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Tandem Mass Spectrometry
Tandem Mass Spectrometry
Tandem Mass Spectrometry is a powerful analytical technique that combines two or more stages of mass spectrometry to provide detailed information about the structure and composition of complex molecules.
This method allows for the separation and identification of individual components within a sample, enabling researchers to gain deeper insights into a wide range of analytes, from small molecules to large biomolecules.
Tandem Mass Spectrometry offers unparalleled sensitivity, selectivity, and specifity, making it an indispensable tool in fields such as proteomics, metabolomics, and pharmacokinetics.
With its ability to provide high-resolution data and facilitate the discovery of novel compounds, Tandem Mass Spectrometry continues to be a cornerstone of modern analytical chemistry and bioscience reserach.
This method allows for the separation and identification of individual components within a sample, enabling researchers to gain deeper insights into a wide range of analytes, from small molecules to large biomolecules.
Tandem Mass Spectrometry offers unparalleled sensitivity, selectivity, and specifity, making it an indispensable tool in fields such as proteomics, metabolomics, and pharmacokinetics.
With its ability to provide high-resolution data and facilitate the discovery of novel compounds, Tandem Mass Spectrometry continues to be a cornerstone of modern analytical chemistry and bioscience reserach.
Most cited protocols related to «Tandem Mass Spectrometry»
Peptides
Proteins
SDS-PAGE
Staphylococcal Protein A
Tandem Mass Spectrometry
Tissue Extracts
Tissues
Trypsin
An Escherichia coli K12 strain was grown in standard LB medium, harvested, washed in PBS, and lysed in BugBuster (Novagen Merck Chemicals, Schwalbach, Germany) according to the manufacturer's protocol. HeLa S3 cells were grown in standard RPMI 1640 medium supplemented with glutamine, antibiotics, and 10% FBS. After being washed with PBS, cells were lysed in cold modified RIPA buffer (50 mm Tris-HCl, pH 7.5, 1 mm EDTA, 150 mm NaCl, 1% N-octylglycoside, 0.1% sodium deoxycholate, complete protease inhibitor mixture (Roche)) and incubated for 15 min on ice. Lysates were cleared by centrifugation, and after precipitation with chloroform/methanol, proteins were resuspended in 6 m urea, 2 m thiourea, 10 mm HEPES, pH 8.0. Prior to in-solution digestion, 60-μg protein samples from HeLa S3 lysates were spiked with either 10 μg or 30 μg of E. coli K12 lysates based on protein amount (Bradford assay). Both batches were reduced with dithiothreitol and alkylated with iodoacetamide. Proteins were digested with LysC (Wako Chemicals, GmbH, Neuss, Germany) for 4 h and then trypsin digested overnight (Promega, GmbH, Mannheim, Germany). Digestion was stopped by the addition of 2% trifluroacetic acid. Peptides were separated by isoelectric focusing into 24 fractions on a 3100 OFFGEL Fractionator (Agilent, GmbH, Böblingen, Germany) as described in Ref. 45 (link). Each fraction was purified with C18 StageTips (46 (link)) and analyzed via liquid chromatography combined with electrospray tandem mass spectrometry on an LTQ Orbitrap (Thermo Fisher) with lock mass calibration (47 (link)). All raw files were searched against the human and E. coli complete proteome sequences obtained from UniProt (version from January 2013) and a set of commonly observed contaminants. MS/MS spectra were filtered to contain at most eight peaks per 100 mass unit intervals. The initial MS mass tolerance was 20 ppm, and MS/MS fragment ions could deviate by up to 0.5 Da (48 (link)). For quantification, intensities can be determined alternatively as the full peak volume or as the intensity maximum over the retention time profile, and the latter method was used here as the default. Intensities of different isotopic peaks in an isotope pattern are always summed up for further analysis. MaxQuant offers a choice of the degree of uniqueness required in order for peptides to be included for quantification: “all peptides,” “only unique peptides,” and “unique plus razor peptides” (42 (link)). Here we chose the latter, because it is a good compromise between the two competing interests of using only peptides that undoubtedly belong to a protein and using as many peptide signals as possible. The distribution of peptide ions over fractions and samples is shown in supplemental Fig. S1 .
Acids
Antibiotics, Antitubercular
Biological Assay
Buffers
Cells
Centrifugation
Chloroform
Cold Temperature
Deoxycholic Acid, Monosodium Salt
Digestion
Dithiothreitol
Edetic Acid
Escherichia coli
Escherichia coli K12
Glutamine
HeLa Cells
HEPES
Homo sapiens
Immune Tolerance
Iodoacetamide
Ions
Isotopes
Liquid Chromatography
Methanol
Peptides
Promega
Protease Inhibitors
Proteins
Proteome
Radioimmunoprecipitation Assay
Retention (Psychology)
Sodium Chloride
Staphylococcal Protein A
Tandem Mass Spectrometry
Thiourea
Tromethamine
Trypsin
Urea
Cells
Crystallins
Dehydrogenase, Alcohol
Dimyristoylphosphatidylcholine
Glycerylphosphorylcholine
GPER protein, human
Heat-Shock Proteins, Small
Lipids
Lipoproteins
Phosphorylcholine
plasma protein Z
Protein Subunits
Range of Motion, Articular
Tandem Mass Spectrometry
Tissue, Membrane
Water Channel
cDNA Library
chemical composition
Gold
Tandem Mass Spectrometry
A key step in placing statistically significant findings from chemometric analyses (as opposed to quantitative metabolomic analyses) into a biological context is to identify significantly altered compounds represented by certain spectral bins or certain clusters of spectral peaks. Once a user has identified lists of MS or NMR peaks that exhibit statistically significant changes, they may use one of several spectral comparison routines and spectral libraries to attempt to identify the compound(s) based on either lists of MS peaks (from MS or MS/MS data), GC-–MS peaks (from EI mass values and retention indices) or NMR peaks (from 1H, 13C or heteronuclear NMR spectra). These compound identification routines and spectral reference libraries were originally developed for the HMDB and for MetaboMiner (11 (link)). While not as comprehensive as some commercial libraries or commercial software, these freely available tools have been shown to be quite powerful in identifying many common compounds. Once compound information becomes available (via quantitative routes or via MetaboAnalyst's metabolite ID software), more insight can be obtained by which metabolic pathways are involved. Pathway mapping has been implemented in MetaboAnalyst using more than 70 pathway diagrams and metabolite libraries derived from the HMDB. Users simply type the names (or synonyms) of the metabolites identified and MetaboAnalyst provides the list of pathways in which these metabolites are found, along with hyperlinks to their pathway images. All results are linked to the HMDB where users can obtain more detailed information for each metabolite or pathway.
Biopharmaceuticals
Cortodoxone
Gas Chromatography-Mass Spectrometry
Nuclear Magnetic Resonance, Heteronuclear
Retention (Psychology)
Tandem Mass Spectrometry
Most recents protocols related to «Tandem Mass Spectrometry»
Example 8
Characterization of Absorption, Distribution, Metabolism, and Excretion of Oral [14C]Vorasidenib with Concomitant Intravenous Microdose Administration of [13C315N3]Vorasidenib in Humans
Metabolite profiling and identification of vorasidenib (AG-881) was performed in plasma, urine, and fecal samples collected from five healthy subjects after a single 50-mg (100 μCi) oral dose of [14C]AG-881 and concomitant intravenous microdose of [13C3 15N3]AG-881.
Plasma samples collected at selected time points from 0 through 336 hour postdose were pooled across subjects to generate 0—to 72 and 96-336-hour area under the concentration-time curve (AUC)-representative samples. Urine and feces samples were pooled by subject to generate individual urine and fecal pools. Plasma, urine, and feces samples were extracted, as appropriate, the extracts were profiled using high performance liquid chromatography (HPLC), and metabolites were identified by liquid chromatography-mass spectrometry (LC-MS and/or LC-MS/MS) analysis and by comparison of retention time with reference standards, when available.
Due to low radioactivity in samples, plasma metabolite profiling was performed by using accelerator mass spectrometry (AMS). In plasma, AG-881 was accounted for 66.24 and 29.47% of the total radioactivity in the pooled AUC0-72 h and AUC96-336 h plasma, respectively. The most abundant radioactive peak (P7; M458) represented 0.10 and 43.92% of total radioactivity for pooled AUC0-72 and AUC96-336 h plasma, respectively. All other radioactive peaks accounted for less than 6% of the total plasma radioactivity and were not identified.
The majority of the radioactivity recovered in feces was associated with unchanged AG-881 (55.5% of the dose), while no AG-881 was detected in urine. In comparison, metabolites in excreta accounted for approximately 18% of dose in feces and for approximately 4% of dose in urine. M515, M460-1, M499, M516/M460-2, and M472/M476 were the most abundant metabolites in feces, and each accounted for approximately 2 to 5% of the radioactive dose, while M266 was the most abundant metabolite identified in urine and accounted for a mean of 2.54% of the dose. The remaining radioactive components in urine and feces each accounted for <1% of the dose.
Overall, the data presented indicate [14C]AG-881 underwent moderate metabolism after a single oral dose of 50-mg (100 μCi) and was eliminated in humans via a combination of metabolism and excretion of unchanged parent. AG-881 metabolism involved the oxidation and conjugation with glutathione (GSH) by displacement of the chlorine at the chloropyridine moiety. Subsequent biotransformation of GSH intermediates resulted in elimination of both glutamic acid and glycine to form the cysteinyl conjugates (M515 and M499). The cysteinyl conjugates were further converted by a series of biotransformation reactions such as oxidation, S-dealkylation, S-methylation, S-oxidation, S-acetylation and N-dealkylation resulting in the formation multiple metabolites.
A summary of the metabolites observed is included in Table 2
Acetylation
AG 30
Biotransformation
Chlorine
Dealkylation
Deamination
Elements, Radioactive
Feces
Glutamic Acid
Glutathione
Glycine
Healthy Volunteers
High-Performance Liquid Chromatographies
Homo sapiens
Hydrolysis
Intravenous Infusion
Ions
Liquid Chromatography
Mass Spectrometry
Metabolism
Methylation
Parent
Plasma
Radioactivity
Retention (Psychology)
Tandem Mass Spectrometry
Urinalysis
Urine
vorasidenib
Example 2
N-(2-chloro-4-(trifluoromethyl)phenyl)-2-(5-ethyl-2-morpholino-7-oxo-6-(piperazin-1-yl)-[1,2,4]triazolo[1,5-a]pyrimidin-4(7H)-yl)acetamide (Intermediate B) (200 mg, 352 μmol) was suspended in DMF (5 mL). Perfluorophenyl 3-hydroxypicolinate (Intermediate CT) (215 mg, 703 μmol) and Et3N (97.0 μL, 703 μmol) were added and the RM was stirred at 70° C. for 3 hours. The RM was concentrated under reduced pressure. The crude product was first purified by column chromatography (Silica gel column: Silica 12 g, eluent DCM:MeOH 100:0 to 90:10). Then a second purification by reverse phase preparative HPLC (RP-HPLC acidic 9: 40 to 50% B in 2 min, 50 to 55% B in 10 min) afforded the title compound.
LC-MS: Rt=0.98 min; MS m/z [M+H]+ 690.6/692.6, m/z [M−H]− 688.4/690.3; UPLC-MS 1
LC-MS: Rt=4.84 min; MS m/z [M+H]+ 690.2/692.2 m/z [M−H]− 688.3/690.3; UPLC-MS 2
1H NMR (400 MHz, DMSO-d6) δ 10.37 (s, br, 1H), 10.34 (s, br, 1H), 8.05 (m, 2H), 7.96 (d, J=2.1 Hz, 1H), 7.72 (dd, J=2.1 Hz, 8.7 Hz, 1H), 7.28 (m, 2H), 5.21 (s, 2H), 4.53 (m, 1H), 3.66 (m, 4H), 3.46 (m, 3H), 3.38 (m, 4H), 3.20 (m, 1H), 2.92 (m, 3H), 2.76 (m, 1H), 2.58 (m, 1H), 1.16 (t, J=7.5 Hz, 3H)
Example 24
To the stirred solution of N-(2-chloro-6-(trifluoromethyl)pyridin-3-yl)-2-(5-ethyl-2-(4-methoxycyclohex-1-en-1-yl)-7-oxo-6-(piperazin-1-yl)-[1,2,4]triazolo[1,5-a]pyrimidin-4(7H)-yl)acetamide (Intermediate Y) (300 mg, 504 μmol), 4-chloro-3-hydroxypicolinic acid (140 mg, 807 μmol), HOBt (136 mg, 1.01 mmol) and EDC.HCl (193 mg, 1.01 mmol) in DCM (20 mL) was added pyridine (122 μL, 1.51 mmol) at 0° C. The RM was stirred at RT for 16 hours. The RM was quenched with NaHCO3 and extracted with DCM. The organic layer was dried over Na2SO4 and concentrated under reduced pressure. The crude product was purified by column chromatography (Silica gel column: Silica 4 g, eluent DCM:MeOH 100:0 to 98:2). The residue was purified by preparative chiral HPLC (instrument: Agilent 1200 series, with single quad mass spectrometer; column: LUX CELLULOSE-4, 250 mm×21.1 mm, 5.0 μm; eluent: A=hexane, B=0.1% HCOOH in EtOH; flow rate: 15 mL/min; detection: 210 nm; injection volume: 0.9 mL; gradient: isocratic: 50(A):50(B)).
Example 24a: The product containing fractions were concentrated at 40° C. and washed with n-pentane (5×10 mL), decanted and dried to give the title compound as an off-white solid—first eluting stereoisomer.
Chiral HPLC (C-HPLC 2): Rt=10.764 min
LC-MS: Rt=1.08 min; MS m/z [M+H]+ 750.5/752.5, m/z [M−H]− 748.4/750.4; UPLC-MS 1
LC-MS: Rt=5.29 min; MS m/z [M+H]+ 750.2/752.2, m/z [M−H]− 748.2/750.2; UPLC-MS 2
1H NMR (400 MHz, DMSO-d6) δ 10.68 (s, br, 2H), 8.56 (d, J=8.1 Hz, 1H), 7.98 (d, J=5.6 Hz, 1H), 7.94 (d, J=8.1 Hz, 1H), 7.50 (d, J=5.1 Hz, 1H), 6.72 (m, 1H), 5.34 (s, 2H), 4.53 (m, 1H), 3.52 (m, 4H), 3.28 (m, 4H), 2.98 (m, 3H), 2.80 (m, 1H), 2.63 (m, 1H), 2.55 (m, 1H), 2.46 (m, 1H), 2.16 (m, 2H), 1.95 (m, 1H), 1.68 (m, 1H), 1.17 (t, J=7.3 Hz, 3H)
Example 24b: The product containing fractions were concentrated at 40° C. and washed with n-pentane (5×10 mL), decanted and dried to give the title compound as an off-white solid—second eluting stereoisomer.
Chiral HPLC (C-HPLC 2): Rt=18.800 min
LC-MS: Rt=1.08 min; MS m/z [M+H]+ 750.1/752.1, m/z [M−H]− 748.2/750.2; UPLC-MS 1
LC-MS: Rt=5.30 min; MS m/z [M+H]+ 750.1/752.1, m/z [M−H]− 748.2/750.2; UPLC-MS 2
1H NMR (400 MHz, DMSO-d6) δ 10.83 (s, br, 1H), 10.55 (s, br, 1H), 8.56 (d, J=8.2 Hz, 1H), 8.06 (d, J=5.3 Hz, 1H), 7.92 (d, J=8.2 Hz, 1H), 7.55 (d, J=5.3 Hz, 1H), 6.72 (m, 1H), 5.35 (s, 2H), 4.54 (m, 1H), 3.54 (m, 4H), 3.28 (m, 3H), 3.25 (m, 1H), 2.99 (m, 3H), 2.81 (m, 1H), 2.62 (m, 1H), 2.41 (m, 2H), 2.16 (m, 2H), 1.96 (m, 1H), 1.66 (m, 1H), 1.18 (t, J=7.3 Hz, 3H)
Example 25
N-(2-chloro-6-(trifluoromethyl)pyridin-3-yl)-2-(5-ethyl-2-(4-methoxycyclohex-1-en-1-yl)-7-oxo-6-(piperazin-1-yl)-[1,2,4]triazolo[1,5-a]pyrimidin-4(7H)-yl)acetamide.HCl (Intermediate Y) (120 mg, 190 μmol) and DIPEA (166 μL, 950 μmol) were dissolved in DCM (5 mL) and then 3-hydroxypicolinoyl chloride (Intermediate CV) (59.9 mg, 380 μmol) was added at 0° C. and stirred for 2 hours. 3-hydroxypicolinoyl chloride (Intermediate CV) (59.9 mg, 380 μmol) was added again and the reaction was continued under stirring for 12 hours. The RM was diluted with DCM and washed with water and aq NaHCO3 (2×20 mL), washed with water and brine, dried over Na2SO4, filtered and concentrated. The crude product was combined with another experiment and purified by column chromatography (Silica gel column: Silica 4 g, eluent DCM:MeOH 100:0 to 99:1) then further purified by reverse phase preparative HPLC (RP-HPLC acidic 10: 40 to 50% B in 2 min, 50 to 60% B in 8 min) to give the title compound as an off-white solid.
The racemate was purified by preparative chiral HPLC (instrument: Agilent 1200 series, with single quad mass spectrometer; column: CELLULOSE-4, 250 mm×21.2 mm; eluent: A=hexane, B=0.1% HCOOH in MeOH:EtOH 1:1; flow rate: 20 mL/min; detection: 210 nm; injection volume: 0.9 mL; gradient: isocratic 60(A):40(B)).
Example 25a: First eluting stereoisomer, off-white solid.
Chiral HPLC (C-HPLC 1): Rt=10.070 min
LC-MS: Rt=0.98 min; MS m/z [M+H]+ 716.5/718.6, m/z [M−H]− 714.3/716.3; UPLC-MS 1
LC-MS: Rt=4.76 min; MS m/z [M+H]+ 716.2/718.2, m/z [M−H]− 714.2/716.2; UPLC-MS 2
1H NMR (400 MHz, DMSO-d6) δ 10.46 (s, br, 2H), 8.56 (d, J=8.5 Hz, 1H), 8.05 (m, 1H), 7.90 (d, J=8.4 Hz, 1H), 7.28 (m, 2H), 6.72 (m, 1H), 5.30 (s, 2H), 4.54 (m, 1H), 3.47 (m, 4H), 3.27 (s, 3H), 3.21 (m, 1H), 2.96 (m, 3H), 2.79 (m, 1H), 2.59 (m, 3H), 2.43 (m, 1H), 2.14 (m, 1H), 1.95 (m, 1H), 1.67 (m, 1H), 1.17 (t, J=7.2 Hz, 3H)
Example 25b: Second eluting stereoisomer, off-white solid.
Chiral HPLC (C-HPLC 1): Rt=16.023 min
LC-MS: Rt=0.96 min; MS m/z [M+H]+ 716.3/718.3, m/z [M−H]− 714.3/716.3; UPLC-MS 1
LC-MS: Rt=4.77 min; MS m/z [M+H]+ 716.2/718.2, m/z [M−H]− 714.2/716.2; UPLC-MS 2
1H NMR (400 MHz, DMSO-d6) δ 10.39 (s, br, 2H), 8.56 (d, J=8.0 Hz, 1H), 8.06 (m, 1H), 7.93 (d, J=8.1 Hz, 1H), 7.28 (m, 2H), 6.72 (m, 1H), 5.32 (s, 2H), 4.54 (m, 1H), 3.46 (m, 4H), 3.27 (s, 3H), 3.20 (m, 1H), 2.96 (m, 3H), 2.79 (m, 1H), 2.59 (m, 3H), 2.41 (m, 1H), 2.14 (m, 1H), 1.95 (m, 1H), 1.68 (m, 1H), 1.17 (t, J=7.1 Hz, 3H)
1-hydroxybenzotriazole
1H NMR
acetamide
Acids
Bicarbonate, Sodium
Bicyclo Compounds
brine
Cellulose
Chlorides
Chromatography
DIPEA
Ethanol
H 718
Hexanes
High-Performance Liquid Chromatographies
Morpholinos
pentane
Piperazine
Pressure
pyridine
Silica Gel
Silicon Dioxide
Stereoisomers
Sulfoxide, Dimethyl
Tandem Mass Spectrometry
Example 18
To the stirred solution of 3-hydroxypicolinic acid (166 mg, 1.19 mmol), EDC.HCl (228 mg, 1.19 mmol), HOBt (161 mg, 1.19 mmol) in DMF (3 mL) was added N-(2-chloro-6-(trifluoromethyl)pyridin-3-yl)-2-(5-ethyl-7-oxo-6-(piperazin-1-yl)-2-(pyrrolidin-1-yl)-[1,2,4]triazolo[1,5-a]pyrimidin-4(7H)-yl)acetamide (Intermediate Q) (330 mg, 596 μmol) and DIPEA (624 μL, 3.57 mmol) and the RM was at RT for 16 hours. The RM was concentrated under reduced pressure and water was added. The resultant brown solid was filtered off and dried under vacuum. The crude product was purified by reverse phase preparative HPLC (RP-HPLC acidic 4: 35 to 40% B in 2 min, 40 to 45% B in 10 min) to give the title compound.
LC-MS: Rt=0.94 min; MS m/z [M+H]+ 675.3/677.3, m/z [M−H]− 673.3/675.3; UPLC-MS 1
LC-MS: Rt=4.68 min; MS m/z [M+H]+ 675.2/677.2, m/z [M−H]− 673.2/675.2; UPLC-MS 2
1H NMR (400 MHz, DMSO-d6) δ 10.54 (s, br, 1H), 10.38 (s, br, 1H), 8.55 (d, J=8.4 Hz, 1H), 8.06 (m, 1H), 7.95 (d, J=8.4 Hz, 1H), 7.28 (m, 2H), 5.25 (s, 2H), 4.53 (m, 1H), 3.46 (m, 3H), 3.35 (m, 4H), 3.19 (m, 1H), 2.91 (m, 3H), 2.75 (m, 1H), 2.57 (m, 1H), 1.89 (m, 4H), 1.15 (t, 3H)
1-hydroxybenzotriazole
1H NMR
acetamide
Acids
DIPEA
High-Performance Liquid Chromatographies
Piperazine
Pressure
Sulfoxide, Dimethyl
Tandem Mass Spectrometry
Vacuum
Example 8
The SFME sample processing can be done in fused silica tubing of smaller diameter which are commonly used as liquid line in liquid chromatography system (e.g., tubing having an inner diameter of 500 μm or less). The extraction can be induced by applying a push and pull force on one side of the tubing. The extract can be either directly analyzed by nanoESI or stored for further operations.
Amitriptyline
BLOOD
Cattle
Liquid Chromatography
Silicon Dioxide
Tandem Mass Spectrometry
Viscosity
Example 10
The objective of this study was to develop an acute model of homocystinuria in nonhuman primates. Male cynomolgus monkeys of approximately 2-5 years of age (average weight of 3.4 kg) were fasted overnight and orally administered a methionine load at 100 or 300 mg/kg, and plasma was collected at 0-, 0.5-, 1-, 2-, 4-, 6-, and 24-hours post-dose for methionine and total homocysteine measurements by LC-MS/MS.
Oral administration of methionine (100 or 300 mg/kg) resulted in a dose-dependent increase in plasma methionine levels, with peak concentration recorded at 30 minutes and 1 hour post dose for 100 mg/kg and 300 mg/kg, respectively (
Administration, Oral
Homocysteine
Homocystinuria
Macaca fascicularis
Males
Methionine
Plasma
Primates
Tandem Mass Spectrometry
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More about "Tandem Mass Spectrometry"
Tandem mass spectrometry (MS/MS or MS2) is a powerful analytical technique that combines multiple stages of mass spectrometry to provide in-depth information about the structure and composition of complex molecules.
This method allows for the separation, identification, and characterization of individual components within a sample, enabling researchers to gain deeper insights into a wide range of analytes, from small molecules to large biomolecules.
Tandem mass spectrometry offers unparalleled sensitivity, selectivity, and specificity, making it an indispensable tool in fields such as proteomics, metabolomics, and pharmacokinetics.
The technique typically involves an initial stage of mass spectrometry to isolate and select precursor ions, followed by one or more subsequent stages of fragmentation and mass analysis to generate detailed structural information.
Q Exactive mass spectrometers, combined with powerful software like Proteome Discoverer and Analyst 1.6.3, are commonly used in tandem mass spectrometry workflows.
These instruments provide high-resolution data and facilitate the discovery of novel compounds, making them essential for modern analytical chemistry and bioscience research.
Trypsin, a commonly used enzyme in proteomics studies, is often employed in tandem mass spectrometry experiments to generate peptide fragments for analysis.
The Mascot search engine is a widely used tool for the identification of proteins from tandem mass spectrometry data.
With its ability to provide detailed information about complex samples, tandem mass spectrometry continues to be a cornerstone of modern analytical techniques.
The EASY-nLC 1000 and Q Exactive Plus systems further enhance the capabilities of this powerful method, enabling researchers to push the boundaries of their investigations and make groundbreaking discoveries.
This method allows for the separation, identification, and characterization of individual components within a sample, enabling researchers to gain deeper insights into a wide range of analytes, from small molecules to large biomolecules.
Tandem mass spectrometry offers unparalleled sensitivity, selectivity, and specificity, making it an indispensable tool in fields such as proteomics, metabolomics, and pharmacokinetics.
The technique typically involves an initial stage of mass spectrometry to isolate and select precursor ions, followed by one or more subsequent stages of fragmentation and mass analysis to generate detailed structural information.
Q Exactive mass spectrometers, combined with powerful software like Proteome Discoverer and Analyst 1.6.3, are commonly used in tandem mass spectrometry workflows.
These instruments provide high-resolution data and facilitate the discovery of novel compounds, making them essential for modern analytical chemistry and bioscience research.
Trypsin, a commonly used enzyme in proteomics studies, is often employed in tandem mass spectrometry experiments to generate peptide fragments for analysis.
The Mascot search engine is a widely used tool for the identification of proteins from tandem mass spectrometry data.
With its ability to provide detailed information about complex samples, tandem mass spectrometry continues to be a cornerstone of modern analytical techniques.
The EASY-nLC 1000 and Q Exactive Plus systems further enhance the capabilities of this powerful method, enabling researchers to push the boundaries of their investigations and make groundbreaking discoveries.