Avance 3 spectrometer

Manufactured by Bruker

Sourced in Germany, United States, Switzerland, Italy, France

The Avance III spectrometer is a nuclear magnetic resonance (NMR) spectrometer developed by Bruker. It is designed to perform high-resolution NMR analysis of chemical samples. The Avance III spectrometer provides advanced hardware and software features to enable precise data acquisition and analysis.

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Close spelling variants of this product

Avance III (981 citations) Avance spectrometer (419 citations) Avance III 500 spectrometer (108 citations) Bruker spectrometers (71 citations) Avance III 400 MHz NMR spectrometer (56 citations) Avance III HD 500 MHz spectrometer (38 citations) Avance III HD 500 NMR spectrometer (20 citations) AVANCE III HD 400 MHz NMR spectrometer (14 citations) Avance III 700 MHz NMR spectrometer (9 citations) Avance III 300 MHz NMR spectrometer (7 citations)

373 protocols using avance 3 spectrometer

Analytical Characterization of Synthetic Compounds

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All commercial
chemicals and solvents were used as obtained from the manufacturer
without further purification. Flash chromatography were run on 200–300
mesh silica gel using a Teledyne CombiFlash instrument. ¹H NMR spectra were recorded on a Bruker AVANCE-III spectrometer at
800 MHz. ¹³C NMR spectra were recorded on a Bruker AVANCE-III
spectrometer at 151 MHz. NMR chemical shifts were reported in δ
(ppm) using residual solvent peaks as standards (CDCl₃–7.26
(H), 77.16 (C); CD₃OD–3.31 (H), 49.00 (C); DMSO-d₆–2.50 (H), 39.52 (C)). Mass spectra
were measured using an LCMS-IT-TOF (Shimadzu) mass spectrometer in
ESI mode. The purity of all final compounds (>95%) were determined
by analytical HPLC (Shim-pack GIST C18 column (250 × 4.6 mm,
particle size 5 μM); 0.05% TFA in H₂O/0.05% TFA in
MeOH gradient eluting system; flow rate = 1.0 mL/min). Preparative
HPLC was conducted using Shimadzu HPLC system (Shim-pack GIST C18
column (250 × 20 mm, particle size 5 μM); H₂O/MeOH gradient eluting system; flow rate = 10.0 mL/min).

Chan H.C., Xu Y., Tan L., Vogel H., Cheng J., Wu D, & Yuan S. (2020). Enhancing the Signaling of GPCRs via Orthosteric Ions. ACS Central Science, 6(2), 274-282.

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Cross-Polarization NMR Spectroscopy of HEA-1 and IBoA-1

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For cross-polarization magic angle spinning solid-state NMR spectroscopy, all samples were packed with magnesium oxide to improve sample balance and spin. Solid-state NMR experiments analyzing HEA-1 samples were conducted using a 16.4 T magnetic field (¹H resonant field of 700.18 MHz) on a Bruker Avance III spectrometer fitted with a ¹H{³¹P, ¹³C} 3.2 mm MAS probe. Solid-state NMR experiments analyzing IBoA-1 samples were conducted using a 11.75 T magnetic field (¹H resonant field of 500.22 MHz) on a Bruker Avance III spectrometer fitted with a 4 mm ¹H/X/Y DSI MAS probe. A magic angle spinning rate of 12.5 or 12 kHz was used for HEA-1 or IBoA-1 samples, respectively. The ¹³C NMR signal was enhanced using cross-polarization (CP) with a ¹H–¹³C contact time of 1.2 ms. With a recycle delay of 3 s, the CP-MAS experiments were performed with a proton 90° pulse time of 4 or 4.55 µs for HEA-1 or IBoA-1 samples, respectively. For the HEA-1 samples, the number of scans was 32,768, with the number of points collected for the experiments was 1024, and a sweep width of 598 ppm. For the IBoA-1 samples, 2400 to 4000 scans were acquired and the acquisition time was 30 ms, with 3742 points collected for a sweep width of 497 ppm. All shifts reported were referenced to tetramethylsilane (TMS) in the solid state indirectly using adamantane (δ = 38.48)^{50 (link)–52 (link)}.

Schwartz J.J, & Boydston A.J. (2019). Multimaterial actinic spatial control 3D and 4D printing. Nature Communications, 10, 791.

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NMR Relaxation Dispersion of Biomolecules

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All experiments were acquired on a Bruker Avance III spectrometer at a static magnetic field of 14.1 T and 298 K. Additionally, relaxation dispersion experiments on CspB were recorded on Bruker Avance III spectrometer at a static magnetic field of 18.8 T. Samples contained 1–3 mM protein (except carbonic anhydrase, which was below 100 µM) and 10% (v/v) D₂O. ¹H CPMG relaxation dispersion experiments were performed with refocusing frequencies between 100 and 1000 Hz (2000 Hz in case of CspB) and B1 field strengths for the CPMG pulses between 13 and 15 kHz. Spectra were processed with NMRPipe (Delaglio et al. 1995 (link)) and analyzed with PINT (Ahlner et al. 2013 (link)).

Raum H.N., Dreydoppel M, & Weininger U. (2018). Conformational exchange of aromatic side chains by 1H CPMG relaxation dispersion. Journal of Biomolecular Nmr, 72(1), 105-114.

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High-Field Solid-State NMR of Materials

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The ¹H MAS NMR experiments were performed at a magnetic
field of 14.1 T (600.12 MHz ¹H Larmor frequency) and a
MAS frequency of 60 kHz on a Bruker AVANCE-III spectrometer equipped
with a 1.3 mm MAS HX probe. Spectra were acquired using a rotor-synchronized,
double-adiabatic spin-echo sequence with a 1.2 μs 90° excitation
pulse length, followed by a pair of 50 μs tanh/tan short high-power
adiabatic pulses (SHAPs) with 5 MHz frequency sweep.^{20 (link)−22 (link)} All pulses were applied at a nutation frequency of 208 kHz. Signal
transients (4096) with a 5 s recycle delay were accumulated for each
sample. The shifts were referenced with respect to tetramethylsilane
(TMS) at 0 ppm. The ²H MAS NMR spectrum was recorded on
a 9.4 T (61.41 MHz ²H Larmor frequency) Bruker AVANCE-III
spectrometer with a 2.5 mm MAS HX probe at a spinning frequency of
30 kHz. The same pulse sequence as for protons was used but with a
3.0 μs 90° excitation pulse and 66.67 μs SHAPs at
a nutation frequency of 83 kHz. Scans (4096) with a 20 s recycle delay
were collected. The shifts were referenced to deuterated TMS (TMS-d₁₂) at 0 ppm.

Nedumkandathil R., Jaworski A., Grins J., Bernin D., Karlsson M., Eklöf-Österberg C., Neagu A., Tai C.W., Pell A.J, & Häussermann U. (2018). Hydride Reduction of BaTiO3 − Oxyhydride Versus O Vacancy Formation. ACS Omega, 3(9), 11426-11438.

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Solid-state NMR Characterization of Ru Complexes

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¹H magic‐angle spinning (MAS) NMR experiments were performed at a magnetic field of 14.1 T (¹H Larmor frequency of 600.12 MHz) on a Bruker Avance‐III spectrometer with a 1.3 mm probehead and 60.00 kHz MAS rate. Acquisitions involved a rotor‐synchronized, double‐adiabatic spin‐echo sequence with a 90° excitation pulse of 1.25 μs followed by a pair of 50.0 μs tanh/tan short high‐power adiabatic pulses (SHAPs) with a 5 MHz frequency sweep. All pulses operated at a nutation frequency of 200 kHz. 128 signal transients with a 5 s relaxation delay were collected. ¹H−¹³C cross‐polarization (CP) MAS experiments were performed at a magnetic field of 9.4 T (Larmor frequencies of 400.13, and 100.61 MHz for ¹H and ¹³C, respectively) on a Bruker Avance‐III spectrometer with a 4 mm probehead and 14.00 kHz MAS rate. Experiments involved Hartmann‐Hahn‐matched ¹H and ¹³C radiofrequency fields applied for 1.5 ms, SPINAL‐64 proton decoupling and 5 s relaxation delay. Chemical shifts were referenced with respect to neat tetramethylsilane (TMS). Models of the Ru_MACHO^TM and APTS(Me) were energy optimized at the revPBE‐D4/def2‐TZVP(Ru)/pcseg‐1 level of theory, and the ¹³C NMR shifts subsequently calculated at the PBE0/def2‐TZVP(Ru)/pcSseg‐1 level with the GIAO approach; in analogy to the protocol in Ref. [37]. Calculations were done with the ORCA code.^[42]

Szego A.E., Church T.L., Bacsik Z., Jaworski A., Ullah L, & Hedin N. (2023). Precapture of CO2 and Hydrogenation into Methanol on Heterogenized Ruthenium and Amine‐Rich Catalytic Systems. ChemistryOpen, 12(6), e202300060.

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NMR Spectroscopic Analysis Protocol

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All the NMR spectra were acquired at 298 K on a 600 MHz BRUKER AVANCE III spectrometer (Bruker, Switzerland) equipped with a cryoprobe. All pulse sequences were undertaken from the Bruker pulse program library. The standard noesygppr1d was employed as a water peak suppression pulse sequence. The 90° pulse width was adjusted to 9 μs for each sample. A total of 65536 data points were collected via 16 scans under conditions of detective frequency at 600.20 MHz, spectrum width (SW) at 20.0253 ppm, central position (O₁) at 4.701 ppm, and a relaxation delay of 5 s. In order to accurately assign the proton signals of the studied compounds, ¹³C-NMR, ¹H-¹H correlation spectroscopy (¹H-¹H COSY), heteronuclear single quantum coherence (HSQC), and heteronuclear multiple bond correlation (HMBC) spectra were recorded for the tested samples. From the tested compounds and TSP-d₄, spin-lattice relaxation time (T₁) values of the quantified protons were measured using a classical inversion recovery pulse sequence with 20 relaxation delays (τ) ranging from 0.001 to 20 s.

Wang Z., Wang Z., Jiang M., Yang J., Meng Q., Guan J., Xu M, & Chai X. (2022). Qualitative and Quantitative Evaluation of Chemical Constituents from Shuanghuanglian Injection Using Nuclear Magnetic Resonance Spectroscopy. Journal of Analytical Methods in Chemistry, 2022, 7763207.

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Peracetylation and Characterization of Compound Z

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Peracetylation of compound Z was performed in pyridine:acetic anhydride 1:1 for 1 h at 100 °C. After drying, three extractions with H₂O:diethyl ether (1:1) were done; the ether phases were collected, washed three times with water and dried. MALDI-TOF MS analyses were performed in the positive ionization and reflectron mode, using the 5800 MALDI-TOF/TOF Analyzer (Applied Biosystems/ABsciex) equipped with a Nd:YAG laser (349 nm wavelength) as described previously^{16 (link)}. ¹H-NMR and ¹H-¹H-NMR COSY spectra were recorded in CDCl₃ at 298° K using a 600-MHz Bruker Avance III spectrometer (Bruker Biospin) equipped with a TCI cryoprobe. Chemical shift values were referenced to CHCl₃ resonance (δH 7.26 ppm). The quantification of MAME unsaturations was performed with TopSpin 3.5 pl7 software.

Lefebvre C., Frigui W., Slama N., Lauzeral-Vizcaino F., Constant P., Lemassu A., Parish T., Eynard N., Daffé M., Brosch R, & Quémard A. (2020). Discovery of a novel dehydratase of the fatty acid synthase type II critical for ketomycolic acid biosynthesis and virulence of Mycobacterium tuberculosis. Scientific Reports, 10, 2112.

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Hypoxia Impacts on BCR-ABL Metabolome

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CB or CB transduced BCR-ABL day 20 cells (+/- 24 hours of hypoxia) were used for NMR analyses. 20–30 million cells were quenched and the intracellular metabolites were extracted, evaporated using a SpeedVac concentrator and stored at 80°C until further analysis. For the NMR analysis dried samples were resuspended in 60 ml of 100mM sodium phosphate buffer containing 500 mM TMSP ((3-trimethylsilyl)propionic-(2,2,3,3-d4)-acid sodium salt) and 10% D₂O, pH 7.0. Samples were vortexed, sonicated and centrifuged briefly, before being transferred into a 1.7mm NMR tube using an automated Gilson sample handler. One-dimensional 1D ¹H-NMR spectra were acquired using a 600-MHz Bruker Avance III spectrometer (Bruker Biospin) with a TCI 1.7mm z-PFG cryogenic probe at 300 K. Each sample was automatically tuned, matched and then shimmed before acquisition of the spectrum. Spectra were processed using the MATLAB-based MetaboLab software [39 (link)]. The chemical shift was calibrated by referencing the TMSP signal to 0 ppm. Spectra were exported into Bruker format for metabolite identification and to determine concentrations using the Chenomx 7.0 software. The extracellular metabolites were measured directly in the used culture medium. All data presented here are in μMolar concentrations.

Sontakke P., Koczula K.M., Jaques J., Wierenga A.T., Brouwers-Vos A.Z., Pruis M., Günther U.L., Vellenga E, & Schuringa J.J. (2016). Hypoxia-Like Signatures Induced by BCR-ABL Potentially Alter the Glutamine Uptake for Maintaining Oxidative Phosphorylation. PLoS ONE, 11(4), e0153226.

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Solid-State NMR Analysis of Biomolecules

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All ssNMR experiments were examined on a triple-channel 400 MHz Bruker AVANCE III spectrometer (Bruker BioSpin, Billerica, MA, USA) in the Biopharmaceutical NMR Lab (BNL) at Pharmaceutical Sciences, MRL (Merck & Co., Inc. West Point, PA, USA). One-dimensional (1D) ¹³C spectra were obtained at magic angle spinning (MAS) of 12 kHz with a Bruker 4 mm HFX MAS probe in double-resonance mode tuned to ¹H and ¹³C-nucleus frequencies. ¹³C spectra were referenced to the tetramethylsilane (TMS). All spectra were obtained at 298 K and processed in Bruker Topspin software (Bruker Corporation, Billerica, MA, USA). 1D ¹³C cross-polarization (CP) transfers were performed with a radio-frequency (RF) strength of 80–100 kHz during a 2 ms contact time. The power level was ramped linearly over a depth of 15–20 kHz on the ¹H channel to enhance CP efficiency. ¹H heteronuclear decoupling for ¹³C was performed at an RF strength of 100 kHz using the SPINAL-64 pulse sequence. ¹H spin-lattice relaxation times in the laboratory frame (T₁) were determined by ¹³C-detected saturation recovery experiments [36 (link)].

Liu X., Lu X., Su Y., Kun E, & Zhang F. (2020). Clay-Polymer Nanocomposites Prepared by Reactive Melt Extrusion for Sustained Drug Release. Pharmaceutics, 12(1), 51.

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Solid-State NMR Analysis of Samples

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NMR analysis was conducted with a standard bore 300 MHz Bruker Avance III spectrometer (Bruker BioSpin, Billerica, MA) equipped with a 4 mm magic angle spinning (MAS) probe, operating at a spinning frequency of 12,000 Hz, following the method by Longbottom et al. (2017) . Spectra were acquired with a variable amplitude cross-polarization (CP) sequence with 1 ms contact time and composite pulse decoupling during signal acquisition. All spectra were exponentially apodized, zero filled to 16,384 data points, and Fourier transformed with 50 Hz line broadening. Dipolar dephasing experiments were carried out on each sample allowing a dephasing delay of 70 μs, following the methods by Smernik and Oades (2011) .

Liu J., Lujan H., Dhungana B., Hockaday W.C., Sayes C.M., Cobb G.P, & Sharma V.K. (2020). Ferrate(VI) pretreatment before disinfection: An effective approach to controlling unsaturated and aromatic halo-disinfection byproducts in chlorinated and chloraminated drinking waters. Environment international, 138, 105641.

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