Two hundred or 400 µM POM-HEX was incubated with 4 nmol GloB, FrmB, or 4 nmol each GloB and FrmB in 500 µL reactions. Reactions were buffered to a final concentration of 50 mM Tris pH 7.5, 50 mM NaCl, 1 mM MgCl2. Reactions were allowed to proceed for 1 hr at 37°C prior to analysis. Samples were prepared for NMR studies by resuspending them in water and 10% (50 µL) D2O (deuterium oxide 99.9% D, contains 0.75 wt% 3-(trimethylsilyl)propionic-2,2,3,3-d4 acid, sodium salt, Sigma–Aldrich). NMR spectra are acquired on a Bruker Avance III HD 500 MHz spectrometer equipped with a cryoprobe. Two-dimensional (2D) 1H-31P HSQC measurements were obtained using hsqcetgp pulse program (with duration of 15 min and scan parameters of two scans, td = 1024 and 256, gpz2 % = 32.40, 31P SW = 40 ppm, O2p = 20 ppm, cnst2 = 22.95) and analyzed using 3.1 TopSpin. The 1D projection of columns excluding the water signal was obtained from the 2D 1H-31P HSQC spectrum by obtaining spectra of positive projection of columns 1–600 and 650–1024 and adding them.
Avance 3 hd 500 mhz
Manufactured by Bruker
Sourced in United States, Germany, Switzerland
The Avance III HD 500 MHz is a high-performance nuclear magnetic resonance (NMR) spectrometer designed and manufactured by Bruker. It operates at a magnetic field strength of 500 MHz and is capable of providing high-resolution NMR analysis of various chemical and biological samples.
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Lab products found in correlation
5 mm inverse probe txi 1h 13c 15n, by Bruker (2 mentions)
Avance 3 hd 300 mhz, by Bruker (2 mentions)
Adiabatic hsqc pulse sequence hsqcetgpsisp2.2, by Bruker (1 mentions)
Spectrum one fourier transform infrared, by PerkinElmer (1 mentions)
Cryoprobe, by Bruker (1 mentions)
Avance neo 600 mhz, by Bruker (1 mentions)
Sephadex lh 20, by Merck Group (1 mentions)
394 dna synthesizer, by Thermo Fisher Scientific (1 mentions)
Micro qtof, by Bruker (1 mentions)
Astra 6, by Wyatt Technology (1 mentions)
Eclipse plus c18, by Agilent Technologies (1 mentions)
Optilab t rex refractive index detector, by Wyatt Technology (1 mentions)
Deuterium oxide, by Merck Group (1 mentions)
Mestrenova 12, by Mestrelab Research (1 mentions)
Genesis xm2, by Ametek (1 mentions)
Optima 7000dv, by PerkinElmer (1 mentions)
Nicolet is10 spectrophotometer, by Thermo Fisher Scientific (1 mentions)
B acs 120, by Bruker (1 mentions)
Dmso d6, by Eurisotop (1 mentions)
Avance 3 600 mhz, by Bruker (1 mentions)
42 protocols using avance 3 hd 500 mhz
1
NMR Analysis of Phosphorylated Compound Reactions
2
Lignin Characterization by 2D HSQC NMR
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The 2D-1H-13C heteronuclear single-quantum coherence (HSQC) NMR spectra were obtained using a Bruker Avance III HD 500 MHz spectrometer operating at a frequency of 125.12 MHz for the 13C nucleus as described by Ji et al. (2021) [32 (link)]. Thirty to fifty milligrams of the dry lignin samples were dissolved in 0.6 mL deuterated dimethylsulfoxide (DMSO)-d6 and the spectra were collected at 298 K. A standard Bruker adiabatic HSQC pulse sequence (hsqcetgpsisp2.2) was used with the following spectra acquisition condition: 1.0 s pulse delay, 64 scans, 1024 data points for 1H, 256 increments for 13C, and a 1JC–H of 145 Hz. The 1H and 13C spectral widths are 13.0 and 220.0 ppm, respectively. The central DMSO solvent peak (δ13C/δ1H = 39.5/2.49 ppm) was used for chemical shifts calibration. HSQC spectra were processed and analyzed with Mestrenova (version 12.0.2) with a matched cosinebell apodization and 2 × zero filling in both dimensions.
3
Isolation and Characterization of Chemical Compounds
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The chemical reagents were
procured from CDH, Sigma-Aldrich, and Loba, India. All yields refer
to isolated products after purification. Products were characterized
by comparing with authentic samples and by spectroscopic techniques,
that is, 1H and 13C NMR, elemental analysis.
AVANCE III HD 500 MHz Bruker Biospin and JEOL AL 300 MHz machines
were used to record the NMR spectra. The spectra were recorded by
dissolving in CDCl3 and DMSO-d6 relative to tetramethylsilane (TMS) (0.00 ppm). In 1H
NMR, chemical shifts were reported in δ values using the internal
standard (TMS) with a number of protons, multiplicities (s-singlet,
d-doublet, t-triplet, q-quartet, and m-multiplet), and coupling constants
(J) in hertz (Hz). Melting points were determined
in open capillaries and were uncorrected.
procured from CDH, Sigma-Aldrich, and Loba, India. All yields refer
to isolated products after purification. Products were characterized
by comparing with authentic samples and by spectroscopic techniques,
that is, 1H and 13C NMR, elemental analysis.
AVANCE III HD 500 MHz Bruker Biospin and JEOL AL 300 MHz machines
were used to record the NMR spectra. The spectra were recorded by
dissolving in CDCl3 and DMSO-d6 relative to tetramethylsilane (TMS) (0.00 ppm). In 1H
NMR, chemical shifts were reported in δ values using the internal
standard (TMS) with a number of protons, multiplicities (s-singlet,
d-doublet, t-triplet, q-quartet, and m-multiplet), and coupling constants
(J) in hertz (Hz). Melting points were determined
in open capillaries and were uncorrected.
4
NMR Spectroscopy of Lignin Media
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Nuclear magnetic resonance (NMR) spectra of lignin media were acquired at 298 K on an AVANCE III HD 500 MHz instrument (Bruker, Switzerland). The sample (80 mg) was dissolved in 0.5 ml of DMSO-d6 (99.8%). The parameters were as follows: pulse angle (30°), pulse width (9.2 μs), delay time (1.00 s), and acquired time (3.28 s).
5
Miniaturized 1H NMR Serum Analysis
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Due to limited volume of serum, 1H NMR analysis was done using an established miniaturized method [16 (link)] that requires only 100 μL serum samples. The method used is described in detail by van Zyl et al. (2020) [17 (link)]. Briefly, all samples were filtered using Amicon Ultra-2 mL 10 000 MWCO centrifugal filters at 4500 g for 20 min – physical removal of all macromolecules, especially proteins. A digital syringe (eVol®) was used to pipette a 90%:10% ratio of sample:NMR buffer solution (pH 7.4) into a 2 mm glass NMR tube. The NMR buffer solution contained the internal standard (trimethylsilylpropionic acid [TSP]), with 1.5 M sodium phosphate and 1% sodium azide in deuterium oxide. The settings for the NMR (Bruker Avance III HD 500 MHz) analysis were identical to those of van Zyl et al. (2020) [17 (link)].
6
NMR Analysis of Candida Mannan Binding
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Reaction buffer 10× (1×, 20 mm sodium phosphate buffer, pH 7.5, containing 100 mm NaCl) and C. albicans mannan were freeze dried and resuspended in D2O twice prior to the experiment. BT3870 was transferred to reaction buffer in D2O by extensive buffer exchange. Initial spectra were recorded of 900 μl of 10 mg ml−1C. albicans mannan in reaction buffer before initiating the reaction by the addition of 100 μl of BT3780 (final concentration, 30 μm ). 1H NMR spectra were recorded in D2O on a Bruker Avance III HD 500 MHz NMR spectrometer operating at 500.15 MHz at regular intervals. The chemical shift is quoted in ppm relative to tetramethylsilane, and each spectrum was acquired with 16 scans. Spectra of mannose and mannose-1-phosphate (2.5 mm in reaction buffer) standards were also recorded.
7
Characterization of Brominated PPO Membranes
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The 1HNMR spectrum of BrPPO was obtained on a Bruker, Avance III HD 500 MHz using deuterated trichloromethane (CDCl3) as a solvent to determine the bromination degree of PPO. A Perkin Elmer, Spectrum One Fourier-transform infrared (FTIR) spectrometer in the frequency range of 4000 to 600 cm−1 was carried out to study the chemical changes in the molecular structure during various synthesis stages. Thermogravimetric analysis was performed using SDT-Q600 TGA instrument in the temperature range of 30 to 600 °C at a heating rate of 10 °C min−1 to evaluate the thermal stability of the samples.
To measure water/electrolyte uptake capacity of the membranes, they were soaked in water/KOH, 7 M solution for 24 h and the weight differences before and after soaking were used for the measurements using Equation 1 [8 (link)].
where Wwet and Wdry are the weights of the membranes after and before soaking in water/electrolyte, respectively. Similarly, dimensional changes of the membranes induced by water/electrolyte uptake were calculated by Equations 2 and 3 [8 (link)].
To measure water/electrolyte uptake capacity of the membranes, they were soaked in water/KOH, 7 M solution for 24 h and the weight differences before and after soaking were used for the measurements using Equation 1 [8 (link)].
where Wwet and Wdry are the weights of the membranes after and before soaking in water/electrolyte, respectively. Similarly, dimensional changes of the membranes induced by water/electrolyte uptake were calculated by Equations 2 and 3 [8 (link)].
8
31P NMR Analysis of Lyophilized Soil Samples
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Preparation of lyophilized material for solution 31 P NMR analysis has been described by Reusser et al. (2020) . Solution 31 P NMR spectroscopy was carried out on one replicate of each treatment using a Bruker Avance III HD 500 MHz NMR spectrometer equipped with a 5 mm liquid-state Prodigy CryoProbe (Bruker Corporation, Billerica, MA, USA) at the NMR facility of the Laboratory of Inorganic Chemistry (H önggerberg, ETH Z ürich). Solution 31 P NMR spectra were acquired at a 31 P frequency of 202.5 MHz and gated broadband proton decoupling with 90 • pulses of 12 μs duration. Spectral resolution was <0.1 Hz following sample shimming across all samples. Two NMR analyses were carried out on all soil samples. The first was an inversion recovery experiment (Vold et al. 1968 ) to obtain the spin-lattice relaxation (T 1 ) times of the 31 P NMR signal. The longest T 1 time for each soil sample was multiplied 5-fold and used as the recycle delay of the subsequent 31 P (1D) NMR analysis. Spin-lattice relaxation times were the longest for orthophosphate across all soil samples, which ranged from 17 to 29 s. The average number of scans across all soil samples was 3754.
9
NMR Spectroscopic Analysis of Cyclodextrins
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The 1H NMR spectra were recorded at 298K on a Bruker AVANCE III HD 500 MHz spectrometer equipped with Bruker 5 mm inverse probe TXI (1H/13C/15N) with z-gradient coil probe. Solution of TSPd4 in D2O was used as internal reference for chemical shifts. To eliminate possible interactions between TSPd4 and the host molecule, the internal reference was introduced into a coaxial insert itself placed in the NMR tube. For all samples, a one dimensional 1H NMR spectrum was acquired using a ZGPRESAT sequence with water pre-saturation at low power. A total of 8 or 16 scans were collected with a 90 °C impulsion time of 10.2 µs, a 30 s relaxation time, an acquisition of 4.09 s, a spectral window of 8000 Hz and 65 K data points zero-filled to 128 K before Fourier transformation with 0.3 Hz line broadening. In addition, the determination of the average molar mass of the two CDs was estimated by an assay with an internal reference (TSP-d4).
10
Characterization of Chemical Compounds
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The 1H, 13C, HSQC, and HMBC NMR spectra were obtained using the Bruker AVANCE III HD 500 MHz and Bruker AVANCE NEO 600 MHz spectrometers (Bruker, Billerica, MA, USA); the chemical shift (δ) was expressed in ppm using TMS as an internal standard. The ESI-MS spectra were obtained using an Agilent 1260 series single quadrupole LC/MS system (Agilent, Santa Clara, CA, USA). Column chromatography (CC) was carried out on silica gel (Merck, Damstadt, Germany 40–63 μm) or Sephadex® LH-20 (Sigma, Uppsala, Sweden). Analytical thin-layer chromatography was conducted on TLC aluminum sheet silica gel 60 F254 (Merck, Damstadt, Germany). The compounds were detected using a UV lamp (254 and 365 nm) or by spraying with 10% sulfuric acid in water and heating.
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