The NMR was performed for acetylated samples dissolved in acetone-d6. Bruker Avance III 500 MHz NMR-spectrometer with Bruker 5 mm BBO probe was used for 1D (1H, 13C) and 2D (HSQC using hsqcetgp pulse sequence) experiments. The spectra were processed with Bruker TopSpin 4.0.5 software. Solvent signals (2.05/29.84 ppm) were used as reference and the signals were assigned based on literature (Ralph and Landucci, 2010 (link); Balakshin and Capanema, 2015 (link)).
Avance 3 500 mhz nmr
Manufactured by Bruker
Sourced in Switzerland
The Avance III 500 MHz NMR is a nuclear magnetic resonance spectrometer. It is designed to perform high-resolution NMR analysis of chemical samples. The core function of the Avance III 500 MHz NMR is to detect and measure the nuclear magnetic properties of atomic nuclei within a sample, providing detailed information about the chemical structure and composition of the substance under investigation.
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Lab products found in correlation
Topspin 4, by Bruker (1 mentions)
5 mm bbo probe, by Bruker (1 mentions)
Melting point apparatus, by Gallenkamp (1 mentions)
Nicolet 6700 spectrometer, by Thermo Fisher Scientific (1 mentions)
Cmt4204, by MTS Systems (1 mentions)
Mestrenova, by Mestrelab Research (1 mentions)
Topspin, by Bruker (1 mentions)
Avance 3 700 mhz, by Bruker (1 mentions)
9 protocols using avance 3 500 mhz nmr
1
Acetylated Sample NMR Analysis
2
Comprehensive NMR, MS, and FTIR Characterization
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The NMR spectra were recorded on a Bruker Avance III-500 MHz NMR. Chemical shifts are given in ppm downfield from Me4Si in DMSO-d6 solution. Coupling constants are given in Hz. MS spectra were performed on an AB Sciex 3200 QTRAP LC-MS/MS. The FTIR spectra were recorded on a Perkin-Elmer FT-IR spectrometer (ATR) and absorption frequencies are reported in cm−1. Elemental analyses were performed with CHNS-932 LECO apparatus and were in good agreement (± 0.2%) with the calculated values. Ultrasonication was performed in an Alex Ultrasonic Bath with a frequency of 32 kHz and a power of 230 W. Melting points were measured on a Gallenkamp melting-point apparatus. TLC was performed on standard conversion aluminum sheets pre-coated with a 0.2-mm layer of silica gel. All of the reagents were commercially available.
3
Comprehensive Characterization of Soy Protein Isolates
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The thermal gravimetric analysis (TGA) of SPIs were measured with Q50 (TA Instruments, NewCastle, DE, USA) at a heating rate of 10 °C min−1 under the protection of N2. The Fourier-transform infrared spectra (FTIR) of the SPIs were recorded using a Nicolet 6700 spectrometer (Thermo Scientific, Nicolet, Waltham, MA, USA). 1H NMR of the B3 and SPIs were recorded using a Bruker AVANCE III 500 MHz NMR instrument. The microstructure of the membranes of SPI-BFDA was tested by Field emission scanning electron microscopy (FESEM, S-3400N). The mechanical property of SPIs was measured with an electromechanical universal testing machine (CMT 4204, MTS systems, Jinan, China) at a stretch rate of 5 mm min−1 (the relative humidity was 85%). The SPIs test samples were cut into (15 mm × 4 mm) dumbbell samples.
4
NMR Spectroscopy of TtTF Proteins
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Both TtTF (EDTA) and TtTF (Zn2+) were concentrated to ~0.1 mM and prepared in a buffer containing 50 mM HEPES-KOH (pH 7.5) and 100 mM KCl. 1H-13C heteronuclear multiple quantum coherence (HMQC) spectra were recorded on Bruker Avance III 500 MHz NMR (Bruker Biospin AG, Fällanden, Switzerland) at 65 °C. The spectra were processed with the NMRPipe software [25 (link)]. Olivia software (https://github.com/yokochi47/Olivia , Accessed date: 22 December 2017) was used to analyze the spectral data.
5
NMR Characterization of Branched Polymers
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Solution-phase nuclear magnetic resonance (NMR) spectra were collected using a Bruker Avance III 500 MHz NMR spectrometer (11.7 T) at 120 °C in 1,1,2,2-tetrachloroethane-d2 and referenced internally to residual solvent signals. 1H NMR spectra (500 MHz) were recorded with 32 scans and 13C{1H} NMR spectra (125 MHz) with ∼9500 scans. Spectra were analyzed using MestReNova (v11.0.1, Mestrelab Research S.L.). The branching density was determined by 1H NMR spectroscopy according to: # branches per 1000 C = (CH3/3)/((CH + CH2 + CH3)/2) × 1000 where CH3, CH2, and CH refer to the integrations obtained for methyl, methylene, and methine resonances, respectively.
6
Determining Dodecane/β-CD Complex Ratio
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The lyophilized precipitates or vesicles were dissolved into DMSO for 1H NMR measurements to determine the actual ratio of dodecane to β-CD. The measurements were performed on an AVANCE III 500 M Hz NMR (Bruker, Switzerland). All the proton signals were calibrated with the TMS at 0.00 ppm. By comparing the integration between β-CD (H1 protons, δ = 4.83 ppm) and dodecane (CH3 protons, δ = 0.83 ppm), dodecance/β-CD complex ratio can be determined.
7
Multinuclear NMR Spectroscopy of Liquid Samples
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High-resolution spectra for 1H, 7Li, 11B, 13C, and 19F were recorded on a Bruker Avance III 500 MHz NMR spectrometer. The measurements at frequencies of 500, 194, 160, 126, and 471 MHz for 1H, 7Li, 11B, 13C, 17O, and 19F, respectively, were carried out at room temperature (22 ± 1 °C). Liquid samples in standard 5 mm NMR tubes without adding a deuterium solvent were placed. The chemical shift scale was calibrated with the DMSO-d6 signal in the capillary as an external standard (2.50 ppm for 1H). The 1H, 7Li, 11B, and 19FNMR spectra were obtained using the standard sequence π/2 pulses, FID. No signal accumulation was applied. To obtain the 13CNMR spectra, a standard sequence from the TopSpin (Bruker) zgpg30 library was used. The sequence is an accumulation of signals from 300 pulses with the suppression of the 1H spin-spin interaction for the duration of all the experimental times. The number of repetitions was ns = 512, and the delay between the repetition sequence was d1 = 1.5 s.
8
Multidimensional NMR Analysis of Compounds
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1H NMR spectra were recorded using a Varian Oxford 300 NMR instrument. 1H-decoupled 31P NMR spectra were recorded using a Bruker AVANCE III 700 MHz. 77Se spectra were recorded using a Bruker Avance III 500 MHz NMR instrument. Variable-temperature 31P NMR spectra were recorded using a Bruker Avance III HD 850 MHz Cryo-NMR instrument. 1H DOSY spectra were recorded using a Bruker Avance III 600 NMR instrument. CD2Cl2 was used as the solvent for variable-temperature 31P NMR spectroscopy and CDCl3 was used for the others. Solid-state 31P magic angle spin NMR spectra were recorded using an AVANCE III HD Solid 500 MHz NMR instrument. Resonance frequencies of 300.04, 850.22, 283.56, 202.46, and 95.38 MHz were used for 1H, 1H DOSY, 31P, solid-state 31P, and 77Se NMR spectral acquisitions, respectively. All samples were prepared in a glovebox, and the NMR spectra were measured within 3 h to prevent degradation or oxidation of the products.
9
NMR Analysis of Samples Using Bruker Spectrometer
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Analysis was performed with a Bruker BioSpin Avance III 500 MHz NMR equipped with a microprobe ( 1 H-13 C-15 N TXI) fitted with an actively shielded Z gradient. Analysis was performed using 256 scans, a relaxation delay of 3 seconds, 32k time domain points and a 90° pulse calibrated on a per sample basis. Water suppression was accomplished by using the Presaturation Using Relaxation Gradients and Echoes program (Brown et al., 2008; (link)Simpson and Brown, 2005) (link). Spectra were apodized through multiplication with an exponential decay corresponding to 0.3 Hz line broadening in the transformed spectra, with a zero filling factor of 2 (Lankadurai et al., 2011; Nagato et al., 2013; (link)Nagato et al., 2015) (link). Acquired spectra were manually phased, baseline corrected and aligned to the trimethyl-silyl group of the DSS internal calibrant and set at δ = 0.00 ppm. Prior to any 1 H NMR analysis, both the D 2 O used and the D 2 O-based phosphate buffer were analyzed to check for impurities.
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