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Avance 2 nmr spectrometer

Manufactured by Bruker
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Sourced in Germany, United States

The Avance II NMR spectrometer is a nuclear magnetic resonance (NMR) instrument used for analytical and structural elucidation applications. It provides high-resolution NMR spectroscopy capabilities for various sample types.

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Lab products found in correlation

Avance 3 nmr spectrometer, by Bruker (4 mentions) Micromass zq, by Waters Corporation (2 mentions) Avance 400 nmr spectrometer, by Bruker (2 mentions) Cdcl3, by Eurisotop (2 mentions) 215 liquid handler, by Gilson (1 mentions) Samplejet, by Bruker (1 mentions) Cryoprobe, by Bruker (1 mentions) Isolera chromatography system, by Biotage (1 mentions) Snap kp sil, by Biotage (1 mentions) Topspin 2, by Bruker (1 mentions) Atr reflector, by PIKE Technologies (1 mentions) Vertex 70, by Bruker (1 mentions) Cary 5000 uv vis nir spectrophotometer, by Agilent Technologies (1 mentions) Uv 2075, by Jasco (1 mentions) 6230 tofms, by Agilent Technologies (1 mentions) V 630 spectrometer, by Jasco (1 mentions) Biflex 4, by Bruker (1 mentions) Mx 2080 32, by Jasco (1 mentions) Nmr spectrometer, by Agilent Technologies (1 mentions) Combiflash system, by Teledyne (1 mentions)

Close spelling variants of this product

Avance spectrometer (419 citations) NMR spectrometer (293 citations) Avance II (229 citations) Avance NMR spectrometer (124 citations) Bruker spectrometers (71 citations) Avance II spectrometer (58 citations) Avance II 400 NMR spectrometer (23 citations) Avance II 400 MHz NMR spectrometer (14 citations) AVANCE-II 600 NMR spectrometer (12 citations) AVANCE II 600 MHz NMR spectrometer (12 citations)

37 protocols using avance 2 nmr spectrometer

1

NMR Metabolite Profiling of Plasma

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Plasma samples were thawed at 4°C in a cold room. Four hundred μL of saline solution (NaCl 0.9% in 10% D2O) was added to 200 μL of each plasma sample. The mixtures were vortexed for 1 minute and centrifuged at 16, 000 g for 15 min at 4°C and 550 μL of supernatant was transferred into 5 mm Bruker NMR tubes (Z105684 Bruker 96 well rack) using Gilson 215 Liquid Handler (Trilution software version 2.0). All 1H-NMR spectra were collected on a 600 MHz Avance II NMR spectrometer (Bruker Biospin, Rheinstetten, Germany) equipped with a 5 mm CryoProbe. A Bruker sampleJet operated by IconNMR in Topspin was used to record spectra automatically. 1D CPMG-presaturated spectra for plasma were recorded. Optimal probe tuning and matching, 90° pulse length, water offset, and receiver gain were adjusted on the representative sample. The probe was automatically locked to H2O+D2O (90%+10%) and shimmed for each sample. All NMR data were acquired at 300 K.
Liu H., Garrett T.J., Tayyari F, & Gu L. (2015). Profiling the Metabolome Changes Caused by Cranberry Procyanidins in Plasma of Female Rats using 1H NMR and UHPLC-Q-Orbitrap-HRMS Global Metabolomics Approaches. Molecular nutrition & food research, 59(11), 2107-2118.
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2

Purification and Characterization of Organic Compounds

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All commercial reagents were used without further purification. Reactions requiring the exclusion of air were carried out under an atmosphere of dry nitrogen in oven dried glassware. All reactions were monitored by thin-layer chromatography (TLC) carried out on EMD Chemicals silica gel 60-F 254 coated glass plates and visualized using UV light (254 nm). Analysis by LC-MS was performed by using an XBridge C18 column run at 1 mL/min and using gradient mixtures of (A) water (0.05% TFA) and (B) methanol. Low-resolution mass spectra (ESI) were collected on a Waters Micromass ZQ in positive-ion mode. Flash chromatography was performed on a Biotage Isolera chromatography system using Biotage SNAP KP-SIL pre-packed columns, and the solvent mixture in brackets was used as eluent. Nuclear magnetic resonance (NMR) spectra were obtained on a Bruker Avance II NMR spectrometer at 400 MHz for 1H NMR spectra. Chemical shifts (ppm) are reported relative to the solvent peak. Signals are designated as follows: s, singlet; d, doublet; dd, doublet of doublet; t, triplet; q, quadruplet; m, multiplet. Coupling constants (J) are shown in Hertz.
Evison B.J., Actis M.L, & Fujii N. (2016). A clickable psoralen to directly quantify DNA interstrand crosslinking and repair. Bioorganic & medicinal chemistry, 24(5), 1071-1078.
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3

NMR Characterization of Peptide-DPC Interactions

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All NMR experiments were carried out with either a Bruker Avance II NMR spectrometer of 750 MHz or an Avance III NMR spectrometer of 600 MHz, both equipped with a regular probe-head. Lyophilized peptides were either dissolved in water, or in water with 200 mM DPC. Pure peptide solutions were characterized by regular 1D 1H and 2D TOCSY (60 ms mixing time), 2D NOESY (150 ms mixing time) and 2D 1H-13C HSQC experiments at 600 MHz, while peptide–DPC mixtures were measured at 750 MHz. Experiments were carried out at 37 °C and 42 °C. Interaction with GM1 was studied by addition of GM1 to final concentration of 0.5 mM. The 1D 31P NMR spectra were recorded at 700 MHz without 1H decoupling, using an acquisition time of 0.9 s, a recycle delay of 5 s, and 64 scans. All spectra were processed using Bruker Topspin software suite.
Siebert H.C., Eckert T., Bhunia A., Klatte N., Mohri M., Siebert S., Kozarova A., Hudson J.W., Zhang R., Zhang N., Li L., Gousias K., Kanakis D., Yan M., Jiménez-Barbero J., Kožár T., Nifantiev N.E., Vollmer C., Brandenburger T., Kindgen-Milles D., Haak T, & Petridis A.K. (2023). Blood pH Analysis in Combination with Molecular Medical Tools in Relation to COVID-19 Symptoms. Biomedicines, 11(5), 1421.
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4

NMR Spectrometry of Organic Compounds

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NMR spectra were recorded on 3 different NMR spectrometers: (1) an Avance II NMR spectrometer (Bruker Biospin) with a vertical 7,05T narrow-bore/ultrashield magnet operating at 300 MHz for 1H observation and 75 MHz for 13C observation by means of a 5-mm direct BBO H/X probe with Z gradient capabilities; (2) an Avance 400 NMR spectrometer (Bruker Biospin) with a vertical 9.4T narrow-bore/ultrashield magnet operating at 400 MHz for 1H observation by means of a 5-mm direct QNP 1H/13C/31P/19F probe with gradient capabilities; (3) an Avance III NMR spectrometer (Bruker Biospin) with a vertical 16.45T narrow-bore/ultrashield magnet operating at 700 MHz for 1H observation by means of a 5-mm TXI 1H/13C/15N probe with Z gradient capabilities. Chemical shifts are reported in parts per million (ppm, δ) relative to the 1H residual signal of the deuterated solvent used. 1H NMR splitting patterns with observed first-order coupling are designated as singlet (s), doublet (d), triplet (t), or quartet (q). Coupling constants (J) are reported in hertz. Data processing was performed with Topspin 2.0 software. Samples were not degassed. CDCl3 from Eurisotop was used after filtration through an alumina pad followed by a distillation over calcium hydride.
Gan Q., Wang X., Kauffmann B., Rosu F., Ferrand Y, & Huc I. (2017). Translation of Rod-Like Template Sequences into Homochiral Assemblies of Stacked Helical Oligomers. Nature nanotechnology, 12(5), 447-452.
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5

Proton NMR Analysis of Calendula and Fucus

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For NMR spectroscopy, the proton spectra were recorded for the extracts of Calendula and Fucus with a 700 MHz Avance II NMR spectrometer (Bruker, Rheinstetten, Germany) equipped with a cryo-probe. The solvent was D2O, and the experimental temperature was 25 °C.
Winter C., Tetyczka C., Pham D.T., Kolb D., Leitinger G., Schönfelder S., Kunert O., Gerlza T., Kungl A., Bucar F, & Roblegg E. (2024). Investigation of Hydrocolloid Plant Polysaccharides as Potential Candidates to Mimic the Functions of MUC5B in Saliva. Pharmaceutics, 16(5), 682.
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6

General Organic Synthesis Procedures

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All commercial reagents were used without further purification, and the solvents were dried using a dry solvent system (Glass Contour Solvent Systems, SG Water USA). Reactions requiring the exclusion of air were carried out under an atmosphere of dry nitrogen in oven dried glassware. All reactions were monitored by thin-layer chromatography (TLC) carried out on EMD Chemicals silica gel 60-F 254 coated glass plates and visualized using UV light (254 nm). Analysis by LC-MS was performed by using an XBridge C18 column run at 1 mL/min and using gradient mixtures of (A) water (0.05% TFA) and (B) methanol. Low-resolution mass spectra (ESI) were collected on a Waters Micromass ZQ in positive-ion mode. Flash-chromatography was performed on a Biotage SP4 chromatography system using Biotage Flash + KP SIL pre-packed columns, and the solvent mixture in brackets was used as eluent. Nuclear magnetic resonance (NMR) spectra were obtained on a Bruker Avance II NMR spectrometer at 400 MHz for 1H NMR spectra. Chemical shifts (ppm) are reported relative to TMS or the solvent peak. Signals are designated as follows: s, singlet; d, doublet; dd, doublet of doublet; t, triplet; q, quadruplet; m, multiplet. Coupling constants (J) are shown in Hertz.
Evison B.J., Actis M.L., Wu Z., Shao Y., Heath R.J., Yang L, & Fujii N. (2014). A site-selective, irreversible inhibitor of the DNA replication auxiliary factor proliferating cell nuclear antigen (PCNA). Bioorganic & medicinal chemistry, 22(22), 6333-6343.
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7

NMR Spectroscopy Protocols for Biomolecular Structure and Dynamics

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A Bruker Avance-II NMR spectrometer (500.13 MHz 1H and 50.68 MHz 15N frequency) equipped with a multinuclear bbi z-gradient probehead was used for all measurements either at 298 K or 278 K temperature. Diffusion experiments were carried out using Bruker’s ‘ledbpgs2s’ stimulated echo DOSY pulse sequence including bipolar and spoil gradients. This was extended with a 2 × 4 ms spin echo period before the detection period to suppress the baseline shift [35 (link)]. 15N relaxation experiments were carried out according to [29 (link)] and evaluated with the model-free approach [30 (link),31 (link)] using the isotropic rotational diffusion approach and a single global correlation time. The recycle delays in T1, T2 experiments were typically 2.5 s, but 5 s in heteronuclear 15N-(1H) NOE. In water saturation difference experiments, two 15N-1H HSQC experiments were run, using 3 s selective water presaturation in one of them, and the difference was calculated by comparison with an undisturbed reference.
Izsépi L., Erdei R., Tevyashova A.N., Grammatikova N.E., Shchekotikhin A.E., Herczegh P, & Batta G. (2021). Bacterial Cell Wall Analogue Peptides Control the Oligomeric States and Activity of the Glycopeptide Antibiotic Eremomycin: Solution NMR and Antimicrobial Studies. Pharmaceuticals, 14(2), 83.
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8

Detailed NMR Spectroscopy Analysis Protocol

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NMR spectra were recorded on an Avance II NMR spectrometer (Bruker Biospin) with a vertical 7.05T narrow-bore/ultrashield magnet operating at 300 MHz for 1H observation, 75 MHz for 13C observation and 121.4 MHz for 31P observation by means of a 5-mm direct BBO H/X probe with Z gradient capabilities. Chemical shifts are reported in ppm and are referenced against residual solvent signals of CDCl3 (δH: 7.26, δC: 77.0), DMSO-d6 (δH: 2.50, δC: 39.4), HDO (δH: 4.8). 31P NMR signals are referenced to PPh3O at 27 ppm. Peak multiplicities are noted as follows: singlet (s), broad singlet (bs), doublet (d), triplet (t), quartet (q), doublet of doublets (dd), doublet of quartets (dq) and multiplet (m). Data processing was performed with Bruker TOPSPIN 2.1 software.
Corvaglia V., Carbajo D., Prabhakaran P., Ziach K., Mandal P.K., Santos V.D., Legeay C., Vogel R., Parissi V., Pourquier P, & Huc I. (2019). Carboxylate-functionalized foldamer inhibitors of HIV-1 integrase and Topoisomerase 1: artificial analogues of DNA mimic proteins. Nucleic Acids Research, 47(11), 5511-5521.
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9

ATR-FTIR and NMR Analysis of Segmented PUIs

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In this work the IR Fourier spectrometer Vertex 70 (Bruker, Bremen, Germany) and the ATR reflector (Pike Technologies, Fitchburg, WI, USA) were used. Zn-Se crystals in the form of prisms with an incidence angle of the radiation on the object θ = 45° were used as ATR elements.
The 1H and 13C NMR spectra of the segmented PUIs was recorded by a 500 MHz Bruker AVANCE II NMR spectrometer (Bruker, Fällanden, Switzerland) using deuterated DMSO-d6 as a solvent at 25 °C.
Sokolova M.P., Bugrov A.N., Smirnov M.A., Smirnov A.V., Lahderanta E., Svetlichnyi V.M, & Toikka A.M. (2018). Effect of Domain Structure of Segmented Poly(urethane-imide) Membranes with Polycaprolactone Soft Blocks on Dehydration of n-Propanol via Pervaporation. Polymers, 10(11), 1222.
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10

Detailed NMR and UV-Vis Analysis of Compounds

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1H-, 11B- and 13C-NMR analysis were performed for all compounds in the study. 1H and 13C spectra were recorded at 25 °C on a 600 MHz AVANCE II NMR spectrometer (Bruker, Johannesburg, South Africa) at 600.28 MHz and 150.95 MHz respectively. 11B-NMR spectra were recorded at 25 °C on a 400 MHz AVANCE III NMR spectrometer (Bruker, Johannesburg, South Africa) at 128.38 MHz. Hydrogen and carbon chemical shifts are relative to hydrogen and carbon in CDCl3 at 7.24 ppm and 77.16 ppm, respectively. The following abbreviations are used to describe peak patterns: s = singlet, d = doublet, t = triplet, q = quartet and m = multiplet. UV/vis spectra were recorded on a Cary 5000 UV-Vis-NIR Spectrophotometer (Varian, Johannesburg, South Africa).
Swarts P.J, & Conradie J. (2020). Synthesis, Spectroscopy, Electrochemistry and DFT of Electron-Rich Ferrocenylsubphthalocyanines. Molecules, 25(11), 2575.
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