Avance 3 600 mhz spectrometer

Manufactured by Bruker

Sourced in Germany, United States, Switzerland, United Kingdom

The Avance III 600 MHz spectrometer is a nuclear magnetic resonance (NMR) spectrometer designed for high-resolution analysis of chemical samples. It operates at a frequency of 600 MHz for proton (1H) NMR measurements. The spectrometer provides precise and reliable data acquisition for a wide range of NMR applications.

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Lab products found in correlation

1260 liquid chromatography system, by Agilent Technologies (10 mentions) Gf254, by Qingdao Haiyang Chemical (9 mentions) Topspin 3, by Bruker (9 mentions) Silica gel, by Qingdao Haiyang Chemical (8 mentions) 5 mm tci cryoprobe, by Bruker (6 mentions) 2707 autosampler, by Waters Corporation (6 mentions) Sephadex lh 20, by Cytiva (6 mentions) Zorbax sb c18 column, by Agilent Technologies (6 mentions) Sephadex lh 20, by GE Healthcare (5 mentions) Sb c18 column, by Agilent Technologies (5 mentions) 5 mm bbfo probe, by Bruker (5 mentions) Autopol 4 automatic polarimeter, by Rudolph Research Analytical (4 mentions) Waters 2535 hplc, by Waters Corporation (4 mentions) Sepa 300 polarimeter, by Horiba (4 mentions) Fourier transform infrared spectrometer, by Shimadzu (4 mentions) Dad detector, by Agilent Technologies (4 mentions) Agilent 6200 q tof ms system, by Agilent Technologies (4 mentions) 5 mm qci 1h 13c 15n 31p probe, by Bruker (4 mentions) Cosmosil c18 column, by Nacalai Tesque (3 mentions) Cosmosil c8 column, by Nacalai Tesque (3 mentions)

Close spelling variants of this product

FT-NMR AVANCE III HD 600 MHz spectrometer AVANCE III 600 MHz Digital NMR Spectrometer Avance III HD 600 MHz NMR spectrometer Avance III 600 MHz NMR spectrometer AVANCE III HD 600 MHz spectrometer AVANCE III 600 MHz FT-NMR spectrometer Avance III HD Ascend 600 MHz spectrometer Avance III HD 600 MHz WB spectrometer Avance 600 MHz spectrometer Avance III 600 MHz

193 protocols using avance 3 600 mhz spectrometer

Metabolite Annotation by 1D and 2D NMR

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All 1D experiments were run using a Bruker Avance III 600 MHz spectrometer equipped with SampleJet. Samples were analysed using one-dimensional watersuppressed 1 H NOESY experiments at 300 K.
Additional 1 H-1 H J-resolved experiments, and 2D-NMR experiments, including 1 H-1 H Total Correlation Spectroscopy (TOCSY), 1 H-1 H Correlation Spectroscopy (COSY), and 1 H- 13 C Heteronuclear Single Quantum Coherence spectroscopy (HSQC), were utilised for metabolite annotation. The data from the 2D NMR experiments was acquired using a Bruker Avance III 600 MHz spectrometer equipped with a cryoprobe.

McGill D., Chekmeneva E., Lindon J.C., Takats Z, & Nicholson J.K. (2019). Application of novel solid phase extraction-NMR protocols for metabolic profiling of human urine. Faraday discussions, 218(0).

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NMR Characterization of Chemical Compounds

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NMR spectra were recorded in D₂O or DMSO-d₆. ¹H NMR spectra were recorded on a Bruker Avance III 400 MHz spectrometer, a Bruker Avance III HD 500 MHz spectrometer, and a Bruker Avance III 600 MHz spectrometer. ¹³C NMR spectra and all 2D NMR spectra (¹H DOSY, ¹H–¹H COSY, ¹H–¹H NOESY, ¹H–¹H TOCSY, ¹H–¹H ROESY, and ¹H–¹³C HSQC) were recorded on a Bruker Avance III 600 MHz spectrometer. Chemical shifts (δ) are expressed in parts-per-million (ppm) and reported relative to the resonance of residual solvent (4.79 ppm at room temperature; for spectra recorded at higher temperatures, the resonance of residual solvent was set to 4.55 ppm for 320 K and 4.45 ppm for 330 K, according to ref. ^{78 (link)}). For ¹H NMR spectra recorded at high dilution, a water suppression program was used.

Yanshyna O., Białek M.J., Chashchikhin O.V, & Klajn R. (2022). Encapsulation within a coordination cage modulates the reactivity of redox-active dyes. Communications Chemistry, 5, 44.

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NMR Relaxation Experiments for Biomolecular Dynamics

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Relaxation experiments were conducted on Bruker Avance Ⅲ 600 MHz spectrometer at 298 K. Standard pulse sequences were used to obtain longitudinal and transverse relaxation rates R₁ and R₂, as well as {¹H}-¹⁵N heteronuclear steady-state NOEs (hnNOEs). For ¹⁵N T₁ measurements, the delay times were set to 0.01, 0.05, 0.1, 0.2, 0.4, 0.8, 1.2, 1.5, and 1.8 s in random order. For ¹⁵N T₂ measurements, the delay times were set to 16.96, 33.92, 50.88, 67.84, 84.80, 101.76, 118.72, 135.68, 152.64, and 186.56 ms in random order. Two delay times were duplicated for both T₁ and T₂ experiments at the end of the experiments to estimate uncertainties of T₁ and T₂ values. For hnNOE experiments, a delay of 2 s was followed by ¹H saturation of 3 s, and in the control experiments without ¹H saturation, a total delay of 5 s was applied. The relaxation data were processed and analyzed with Bruker Dynamics Center 2.3 (Bruker, Billerica, MA, USA).

Guo C., Zhang H., Lin W., Chen H., Chang T., Wu Z., Yu J, & Lin D. (2022). ADP-Induced Conformational Transition of Human Adenylate Kinase 1 Is Triggered by Suppressing Internal Motion of α3α4 and α7α8 Fragments on the ps-ns Timescale. Biomolecules, 12(5), 671.

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NMR Titration Analysis of hAK1 Binding

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NMR titration experiments were conducted on Bruker Avance Ⅲ 600 MHz spectrometer (Bruker, Billerica, MA, USA) at 298K. The apo-hAK1 sample was solved in NMR buffer added with 5 mM EDTA. The holo-hAK1 sample was solved in NMR buffer added with 5 mM MgCl₂, and ADP was titrated step-by-step according to the following molar ratios of protein: ligand: 1:0, 1:0.5, 1:1, 1:2, 1:3, 1:4, 1:5, 1:6, 1:7, 1:8. We calculated chemical shift perturbations (∆δ) of hAK1 at the molar ratio of 1:8, using the following formula:

Δ δ = \sqrt{{Δ δ}^{2} ({}^{1}H) + {Δ δ}^{2} ({}^{15}N) / 25},

where ∆δ(¹H) is the perturbation in proton and ∆δ(¹⁵N) is the perturbation in nitrogen dimension.

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Analytical Characterization of Compounds

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Stable isotopically labeled compounds were purchased from Cambridge Isotope Laboratories, Inc. The corresponding unlabeled compounds were purchased from ThermoFisher Scientific. All solvents used for UPLC and HPLC were Optima grade, and water used for chromatography was purified by a Milli-Q water purification system. High resolution MS for pure compounds and metabolomics experiments were performed on a Water Synapt G2Si q-TOF system. NMR spectra were acquired on a Bruker AVANCE III 600 MHz spectrometer, with a 5 mm TCI cryoprobe, and referenced to residual solvent proton and carbon signals. UV spectra were obtained on an Agilent Cary 300 spectrophotometer. Optical rotations were measured on a Perkin Elmer 341 polarimeter.

McCaughey C.S., van Santen J.A., van der Hooft J.J., Medema M.H, & Linington R.G. (2021). An Isotopic Labeling Approach Linking Natural Products with Biosynthetic Gene Clusters. Nature chemical biology, 18(3), 295-304.

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Analytical Characterization of Compounds

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Semi-preparative HPLC Purification of Compounds

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Semi-preparative HPLC purification was performed on a Waters 2535 HPLC connected with a 2998 PDA Detector and a 2707 Autosampler (Waters, Milford, MA, USA). Separations were performed on a COSMOSIL C18 column (5 μm, 10 × 250 mm) (Nacalai Tesque, Kyoto, Japan), a COSMOSIL C8 column (5 μm, 10 × 250 mm) (Nacalai Tesque, Kyoto, Japan) and a YMC-pack diol column (5 μm, 10 × 50 mm; 5 μm, 20 × 150 mm) (Yamamura Chemical Research, Kyoto, Japan). Direct injection high resolution ESIMS and LC-DAD-ESIMS analyses were recorded on an ultra-performance liquid chromatography-quadrupole/electrostatic field orbitrap high resolution mass spectrometry (Thermo Fisher Scientific, Waltham, MA, USA). The NMR spectra were recorded on an AVANCE III 600 MHz spectrometer (Bruker BioSpin, Ettlingen, Germany). Optical rotations were recorded on an Autopol IV Automatic Polarimeter (Rudolph Research Analytical, Hackettstown, NJ, USA). Chromatography grade solvents were used for HPLC, and all other chemical reagents were analytical grade. Sephadex LH-20 dextran gel was purchased from Amersham Pharmacia Biotech Co. (Piscataway, NJ, USA).

He J., Tang P., Liu M., Liao G., Lu R, & Yang X. (2023). Triterpenoid saponins and C21 steroidal glycosides from Gymnema tingens and their glucose uptake activities. RSC Advances, 13(11), 7503-7513.

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Quantitative Lipoprotein Analysis by NMR

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Quantitative analysis of circulating lipoproteins was performed at the nuclear magnetic resonance facility at Gothenburg using a Bruker Avance III 600 MHz spectrometer.^{27 (link),42 (link)} Plasma samples from 16 patients and 13 healthy subjects were available for lipoprotein profile analysis. The analysis was performed according to the Bruker in vitro diagnostics research standard operating procedures (https://www.bruker.com/products/mr/nmr/avance-ivdr/overview.html). Lipoprotein fractions were obtained using Bruker in vitro diagnostics research methods.^{23 (link)} For information about principal lipoprotein fractions, refer to Supplemental Table 1, and for the list of measured lipoprotein fractions/subfractions, refer to Supplemental Table 2 (available at http://links.lww.com/PR9/A171).

Jönsson M., Bäckryd E., Jonasson L., Gerdle B, & Ghafouri B. (2022). Differences in plasma lipoprotein profiles between patients with chronic peripheral neuropathic pain and healthy controls: an exploratory pilot study. Pain Reports, 7(5), e1036.

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NMR Characterization of Smad5 Complexes

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NMR data were acquired on a Bruker Avance III 600-MHz spectrometer equipped with a cryogenic probe head and a z-pulse field gradient unit at 298 K using Non-Uniform Sampling (NUS) and BEST-TROSY backbone experiments [8] (link), [48] , [66] (link), [68] (link), [77] (link). Proline residues were connected using a set of specific experiments [13] (link). T₁ and T₂ relaxation measurements were acquired using standard pulse sequences [8] (link). The rotational correlation times (τ_c) of the Smad5, Smad5-gly as well as of their complexes with DNA were calculated essentially as described [73] (link), [54] (link), [5] (link) using several protein concentrations in buffer 1 supplemented with 10% D₂O. Spectra were processed with NMRPipe [20] and MddNMR [66] (link). Backbone assignment was performed with CARA [10] as previously described [54] (link), [5] (link). T₁, T₂ and hetNOE data were processed and integrated with TopSpin3.5, Bruker BioSpin Corp. (https://www.bruker.com). K_D fittings from R₂ values were calculated with GraphPad Prism following established procedures [11] (link).
Molecular Weight determinations from τ_c values were performed using the correlations determined by the Northeast Structural Genomics Consortium and collected in the literature [72] (link), with the following relation: MW = 1.569*τ_c + 0.4972.

Ruiz L., Kaczmarska Z., Gomes T., Aragon E., Torner C., Freier R., Baginski B., Martin-Malpartida P., de Martin Garrido N., Marquez J.A., Cordeiro T.N., Pluta R, & Macias M.J. (2021). Unveiling the dimer/monomer propensities of Smad MH1-DNA complexes. Computational and Structural Biotechnology Journal, 19, 632-646.

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NMR-based Metabolite Profiling of Biological Samples

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Cecal content, feces and serum metabolites were extracted as previously described (Cai et al., 2016 (link); Shi et al., 2013 (link)). ¹H NMR spectra were recorded at 298 K on a Bruker Avance III 600 MHz spectrometer equipped with an inverse cryogenic probe (Bruker Biospin, Germany). NMR spectra of cecal and fecal samples were acquired using the first increment of NOESY pulse sequence with presaturation (Bruker 1D noesygppr1d pulse sequence). The serum spectra were acquired with a Carr-Purcell-Meiboom-Gill pulse sequence [recycle delay-90°-(τ−180°-τ)_n-acquisition]. Quality of all spectra were improved by phase adjustment, baseline correction and calibration using Topspin 3.0 (Bruker Biospin, Germany). The spectral region δ 0.50–9.50 was integrated into bins with equal width of 0.004 ppm (2.4 HZ) using AMIX package (V3.8, Bruker Biospin) for relative concentration analysis. The metabolites were assigned based on published results (Cai et al., 2016 (link); Dong et al., 2013 (link); Tian et al., 2012 (link)).

Chagwedera D.N., Ang Q.Y., Bisanz J.E., Leong Y.A., Ganeshan K., Cai J., Patterson A.D., Turnbaugh P.J, & Chawla A. (2019). Nutrient sensing in CD11c cells alters the gut microbiota to regulate food intake and body mass. Cell metabolism, 30(2), 364-373.e7.

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