation of lysine residues at the surface of proteins and its detection with mass spectrometry. The flow chart shows each labeling step and the resultant relative measurement of surface accessibility for chemical modification based on mass spectrometric quantification of isotope labeled peptides. Proteins are labeled with isotope defined reagents at solvent exposed lysine residues (K) with two methyl moieties ( 13 CD 3 , heavy) in vivo . Protein are then digested in peptides with the endoproteinase Chymotrypsin, and all newly accessible primary amines labeled with two methyl moieties (CH 3 , light). Peptides are separated by liquid chromatography (LC) and transferred into gas phase by <t>electrospray</t> ionization (nano ESI). High mass resolution (Orbitrap) mass spectra (MS) and fragment ion mass spectra (MS/MS) are acquired. Peptides are identified with a database search using ProLuCID and quantified with Census. The “surfaces of all protein complexes” (SoPaX) algorithm within ProteinClusterQuant (PCQ) determines and compares the relative surface accessibility of lysine residues.
    Electrospray Ionization Source, supplied by Thermo Fisher, used in various techniques. Bioz Stars score: 99/100, based on 1752 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    99
    Agilent technologies esi source
    Annotations of lipids by MS2Analyzer. (a) QTOF MS/MS of digalactosyldiacylglycerol 18:3/16:0 in positive <t>electrospray</t> mode, indicating the neutral loss of the DGDG headgroup from the [M + NH 4 ] + adduct precursor ion as well as m / z differences for product ions indicating both acyl side chains. Note that positional isomers of acyl groups cannot be determined with this method. (b) QTOF MS/MS of phosphatidylglycerol 16:0/16:0 in negative electrospray mode, indicating the characteristic product ions of the phosphatidylglycerol headgroup ( m / z 152.995) and the acyl side chains ( m / z 255.233).
    Esi Source, supplied by Agilent technologies, used in various techniques. Bioz Stars score: 99/100, based on 1197 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    92
    Waters Corporation esi source
    ( a )–( c ): <t>ESI-IMS-MS</t> Driftscope plots showing drift time (x axis) versus m/z (y axis) for β 2 m and variants at pH 6.8. ( a ) wild-type β 2 m, ( b ) single mutant I7A, and ( c ) double mutant I7A/P32G. Insets at the right hand side: the summed, full scan m/z spectra of each protein showing the charge state ions detected.
    Esi Source, supplied by Waters Corporation, used in various techniques. Bioz Stars score: 92/100, based on 529 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    91
    Abbott Laboratories pcr esi ms
    Assessment of factors influencing performance of <t>PCR/ESI-MS.</t>
    Pcr Esi Ms, supplied by Abbott Laboratories, used in various techniques. Bioz Stars score: 91/100, based on 182 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    91
    Thermo Fisher nano esi source
    A peptic peptide identified by <t>nano-LC/ESI-MS/MS.</t> (A) Extracted ion chromatogram of a peptic peptide eluted from an LC column at 34.6 min. This peptide was detected at m/z 892.9, 595.9 and 447.3 as doubly, triply and quadruply charged ions, respectively
    Nano Esi Source, supplied by Thermo Fisher, used in various techniques. Bioz Stars score: 91/100, based on 486 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    93
    Waters Corporation electrospray ionization esi source
    Ultra-performance liquid <t>chromatography-electrospray</t> ionization-quadrupole time-of-flight-mass spectrometry <t>(UPLC-ESI-Q-TOF-MSE)</t> spectra of metabolites in mouse plasma (left) and UPLC-ESI-Q-TOF-MSE spectra of metabolites in microorganisms (right) from the same sample and fragmentation sites in the high energy spectrum. ( A ) Monohydroxylation metabolite, ( B ) dihydroxylation metabolite, ( C ) deoxyartemisinin (de-ART), ( D ) deoxygenation followed by hydroxylation metabolite, ( E ) dihydroartemisinin (DHA) and deoxygenated DHA, ( F ) hydrogenated DHA, and ( G ) hydrogenation followed by deoxidization of DHA. A blue box behind the low-energy fragment ions shows in-source fragment ions and a green box indicates adduct clusters.
    Electrospray Ionization Esi Source, supplied by Waters Corporation, used in various techniques. Bioz Stars score: 93/100, based on 360 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    99
    Thermo Fisher heated electrospray ionization hesi ii probe
    Ultra-performance liquid <t>chromatography-electrospray</t> ionization-quadrupole time-of-flight-mass spectrometry <t>(UPLC-ESI-Q-TOF-MSE)</t> spectra of metabolites in mouse plasma (left) and UPLC-ESI-Q-TOF-MSE spectra of metabolites in microorganisms (right) from the same sample and fragmentation sites in the high energy spectrum. ( A ) Monohydroxylation metabolite, ( B ) dihydroxylation metabolite, ( C ) deoxyartemisinin (de-ART), ( D ) deoxygenation followed by hydroxylation metabolite, ( E ) dihydroartemisinin (DHA) and deoxygenated DHA, ( F ) hydrogenated DHA, and ( G ) hydrogenation followed by deoxidization of DHA. A blue box behind the low-energy fragment ions shows in-source fragment ions and a green box indicates adduct clusters.
    Heated Electrospray Ionization Hesi Ii Probe, supplied by Thermo Fisher, used in various techniques. Bioz Stars score: 99/100, based on 70 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    92
    Shimadzu Corporation lc esi ms
    Ultra-performance liquid <t>chromatography-electrospray</t> ionization-quadrupole time-of-flight-mass spectrometry <t>(UPLC-ESI-Q-TOF-MSE)</t> spectra of metabolites in mouse plasma (left) and UPLC-ESI-Q-TOF-MSE spectra of metabolites in microorganisms (right) from the same sample and fragmentation sites in the high energy spectrum. ( A ) Monohydroxylation metabolite, ( B ) dihydroxylation metabolite, ( C ) deoxyartemisinin (de-ART), ( D ) deoxygenation followed by hydroxylation metabolite, ( E ) dihydroartemisinin (DHA) and deoxygenated DHA, ( F ) hydrogenated DHA, and ( G ) hydrogenation followed by deoxidization of DHA. A blue box behind the low-energy fragment ions shows in-source fragment ions and a green box indicates adduct clusters.
    Lc Esi Ms, supplied by Shimadzu Corporation, used in various techniques. Bioz Stars score: 92/100, based on 201 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    99
    Agilent technologies jet stream electrospray ionization source
    Ultra-performance liquid <t>chromatography-electrospray</t> ionization-quadrupole time-of-flight-mass spectrometry <t>(UPLC-ESI-Q-TOF-MSE)</t> spectra of metabolites in mouse plasma (left) and UPLC-ESI-Q-TOF-MSE spectra of metabolites in microorganisms (right) from the same sample and fragmentation sites in the high energy spectrum. ( A ) Monohydroxylation metabolite, ( B ) dihydroxylation metabolite, ( C ) deoxyartemisinin (de-ART), ( D ) deoxygenation followed by hydroxylation metabolite, ( E ) dihydroartemisinin (DHA) and deoxygenated DHA, ( F ) hydrogenated DHA, and ( G ) hydrogenation followed by deoxidization of DHA. A blue box behind the low-energy fragment ions shows in-source fragment ions and a green box indicates adduct clusters.
    Jet Stream Electrospray Ionization Source, supplied by Agilent technologies, used in various techniques. Bioz Stars score: 99/100, based on 123 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    93
    Shimadzu Corporation esi source
    Ultra-performance liquid <t>chromatography-electrospray</t> ionization-quadrupole time-of-flight-mass spectrometry <t>(UPLC-ESI-Q-TOF-MSE)</t> spectra of metabolites in mouse plasma (left) and UPLC-ESI-Q-TOF-MSE spectra of metabolites in microorganisms (right) from the same sample and fragmentation sites in the high energy spectrum. ( A ) Monohydroxylation metabolite, ( B ) dihydroxylation metabolite, ( C ) deoxyartemisinin (de-ART), ( D ) deoxygenation followed by hydroxylation metabolite, ( E ) dihydroartemisinin (DHA) and deoxygenated DHA, ( F ) hydrogenated DHA, and ( G ) hydrogenation followed by deoxidization of DHA. A blue box behind the low-energy fragment ions shows in-source fragment ions and a green box indicates adduct clusters.
    Esi Source, supplied by Shimadzu Corporation, used in various techniques. Bioz Stars score: 93/100, based on 196 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    94
    Thermo Fisher esi ms
    Ultra-performance liquid <t>chromatography-electrospray</t> ionization-quadrupole time-of-flight-mass spectrometry <t>(UPLC-ESI-Q-TOF-MSE)</t> spectra of metabolites in mouse plasma (left) and UPLC-ESI-Q-TOF-MSE spectra of metabolites in microorganisms (right) from the same sample and fragmentation sites in the high energy spectrum. ( A ) Monohydroxylation metabolite, ( B ) dihydroxylation metabolite, ( C ) deoxyartemisinin (de-ART), ( D ) deoxygenation followed by hydroxylation metabolite, ( E ) dihydroartemisinin (DHA) and deoxygenated DHA, ( F ) hydrogenated DHA, and ( G ) hydrogenation followed by deoxidization of DHA. A blue box behind the low-energy fragment ions shows in-source fragment ions and a green box indicates adduct clusters.
    Esi Ms, supplied by Thermo Fisher, used in various techniques. Bioz Stars score: 94/100, based on 1415 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    92
    Waters Corporation electrospray ionization mass spectrometry esi ms
    <t>Electrospray</t> ionization-tandem mass spectrum of moanachelin gly-D (C14:0).
    Electrospray Ionization Mass Spectrometry Esi Ms, supplied by Waters Corporation, used in various techniques. Bioz Stars score: 92/100, based on 279 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    92
    Waters Corporation electrospray ionization mass spectrometry
    Purification and identification of rLatroeggtoxin-V. ( A ) Chromatogram of RP-HPLC purification of rLatroeggtoxin-V. ( B ) Molecular weight determination of rLatroeggtoxin-V by <t>electrospray</t> ionization mass spectrometry. The m / z value and the number of charges for each rLatroeggtoxin-V ion peak were labeled.
    Electrospray Ionization Mass Spectrometry, supplied by Waters Corporation, used in various techniques. Bioz Stars score: 92/100, based on 246 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    91
    Agilent technologies g1607a ce esi ms sprayer kit
    Purification and identification of rLatroeggtoxin-V. ( A ) Chromatogram of RP-HPLC purification of rLatroeggtoxin-V. ( B ) Molecular weight determination of rLatroeggtoxin-V by <t>electrospray</t> ionization mass spectrometry. The m / z value and the number of charges for each rLatroeggtoxin-V ion peak were labeled.
    G1607a Ce Esi Ms Sprayer Kit, supplied by Agilent technologies, used in various techniques. Bioz Stars score: 91/100, based on 368 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    92
    Agilent technologies electrospray ionization mass spectrometry esi ms
    Purification and identification of rLatroeggtoxin-V. ( A ) Chromatogram of RP-HPLC purification of rLatroeggtoxin-V. ( B ) Molecular weight determination of rLatroeggtoxin-V by <t>electrospray</t> ionization mass spectrometry. The m / z value and the number of charges for each rLatroeggtoxin-V ion peak were labeled.
    Electrospray Ionization Mass Spectrometry Esi Ms, supplied by Agilent technologies, used in various techniques. Bioz Stars score: 92/100, based on 392 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    99
    Thermo Fisher electrospray ionization esi source
    Purification and identification of rLatroeggtoxin-V. ( A ) Chromatogram of RP-HPLC purification of rLatroeggtoxin-V. ( B ) Molecular weight determination of rLatroeggtoxin-V by <t>electrospray</t> ionization mass spectrometry. The m / z value and the number of charges for each rLatroeggtoxin-V ion peak were labeled.
    Electrospray Ionization Esi Source, supplied by Thermo Fisher, used in various techniques. Bioz Stars score: 99/100, based on 520 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    93
    Agilent technologies electrospray ionization mass spectrometry
    Identification of CAM-W produced by recombinant B. subtilis WB 700. ( A ) Analysis of tricine-SDS-PAGE (a) cropped from Supplementary Figure 1 and western blots (b and c) cropped from Supplementary Figures 2 and 3 of the total extracellular proteins from B. subtilis WB700 harboring pDM031 induced without maltose (lane 1) or with maltose (lane 2). These gels were run under the same experimental conditions. The EDDIE and CAM-W bands are indicated by (←) and (← ← ). The bands present in (a) lane 2 were confirmed by western blotting, as shown in (b) and (c). The marker lane contained a broad range protein marker (#P7702, New England Biolabs, USA). ( B ) RP-HPLC analysis of purified CAM-W. ( C ) <t>Electrospray</t> ionization mass spectrometry analysis of purified recombinant CAM-W.
    Electrospray Ionization Mass Spectrometry, supplied by Agilent technologies, used in various techniques. Bioz Stars score: 93/100, based on 315 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    Image Search Results


    Schematic of the CPP method. CPP includes in vivo chemical methylation of lysine residues at the surface of proteins and its detection with mass spectrometry. The flow chart shows each labeling step and the resultant relative measurement of surface accessibility for chemical modification based on mass spectrometric quantification of isotope labeled peptides. Proteins are labeled with isotope defined reagents at solvent exposed lysine residues (K) with two methyl moieties ( 13 CD 3 , heavy) in vivo . Protein are then digested in peptides with the endoproteinase Chymotrypsin, and all newly accessible primary amines labeled with two methyl moieties (CH 3 , light). Peptides are separated by liquid chromatography (LC) and transferred into gas phase by electrospray ionization (nano ESI). High mass resolution (Orbitrap) mass spectra (MS) and fragment ion mass spectra (MS/MS) are acquired. Peptides are identified with a database search using ProLuCID and quantified with Census. The “surfaces of all protein complexes” (SoPaX) algorithm within ProteinClusterQuant (PCQ) determines and compares the relative surface accessibility of lysine residues.

    Journal: bioRxiv

    Article Title: Covalent Protein Painting Reveals Structural Changes in the Proteome in Alzheimer Disease

    doi: 10.1101/2020.01.31.929117

    Figure Lengend Snippet: Schematic of the CPP method. CPP includes in vivo chemical methylation of lysine residues at the surface of proteins and its detection with mass spectrometry. The flow chart shows each labeling step and the resultant relative measurement of surface accessibility for chemical modification based on mass spectrometric quantification of isotope labeled peptides. Proteins are labeled with isotope defined reagents at solvent exposed lysine residues (K) with two methyl moieties ( 13 CD 3 , heavy) in vivo . Protein are then digested in peptides with the endoproteinase Chymotrypsin, and all newly accessible primary amines labeled with two methyl moieties (CH 3 , light). Peptides are separated by liquid chromatography (LC) and transferred into gas phase by electrospray ionization (nano ESI). High mass resolution (Orbitrap) mass spectra (MS) and fragment ion mass spectra (MS/MS) are acquired. Peptides are identified with a database search using ProLuCID and quantified with Census. The “surfaces of all protein complexes” (SoPaX) algorithm within ProteinClusterQuant (PCQ) determines and compares the relative surface accessibility of lysine residues.

    Article Snippet: Following chromatographic separation, peptides were transferred into an Orbitrap Lumos mass spectrometer by electrospray ionization (nanoEasy, Thermo Fisher Scientific).

    Techniques: In Vivo, Methylation, Mass Spectrometry, Labeling, Modification, Liquid Chromatography, Tandem Mass Spectroscopy

    Annotations of lipids by MS2Analyzer. (a) QTOF MS/MS of digalactosyldiacylglycerol 18:3/16:0 in positive electrospray mode, indicating the neutral loss of the DGDG headgroup from the [M + NH 4 ] + adduct precursor ion as well as m / z differences for product ions indicating both acyl side chains. Note that positional isomers of acyl groups cannot be determined with this method. (b) QTOF MS/MS of phosphatidylglycerol 16:0/16:0 in negative electrospray mode, indicating the characteristic product ions of the phosphatidylglycerol headgroup ( m / z 152.995) and the acyl side chains ( m / z 255.233).

    Journal: Analytical Chemistry

    Article Title: MS2Analyzer: A Software for Small Molecule Substructure Annotations from Accurate Tandem Mass Spectra

    doi: 10.1021/ac502818e

    Figure Lengend Snippet: Annotations of lipids by MS2Analyzer. (a) QTOF MS/MS of digalactosyldiacylglycerol 18:3/16:0 in positive electrospray mode, indicating the neutral loss of the DGDG headgroup from the [M + NH 4 ] + adduct precursor ion as well as m / z differences for product ions indicating both acyl side chains. Note that positional isomers of acyl groups cannot be determined with this method. (b) QTOF MS/MS of phosphatidylglycerol 16:0/16:0 in negative electrospray mode, indicating the characteristic product ions of the phosphatidylglycerol headgroup ( m / z 152.995) and the acyl side chains ( m / z 255.233).

    Article Snippet: In order to reduce the impact from different instruments, ionizations, and adducts, only [M + H]+ spectra acquired under positive electrospray ionization from Agilent QTOF 6530 mass spectrometers were used.

    Techniques: Mass Spectrometry

    ( a )–( c ): ESI-IMS-MS Driftscope plots showing drift time (x axis) versus m/z (y axis) for β 2 m and variants at pH 6.8. ( a ) wild-type β 2 m, ( b ) single mutant I7A, and ( c ) double mutant I7A/P32G. Insets at the right hand side: the summed, full scan m/z spectra of each protein showing the charge state ions detected.

    Journal: Journal of the American Society for Mass Spectrometry

    Article Title: Monitoring Copopulated Conformational States During Protein Folding Events Using Electrospray Ionization-Ion Mobility Spectrometry-Mass Spectrometry

    doi: 10.1016/j.jasms.2007.09.017

    Figure Lengend Snippet: ( a )–( c ): ESI-IMS-MS Driftscope plots showing drift time (x axis) versus m/z (y axis) for β 2 m and variants at pH 6.8. ( a ) wild-type β 2 m, ( b ) single mutant I7A, and ( c ) double mutant I7A/P32G. Insets at the right hand side: the summed, full scan m/z spectra of each protein showing the charge state ions detected.

    Article Snippet: ESI-IMS-MS Analyses Samples were infused into the ESI source of a Synapt HDMS, a hybrid quadrupole-IMS-orthogonal acceleration time-of-flight mass spectrometer (oa-TOF) [ ] (Waters UK Ltd, Manchester, UK) using a Harvard syringe pump (model 22; Harvard Apparatus, Holliston, MA) with a flow rate of 10 μL min−1 .

    Techniques: Mass Spectrometry, Mutagenesis

    ESI-IMS-MS Driftscope plots showing drift time (x axis) versus m/z (y axis) for wild-type β 2 m analyzed at ( a ) pH 6.23, ( b ) pH 4.28, ( c ) pH 3.54, and ( d ) pH 2.60. The number of conformeric species observed for each individual charge state can be seen. Insets at the right hand side of each plot: the summed, full scan m/z spectra of wild-type β 2 m for each data acquisition showing the charge state ions detected.

    Journal: Journal of the American Society for Mass Spectrometry

    Article Title: Monitoring Copopulated Conformational States During Protein Folding Events Using Electrospray Ionization-Ion Mobility Spectrometry-Mass Spectrometry

    doi: 10.1016/j.jasms.2007.09.017

    Figure Lengend Snippet: ESI-IMS-MS Driftscope plots showing drift time (x axis) versus m/z (y axis) for wild-type β 2 m analyzed at ( a ) pH 6.23, ( b ) pH 4.28, ( c ) pH 3.54, and ( d ) pH 2.60. The number of conformeric species observed for each individual charge state can be seen. Insets at the right hand side of each plot: the summed, full scan m/z spectra of wild-type β 2 m for each data acquisition showing the charge state ions detected.

    Article Snippet: ESI-IMS-MS Analyses Samples were infused into the ESI source of a Synapt HDMS, a hybrid quadrupole-IMS-orthogonal acceleration time-of-flight mass spectrometer (oa-TOF) [ ] (Waters UK Ltd, Manchester, UK) using a Harvard syringe pump (model 22; Harvard Apparatus, Holliston, MA) with a flow rate of 10 μL min−1 .

    Techniques: Mass Spectrometry

    ( a ) The summed m/z spectrum from an ESI-IMS-MS data acquisition of cytochrome c analyzed in 50 mM aqueous ammonium acetate solution acidified to pH 3 showing a charge state distribution from +6 to +20 ions consistent with monomeric protein (12,359.4 Da). ( b ) ESI-IMS-MS Driftscope plot showing drift time (x axis) versus m/z (y axis) for the analysis of cytochrome c in 50 mM aqueous ammonium acetate solution acidified to pH 3. ( c ) ESI-IMS-MS drift time versus intensity graphs for the m/z 1237.0 (+10 ions; upper), m/z 1374.4 (+9 ions; middle), and m/z 1546.0 (+8 ions; lower) signals detected during the analysis of cytochrome c in 50 mM aqueous ammonium acetate solution acidified to pH 3.

    Journal: Journal of the American Society for Mass Spectrometry

    Article Title: Monitoring Copopulated Conformational States During Protein Folding Events Using Electrospray Ionization-Ion Mobility Spectrometry-Mass Spectrometry

    doi: 10.1016/j.jasms.2007.09.017

    Figure Lengend Snippet: ( a ) The summed m/z spectrum from an ESI-IMS-MS data acquisition of cytochrome c analyzed in 50 mM aqueous ammonium acetate solution acidified to pH 3 showing a charge state distribution from +6 to +20 ions consistent with monomeric protein (12,359.4 Da). ( b ) ESI-IMS-MS Driftscope plot showing drift time (x axis) versus m/z (y axis) for the analysis of cytochrome c in 50 mM aqueous ammonium acetate solution acidified to pH 3. ( c ) ESI-IMS-MS drift time versus intensity graphs for the m/z 1237.0 (+10 ions; upper), m/z 1374.4 (+9 ions; middle), and m/z 1546.0 (+8 ions; lower) signals detected during the analysis of cytochrome c in 50 mM aqueous ammonium acetate solution acidified to pH 3.

    Article Snippet: ESI-IMS-MS Analyses Samples were infused into the ESI source of a Synapt HDMS, a hybrid quadrupole-IMS-orthogonal acceleration time-of-flight mass spectrometer (oa-TOF) [ ] (Waters UK Ltd, Manchester, UK) using a Harvard syringe pump (model 22; Harvard Apparatus, Holliston, MA) with a flow rate of 10 μL min−1 .

    Techniques: Mass Spectrometry

    Assessment of factors influencing performance of PCR/ESI-MS.

    Journal: Journal of Clinical Microbiology

    Article Title: Broad-Range PCR Coupled with Electrospray Ionization Time of Flight Mass Spectrometry for Detection of Bacteremia and Fungemia in Patients with Neutropenic Fever

    doi: 10.1128/JCM.01066-16

    Figure Lengend Snippet: Assessment of factors influencing performance of PCR/ESI-MS.

    Article Snippet: Episodes with polymicrobial infection, where PCR/ESI-MS detected only the definite pathogen and not the potential contaminant(s), were categorized as true positive for PCR/ESI-MS compared to BC. summarizes all microorganisms detected by both methods, PCR/ESI-MS only, and BC only.

    Techniques: Polymerase Chain Reaction, Mass Spectrometry

    PCR/ESI-MS and blood culture results by specimen.

    Journal: Journal of Clinical Microbiology

    Article Title: Broad-Range PCR Coupled with Electrospray Ionization Time of Flight Mass Spectrometry for Detection of Bacteremia and Fungemia in Patients with Neutropenic Fever

    doi: 10.1128/JCM.01066-16

    Figure Lengend Snippet: PCR/ESI-MS and blood culture results by specimen.

    Article Snippet: Episodes with polymicrobial infection, where PCR/ESI-MS detected only the definite pathogen and not the potential contaminant(s), were categorized as true positive for PCR/ESI-MS compared to BC. summarizes all microorganisms detected by both methods, PCR/ESI-MS only, and BC only.

    Techniques: Polymerase Chain Reaction, Mass Spectrometry

    Results of blood cultures (BC) and PCR/ESI-MS in the 105 cases of neutropenic fever. Bloodstream infection (BSI) included both definite and probable BSI based on BC and/or PCR/ESI-MS. MO, microorganism; +, positive result; −, negative result;

    Journal: Journal of Clinical Microbiology

    Article Title: Broad-Range PCR Coupled with Electrospray Ionization Time of Flight Mass Spectrometry for Detection of Bacteremia and Fungemia in Patients with Neutropenic Fever

    doi: 10.1128/JCM.01066-16

    Figure Lengend Snippet: Results of blood cultures (BC) and PCR/ESI-MS in the 105 cases of neutropenic fever. Bloodstream infection (BSI) included both definite and probable BSI based on BC and/or PCR/ESI-MS. MO, microorganism; +, positive result; −, negative result;

    Article Snippet: Episodes with polymicrobial infection, where PCR/ESI-MS detected only the definite pathogen and not the potential contaminant(s), were categorized as true positive for PCR/ESI-MS compared to BC. summarizes all microorganisms detected by both methods, PCR/ESI-MS only, and BC only.

    Techniques: Polymerase Chain Reaction, Mass Spectrometry, Infection

    A peptic peptide identified by nano-LC/ESI-MS/MS. (A) Extracted ion chromatogram of a peptic peptide eluted from an LC column at 34.6 min. This peptide was detected at m/z 892.9, 595.9 and 447.3 as doubly, triply and quadruply charged ions, respectively

    Journal: Rapid communications in mass spectrometry : RCM

    Article Title: Conformational changes in Akt1 activation probed by amide hydrogen/deuterium exchange and nano-electrospray ionization mass spectrometry †

    doi: 10.1002/rcm.4085

    Figure Lengend Snippet: A peptic peptide identified by nano-LC/ESI-MS/MS. (A) Extracted ion chromatogram of a peptic peptide eluted from an LC column at 34.6 min. This peptide was detected at m/z 892.9, 595.9 and 447.3 as doubly, triply and quadruply charged ions, respectively

    Article Snippet: Prior to the H/D exchange studies, fragments generated from the pepsin digestion of both active and inactive forms of Akt were identified either by LC/MS/MS using an Agilent ion trap mass spectrometer (XCT) equipped with an Agilent 1100 nanoflow HPLC system or by off-line static nano-ESI-MS/MS analysis using a Q-Star Pulsar Qq-TOF mass spectrometer equipped with a nano-ESI source (ABI, Applied Biosystems Instruments).

    Techniques: Mass Spectrometry

    Peptic peptides identified by static nano-ESI-MS/MS. (A) Reconstructed MS spectrum of the peptic digest of Akt. (B) Identification of the peptic peptide detected at m/z 797 as the triply charged ion by MS/MS.

    Journal: Rapid communications in mass spectrometry : RCM

    Article Title: Conformational changes in Akt1 activation probed by amide hydrogen/deuterium exchange and nano-electrospray ionization mass spectrometry †

    doi: 10.1002/rcm.4085

    Figure Lengend Snippet: Peptic peptides identified by static nano-ESI-MS/MS. (A) Reconstructed MS spectrum of the peptic digest of Akt. (B) Identification of the peptic peptide detected at m/z 797 as the triply charged ion by MS/MS.

    Article Snippet: Prior to the H/D exchange studies, fragments generated from the pepsin digestion of both active and inactive forms of Akt were identified either by LC/MS/MS using an Agilent ion trap mass spectrometer (XCT) equipped with an Agilent 1100 nanoflow HPLC system or by off-line static nano-ESI-MS/MS analysis using a Q-Star Pulsar Qq-TOF mass spectrometer equipped with a nano-ESI source (ABI, Applied Biosystems Instruments).

    Techniques: Mass Spectrometry

    Ultra-performance liquid chromatography-electrospray ionization-quadrupole time-of-flight-mass spectrometry (UPLC-ESI-Q-TOF-MSE) spectra of metabolites in mouse plasma (left) and UPLC-ESI-Q-TOF-MSE spectra of metabolites in microorganisms (right) from the same sample and fragmentation sites in the high energy spectrum. ( A ) Monohydroxylation metabolite, ( B ) dihydroxylation metabolite, ( C ) deoxyartemisinin (de-ART), ( D ) deoxygenation followed by hydroxylation metabolite, ( E ) dihydroartemisinin (DHA) and deoxygenated DHA, ( F ) hydrogenated DHA, and ( G ) hydrogenation followed by deoxidization of DHA. A blue box behind the low-energy fragment ions shows in-source fragment ions and a green box indicates adduct clusters.

    Journal: Molecules

    Article Title: A Microbial Transformation Model for Simulating Mammal Metabolism of Artemisinin

    doi: 10.3390/molecules24020315

    Figure Lengend Snippet: Ultra-performance liquid chromatography-electrospray ionization-quadrupole time-of-flight-mass spectrometry (UPLC-ESI-Q-TOF-MSE) spectra of metabolites in mouse plasma (left) and UPLC-ESI-Q-TOF-MSE spectra of metabolites in microorganisms (right) from the same sample and fragmentation sites in the high energy spectrum. ( A ) Monohydroxylation metabolite, ( B ) dihydroxylation metabolite, ( C ) deoxyartemisinin (de-ART), ( D ) deoxygenation followed by hydroxylation metabolite, ( E ) dihydroartemisinin (DHA) and deoxygenated DHA, ( F ) hydrogenated DHA, and ( G ) hydrogenation followed by deoxidization of DHA. A blue box behind the low-energy fragment ions shows in-source fragment ions and a green box indicates adduct clusters.

    Article Snippet: Instruments and LC–MS/MS Conditions The UPLC-ESI-Q-TOF-MSE system consisted of a Waters ACQUITY I-class UPLC and Xevo G2-XS Q-TOF Mass Spectrometer (Waters, Manchester, UK), equipped with an electrospray ionization (ESI) source (Waters, Manchester, UK).

    Techniques: Liquid Chromatography, Mass Spectrometry

    Electrospray ionization-tandem mass spectrum of moanachelin gly-D (C14:0).

    Journal: Journal of biological inorganic chemistry : JBIC : a publication of the Society of Biological Inorganic Chemistry

    Article Title: Amino acid variability in the peptide composition of a suite of amphiphilic peptide siderophores from an open ocean Vibrio species

    doi: 10.1007/s00775-013-0995-3

    Figure Lengend Snippet: Electrospray ionization-tandem mass spectrum of moanachelin gly-D (C14:0).

    Article Snippet: The masses of the siderophores and the siderophore fragments were determined by electrospray ionization mass spectrometry (ESI-MS) and tandem mass spectrometry on a Micromass Q-TOF2 (Waters Corp.).

    Techniques:

    Electrospray ionization-tandem mass spectrum of moanachelin ala-D (C14:0).

    Journal: Journal of biological inorganic chemistry : JBIC : a publication of the Society of Biological Inorganic Chemistry

    Article Title: Amino acid variability in the peptide composition of a suite of amphiphilic peptide siderophores from an open ocean Vibrio species

    doi: 10.1007/s00775-013-0995-3

    Figure Lengend Snippet: Electrospray ionization-tandem mass spectrum of moanachelin ala-D (C14:0).

    Article Snippet: The masses of the siderophores and the siderophore fragments were determined by electrospray ionization mass spectrometry (ESI-MS) and tandem mass spectrometry on a Micromass Q-TOF2 (Waters Corp.).

    Techniques:

    Purification and identification of rLatroeggtoxin-V. ( A ) Chromatogram of RP-HPLC purification of rLatroeggtoxin-V. ( B ) Molecular weight determination of rLatroeggtoxin-V by electrospray ionization mass spectrometry. The m / z value and the number of charges for each rLatroeggtoxin-V ion peak were labeled.

    Journal: Toxins

    Article Title: Anti-Breast Cancer Activity of Latroeggtoxin-V Mined from the Transcriptome of Spider Latrodectus tredecimguttatus Eggs

    doi: 10.3390/toxins10110451

    Figure Lengend Snippet: Purification and identification of rLatroeggtoxin-V. ( A ) Chromatogram of RP-HPLC purification of rLatroeggtoxin-V. ( B ) Molecular weight determination of rLatroeggtoxin-V by electrospray ionization mass spectrometry. The m / z value and the number of charges for each rLatroeggtoxin-V ion peak were labeled.

    Article Snippet: The molecular weight of the components in each elution peak was determined by electrospray ionization mass spectrometry (Waters ACQUITY UPLC/Xevo G2 QTOF, Waters, Milford, MA, USA) and thus the peak containing recombinant Latroeggtoxin-V (rLatroeggtoxin-V) was selected and lyophilized.

    Techniques: Purification, High Performance Liquid Chromatography, Molecular Weight, Mass Spectrometry, Labeling

    Identification of CAM-W produced by recombinant B. subtilis WB 700. ( A ) Analysis of tricine-SDS-PAGE (a) cropped from Supplementary Figure 1 and western blots (b and c) cropped from Supplementary Figures 2 and 3 of the total extracellular proteins from B. subtilis WB700 harboring pDM031 induced without maltose (lane 1) or with maltose (lane 2). These gels were run under the same experimental conditions. The EDDIE and CAM-W bands are indicated by (←) and (← ← ). The bands present in (a) lane 2 were confirmed by western blotting, as shown in (b) and (c). The marker lane contained a broad range protein marker (#P7702, New England Biolabs, USA). ( B ) RP-HPLC analysis of purified CAM-W. ( C ) Electrospray ionization mass spectrometry analysis of purified recombinant CAM-W.

    Journal: Scientific Reports

    Article Title: Efficient biosynthesis of a Cecropin A-melittin mutant in Bacillus subtilis WB700

    doi: 10.1038/srep40587

    Figure Lengend Snippet: Identification of CAM-W produced by recombinant B. subtilis WB 700. ( A ) Analysis of tricine-SDS-PAGE (a) cropped from Supplementary Figure 1 and western blots (b and c) cropped from Supplementary Figures 2 and 3 of the total extracellular proteins from B. subtilis WB700 harboring pDM031 induced without maltose (lane 1) or with maltose (lane 2). These gels were run under the same experimental conditions. The EDDIE and CAM-W bands are indicated by (←) and (← ← ). The bands present in (a) lane 2 were confirmed by western blotting, as shown in (b) and (c). The marker lane contained a broad range protein marker (#P7702, New England Biolabs, USA). ( B ) RP-HPLC analysis of purified CAM-W. ( C ) Electrospray ionization mass spectrometry analysis of purified recombinant CAM-W.

    Article Snippet: The molecular weight of the purified CAM-W was measured using electrospray ionization mass spectrometry (Agilent, USA).

    Techniques: Chick Chorioallantoic Membrane Assay, Produced, Recombinant, Western Blot, SDS Page, Marker, High Performance Liquid Chromatography, Purification, Mass Spectrometry