Q exactive plus mass spectrometer

Manufactured by Waters Corporation

Sourced in United States

The Q-Exactive Plus mass spectrometer is a high-resolution, accurate-mass (HRAM) instrument designed for a wide range of analytical applications. It features a quadrupole-Orbitrap mass analyzer that provides high-resolution, accurate-mass measurements. The Q-Exactive Plus is capable of performing full-scan MS and targeted MS/MS experiments with consistent high mass accuracy.

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Lab products found in correlation

Aquity uplc system, by Waters Corporation (1 mentions) Biopharma finder, by Thermo Fisher Scientific (1 mentions) C4 column, by Waters Corporation (1 mentions) Trypsin gold ms grade, by Promega (1 mentions) Nanoacquity uplc column, by Waters Corporation (1 mentions)

Close spelling variants of this product

Q Exactive (14 citations) Q Exactive Plus (6 citations) Exactive mass spectrometer (2 citations)

5 protocols using q exactive plus mass spectrometer

Protein Mass Determination via LC-MS

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Protein masses were determined using LC-MS with an Aquity UPLC system (Waters) linked to a Q-ExactivePlus mass spectrometer. A BioResolve RP mAB Polyphenyl column 2.1 × 50 mm was developed with a gradient comprising 0.1% formic acid (A) and 0.5% formic acid in acetonitrile (B) with a flow rate of 0.4 ml/min and initial conditions 5% B; 0.5 min: 10% B; 9 min: 60% B; 10 min 80% B; 11 min 5% B. The mass spectrometer was operated in positive mode with resolution 17,500 and m/z range 400 to 4000. Automatic gain control and maximum injection time were set to 3 × 10⁶ and 200 msec, respectively. Raw data were processed with BioPharmaFinder (Thermo) using the Respect option with standard settings suitable for proteins of MyoB molecular weight.

Pires I., Hung Y.F., Bergmann U., Molloy J.E, & Kursula I. (2022). Analysis of Plasmodium falciparum myosin B ATPase activity and structure in complex with the calmodulin-like domain of its light chain MLC-B. The Journal of Biological Chemistry, 298(12), 102634.

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Molecular Weight Analysis of Purified Proteins

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Molecular weight analysis of the purified proteins was performed by Electrospray ionization mass spectrometry in combination with liquid chromatography (LC–ESI–MS) using a Q-Exactive Plus Mass Spectrometer (Waters, MA, USA). 0.5 mg/ mL of the purified protein of interest was first subjected to denaturation using 5 M guanidine hydrochloride. Post-denaturation, NEM-trapped samples were treated with 10 mM NEM, incubated at room temperature for 10 min and the alkylation reaction was then quenched with 0.5% trifluoroacetic acid (TFA) prior to analysis. For the non-NEM trapped samples, 0.5% TFA was directly added to the denatured protein samples prior to analysis. The experimental molecular weight (M_exp) of the protein was obtained by mass spectrometry analysis and the theoretical molecular weight (M_theor) was calculated using ExPasy ProtParam tool^{58 (link)} based on the amino acid sequence of the proteins.

Tungekar A.A, & Ruddock L.W. (2023). Design of an alternate antibody fragment format that can be produced in the cytoplasm of Escherichia coli. Scientific Reports, 13, 14188.

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Large-Scale Protein Characterization by LC-MS

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A Thermo Q-Exactive Plus mass spectrometer coupled with C4 column (Waters; 2.1 mm × 50 mm; Part No. 186004495) in high mass range mode was used for LC-MS analysis. The column temperature was maintained at 60 °C with flow rate at 0.25 mL/min using Buffer A (0.1% FA) and Buffer B (0.1% FA in ACN). The 20 min run was performed through gradient 15 to 60% ACN in 9 min, 2 min increase to 90% ACN followed by washout for 2 min at 90% ACN, and re-equilibration at 15% ACN for 5 min. Spray voltage was set to 3.5 kV, S-lens RF level at 100, and heated capillary at 253 °C. In source CID was 10 eV. Full scan resolution was set to 17.5 K at m/z 200 with 10 average microscans. Target value was set at 3 × 10⁶ with a maximum injection time of 200 ms. Mass range was set to 500–5000 m/z. All data was acquired in profile mode using positive polarity. LC-MS results were deconvoluted using Intact Protein Analysis in BioPharma Finder 3.2 software. Data were manually confirmed.

Hsiao W.C., Niu G.H., Lo C.F., Wang J.Y., Chi Y.H., Huang W.C., Tung C.W., Sung P.J., Tsou L.K, & Zhang M.M. (2023). Marine diterpenoid targets STING palmitoylation in mammalian cells. Communications Chemistry, 6, 153.

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Protein Mass Spectrometry Analysis

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Electrospray ionization mass spectrometry combined with liquid chromatography (LC–ESI–MS) was employed to measure the molecular weights of purified proteins using a Q Exactive Plus Mass Spectrometer (Waters). Protein samples (0.5 mg/mL) were first subjected to denaturation using 5 M guanidine hydrochloride. Post-denaturation, non-NEM trapped samples were treated with 0.5% trifluoroacetic acid (TFA) prior to analysis. NEM-trapped samples were incubated with 10 mM NEM for 10 min at room temperature and the reaction was quenched with 0.5% TFA prior to analysis. The theoretical molecular weight (M_theor) was calculated using the amino acid sequence of the proteins using the ExPasy ProtParam tool^{45 (link)}. The experimental molecular weight (M_exp) was obtained from mass spectrometry analysis.

Tungekar A.A., Recacha R, & Ruddock L.W. (2023). Production of neutralizing antibody fragment variants in the cytoplasm of E. coli for rapid screening: SARS-CoV-2 a case study. Scientific Reports, 13, 4408.

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Proteomic Analysis of PAM and V-ATPase Complexes

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Subcellular fractions from PAM-1 cells were separated by BN-PAGE/SDS-PAGE and visualized using the SilverSNAP Kit (Pierce, Rockford, IL). Vertical strips of gels spanning the region known to contain PAM and V-ATPase complexes were excised using a sterile scalpel, placed into a sterile Eppendorf microfuge tube and frozen. Gel fragments were washed 4 times: first with 500 μL 60% acetonitrile containing 0.1%TFA; then with 5% acetic acid; then with 250 μL 50% H₂O/50% acetonitrile; then with 250 μL 50% CH₃CN/50 mM NH₄HCO₃. Gel fragments were washed with 250 μL 50% CH₃CN/10 mM NH₄HCO₃ prior to drying in a Speed Vac. 1 μg of trypsin (Promega Trypsin Gold MS grade) freshly diluted into 10 mM NH₄HCO₃ was added to the dried gels pieces and incubated at 37°C for 18 hours (20). Briefly, peptides were separated on a nanoAcquity™ UPLC™ column (Waters) coupled to a Q-Exactive Plus mass spectrometer. High resolution tandem LC MS/MS data were collected by Higher-Energy Collisional Dissociation (HCD) with a 1.4 Da window followed by normalized collision energy of 32%. Resulting LC MS/MS data were analyzed and processed through Proteome Discoverer (linked to MASCOT and a Sequest Search engine).

Rao V.K., Zavala G., Roy A.D., Mains R.E, & Eipper B.A. (2018). A pH-sensitive luminal His-cluster promotes interaction of PAM with V-ATPase along the secretory and endocytic pathways of peptidergic cells. Journal of cellular physiology, 234(6), 8683-8697.

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