1H-NMR spectra were recorded at 500 MHz using a Bruker AVANCE III 400 WB spectrometer (Bruker BioSpin AG, Fällanden, Switzerland). Chemical shifts were reported in ppm relative to residual deuterated solvent or to an internal standard (tetramethylsilane, TMS).
Avance 3 400 wb spectrometer
Manufactured by Bruker
Sourced in Switzerland, United States, Germany
The AVANCE III 400 WB spectrometer is a nuclear magnetic resonance (NMR) spectrometer designed and manufactured by Bruker. It operates at a magnetic field strength of 9.4 Tesla, enabling high-resolution analysis of chemical samples.
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Lab products found in correlation
Avance 3 600 wb spectrometer, by Bruker (1 mentions)
X pert pro, by Malvern Panalytical (1 mentions)
Cary 630 ftir spectrometer, by Agilent Technologies (1 mentions)
S 4800 scanning electron microscope, by Hitachi (1 mentions)
3flex apparatus, by Micromeritics (1 mentions)
Drx 300 spectrometer, by Bruker (1 mentions)
Tga sdta851e sf 1100, by Mettler Toledo (1 mentions)
D8 advance, by Bruker (1 mentions)
Double resonance mas probe head, by Bruker (1 mentions)
D8 quest diffractometer, by Bruker (1 mentions)
Asap 2460, by Micromeritics (1 mentions)
Quanta 400 feg, by Thermo Fisher Scientific (1 mentions)
D max 2200, by Rigaku (1 mentions)
Q50 tg, by TA Instruments (1 mentions)
Vector 22 ftir spectrometer, by Bruker (1 mentions)
X pert pro mrd x ray diffractometer, by Malvern Panalytical (1 mentions)
Sdt q600 thermogravimetric analyzer, by TA Instruments (1 mentions)
Maldi target plate, by Thermo Fisher Scientific (1 mentions)
Abi 4800 maldi tof tof mass spectrometer, by Thermo Fisher Scientific (1 mentions)
Vario el cube, by Elementar (1 mentions)
19 protocols using avance 3 400 wb spectrometer
1
NMR Spectroscopy Protocol for Chemical Analysis
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1H-NMR spectra were recorded at 500 MHz using a Bruker AVANCE III 400 WB spectrometer (Bruker BioSpin AG, Fällanden, Switzerland). Chemical shifts were reported in ppm relative to residual deuterated solvent or to an internal standard (tetramethylsilane, TMS).
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1H-NMR spectra were recorded at 500 MHz using a Bruker AVANCE III 400 WB spectrometer (Bruker BioSpin AG, Fällanden, Switzerland). Chemical shifts were reported in ppm relative to residual deuterated solvent or to an internal standard (tetramethylsilane, TMS).
2
Selective Monitoring of 13C Amorphous Signals
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All the 7Li and 13C MAS NMR experiments were performed on a Bruker AVANCE III 600 WB spectrometer (Bruker Inc., Karlsruhe, Germany) operating at 233.23 and 150.11 MHz for 7Li and 13C, respectively. In the 7Li experiments, the recycle delay was set to 150 s to ensure complete relaxation of the 7Li spins. The exchange time was set to 1–200 ms in the 2D 7Li–7Li exchange experiments; the MAS speed was 10 kHz. The static 7Li quantitative experiments were performed on a Bruker AVANCE III 400WB spectrometer operating at 155.52 MHz for 7Li. The 7Li and 13C chemical shifts were calibrated using LiCl aqueous solution (1 mol/L, 0 ppm) and adamantine (38.56 ppm), respectively.
We designed a unique pulse sequence for 13C single pulse excitation NMR to monitor the 13C amorphous signals. This sequence used a very short relaxation delay to recover the desired amorphous signals selectively (seeFigure 2 ). The train of the π/2 pulses saturated the signals recovered during the recycling delay. The following relaxation delay was then used to recover the desired signals selectively with a very fast T1 relaxation (spin lattice relaxation). The relaxation delay was set to 0.05 s to select the mobile amorphous signals.
We designed a unique pulse sequence for 13C single pulse excitation NMR to monitor the 13C amorphous signals. This sequence used a very short relaxation delay to recover the desired amorphous signals selectively (see
3
Solid-State NMR Characterization of Adsorbed Organic Species
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The 133Cs and 13C MAS NMR experiments were performed using a Bruker Avance III 400WB spectrometer at the resonance frequencies of 52.5 MHz and 100.6 MHz, respectively. 133Cs MAS NMR spectra were recorded with single-pulse excitation of 2.0 µs and the repetition time of 3 s. A sample spinning rate of 22 kHz was used and 24,000 scans were accumulated. The chemical shifts were referenced to a 1.0 M solution of CsCl. 13C MAS NMR measurements were performed via exciting the 13C spins with single-pulses of 2.0 µs and with a repetition time of 20 s thus avoiding relaxation effects by T1. The sample spinning rate was 8 kHz and 320 scans were collected for each spectrum. The chemical shifts of the 13C nuclei in the adsorbed organic species were determined with respect to tetramethylsilane as the external reference with an accuracy ±1 ppm.
4
Comprehensive Materials Characterization Protocol
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Infrared spectra were recorded on an Agilent Cary 630 FTIR spectrometer equipped with an ATR module. Thermogravimetric analysis was carried out with a Mettler Toledo TGA/SDTA 851e/SF/1100 between 25 and 800 °C at a rate of 5 °C min–1 with a flow of N2 : O2 (4 : 1). PXRD patterns were collected in a PANalytical X'Pert PRO diffractometer using copper radiation (Cu Kα) with an X'Celerator detector, operating at 40 mA and 45 kV. Profiles were collected in the 2° < 2θ < 90° range with a step size of 0.013. Particle morphologies and dimensions were studied with a Hitachi S-4800 scanning electron microscope operating at 20 kV over metalized samples. Surface area, pore size and volume values were calculated from nitrogen adsorption–desorption isotherms recorded at 77 K on a Micromeritics 3Flex apparatus. Samples were degassed overnight at 150 °C and 10–6 Torr prior to analysis. Surface areas were estimated according to the BET model and pore size dimensions were calculated using Non-Linear Density Functional Theory (NLDFT) models for the adsorption branch assuming a cylindrical pore model. 13C-CP-MAS-NMR was carried out on a Bruker Avance III 400 WB Spectrometer. Samples were loaded in a 4 mm zirconia rotor and spun at 8 kHz. 1H-NMR spectra were run on a Bruker DRX300 spectrometer. See ESI† for additional experimental details on digestion of the solids for NMR study.
5
Characterization of Crystalline and Amorphous States
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The structure of crystalline and amorphous states of the samples synthesized were characterized by powder X-ray diffraction, which was performed on a D8 ADVANCE powder diffractometer (Bruker AXS, Karlsruhe, Germany), using Cu Kα radiation (λ = 1.5418 Å) with a step size of 0.02°.
Temperature-dependent studies of Raman spectra were performed on a Horiba Jobin Y’von LabRAM HR800 micro_Raman spectrometer equipped with a microscopic heating furnace (Linkam, TS1500, Epsom, UK) with a temperature deviation about ±1 K. A 355 nm ultraviolet pulse laser beam operating at 100 mW was used as an excitation source. The slits were set to achieve a resolution of 2 cm−1.
The 27Al MAS NMR spectra were obtained using a Bruker AVANCE III 400 WB spectrometer operating at 9.4 T with a spinning rate of 10 kHz. A recycle delay of 2 s was used along with a 4 mm double resonance MAS probe. The chemical shift values for 27Al nuclei were determined with reference to a 1 M aqueous solution of Al(NO3)3.
Temperature-dependent studies of Raman spectra were performed on a Horiba Jobin Y’von LabRAM HR800 micro_Raman spectrometer equipped with a microscopic heating furnace (Linkam, TS1500, Epsom, UK) with a temperature deviation about ±1 K. A 355 nm ultraviolet pulse laser beam operating at 100 mW was used as an excitation source. The slits were set to achieve a resolution of 2 cm−1.
The 27Al MAS NMR spectra were obtained using a Bruker AVANCE III 400 WB spectrometer operating at 9.4 T with a spinning rate of 10 kHz. A recycle delay of 2 s was used along with a 4 mm double resonance MAS probe. The chemical shift values for 27Al nuclei were determined with reference to a 1 M aqueous solution of Al(NO3)3.
6
Starch Crystallinity Analysis by NMR
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The 13C CP/MAS NMR analysis of starch was performed on a Bruker Avance III 400 WB spectrometer according to a previously established method [19 (link)]. And the calculation of the specific relative crystallinity (RC), double helix content (DH), and amorphous phase (PPA) adopted the method of Yin et al., and Atichokudomchai et al. [24 (link),25 (link)].
7
Structural Analysis of Hydrogels
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Chemical structures of the hydrogels were investigated by ATR–FTIR spectroscopy using a Nicolet™ iS50 FTIR Spectrometer in the 4000–500 cm−1 range with a resolution of 4 cm−1, and an average of 32 scans were acquired. The analysis was performed in triplicate. 13C Magic-angle spinning nuclear magnetic resonance (13C MAS NMR) spectra of neat CS, pure PVA, and CS/PVA gel beads were acquired using an AVANCE III 400 WB spectrometer (Bruker, Billerica, MA, USA) operated at a frequency of 400 MHz to explore the chemical structures of the crosslinked hydrogels.
8
Quantitative NMR Analysis of Adsorbed Molecules
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The solid-state MAS NMR experiments were carried out using a Bruker Avance III 400WB spectrometer at room temperature. MAS speed of all our samples was 12 kHz. The high-power decoupling was used for the quantitative 31P analysis. Considering the long relaxation time of 31P nuclei in NMR experiment, we used 30° pulse with the width of 1.20 μs, 15 s delay time. The radiofrequency for decoupling was 59 kHz. The spectral width was 400 p.p.m., from 200 to −200 p.p.m. The number of scanning was 800. The 31P chemical shifts were reported relative to 85% aqueous solution of H3PO4, with NH4H2PO4 as a secondary standard (0.81 p.p.m.). The quantitative analysis of adsorbed TMP molecules was calculated according to the calibration line established by running standard samples with various adsorbed TMP concentration (see Supplementary Note 7 , Supplementary Figs. 20 –22 and Supplementary Table 7 for more details).
9
Quantitative 31P NMR Spectroscopy of Adsorbed TMPO
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Solid-state MAS NMR spectroscopy experiments were carried out using a Bruker Avance III 400WB spectrometer at room temperature. To remove the effect of proton spins on quantitative 31P spectra (i.e., Fig. 4a ), a strong radio frequency field (B) is usually applied at the resonance frequency of the non-observed abundant spins (1H herein), which contribute to the coupling of both spin species. The high power decoupling was thus used for the quantitative 31P analysis. Considering the long relaxation time of 31P nuclei in NMR spectroscopy experiment, 30° pulse with 1.20 μs width and 15 s delay time. The radiofrequency for decoupling was 59 kHz. The spectral width was 400 ppm, from 200 to −200 ppm. The number of scanning was 800 and spinning frequency was 10 kHz. The 31P chemical shifts were reported relative to 85% aqueous solution of H3PO4, with NH4H2PO4 as a secondary standard (0.81 ppm). The quantitative analysis of adsorbed TMPO molecules was then calculated according to the calibration line established by running standard samples with various adsorbed TMPO concentration47 (link), 48 (link). On the other hand, for samples without adsorbing TMPO (Supplementary Fig. 4 ), the 1H-31P cross-polarization was used.
10
Cellulose Isolation and Characterization
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The crystallinity and crystal forms of the cellulose were characterized by solid-state cross-polarization/magic angle spinning (CP/MAS) 13C NMR. Cellulose was isolated according to the following protocol, as modified from a previous procedure [26 (link)]; Briefly, the fiber samples (9 g) were dispersed into 750 mL of deionized water. Then glacial acetic acid (6 mL) and sodium chlorite (6 g) were added to the mixture. The mixture was sealed in a reaction flask and maintained at 70 °C with stirring for 2 h. This treatment was repeated until the solid residue turned white and the lignin content was very low. After that, cellulose was isolated from 2 g of solid residue by soaking in 200 mL of 2.5 M HCl at 100 °C for 4 h and was then filtered and washed with deionized water.
Solid-state NMR measurements were carried out on a AVANCE III 400 WB spectrometer (Bruker, Germany) operating at a frequency of 100.69 MHz for 13C using a 4-mm Bruker double-resonance MAS probe head at a spinning speed of 10 kHz. Acquisition was performed with a CP pulse sequence using a 2.5-µs proton 90° pulse, a 1.5-ms contact pulse, and a 3.0-s delay between repetitions.
Solid-state NMR measurements were carried out on a AVANCE III 400 WB spectrometer (Bruker, Germany) operating at a frequency of 100.69 MHz for 13C using a 4-mm Bruker double-resonance MAS probe head at a spinning speed of 10 kHz. Acquisition was performed with a CP pulse sequence using a 2.5-µs proton 90° pulse, a 1.5-ms contact pulse, and a 3.0-s delay between repetitions.
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