NMR spectrum of compound was obtained on a Bruker (500 MHz) NMR (Bruker, Switzerland) at a constant temperature, controlled and adjusted to room temperature. The chemical shifts were shown in δ values (ppm) with tetra-methylsilane as an internal standard. The deuterated chloroform was used as the solvent for recording of 1H and 13C NMR spectra.
500 mhz nmr
Manufactured by Bruker
Sourced in United States, Germany
The 500 MHz NMR is a nuclear magnetic resonance spectrometer that operates at a frequency of 500 MHz. It is designed to analyze the molecular structure and properties of chemical compounds by detecting the magnetic properties of their atomic nuclei.
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Lab products found in correlation
Escalab 250, by Thermo Fisher Scientific (3 mentions)
Refractive index detector, by Waters Corporation (2 mentions)
Cary 300, by PerkinElmer (1 mentions)
Tlc silica gel 60 f254, by Merck Group (1 mentions)
Microtof, by Bruker (1 mentions)
Jem arm200cf, by JEOL (1 mentions)
V 770, by Jasco (1 mentions)
Vertex 70, by Bruker (1 mentions)
Amix software, by Bruker (1 mentions)
Spss statistics 20, by IBM (1 mentions)
D8 advance, by Bruker (1 mentions)
Ft ir 6600 spectrometer, by Jasco (1 mentions)
Silica gel 60 f254, by Merck Group (1 mentions)
Kieselgel 60 f254, by Merck Group (1 mentions)
Quantamaster 40 spectrofluorometer, by Horiba (1 mentions)
600 mhz nmr instrument, by Bruker (1 mentions)
Siliaflash f60, by Silicycle (1 mentions)
Acquity lc, by Waters Corporation (1 mentions)
Spectramax m3, by Molecular Devices (1 mentions)
Sds page, by Bio-Rad (1 mentions)
28 protocols using 500 mhz nmr
1
NMR Spectroscopy of Organic Compound
2
Spectroscopic Characterization of Organic Compounds
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The 1H- and 13C-NMR data were collected on a Bruker 500 MHz NMR (Bruker Ltd., Rheinstetten, Germany) in CDCl3, DMSO-d6, and acetone-d6 as solvents at room temperature, with tetramethylsilane (TMS) as an internal reference. High-resolution mass spectra (HRMS) were recorded by an electrospray ionization mass (ESI-MS) spectrometer (MicrOTOF, Bruker, Rheinstetten, Germany). The absorbance and fluorescence spectra were measured on a UV–Vis spectrophotometer (Agilent Technologies Cary 300, CA, USA) and a fluorescence spectrophotometer (PerkinElmer LS55, MA, USA), respectively. All glassware was oven-dried prior to use. All reagents and solvents were purchased from the companies Sigma Aldrich and Merck (MO, USA), TCI (Tokyo, Japan), or Carlo Erba (Barcelona, Spain)and used without further purification. Analytical thin-layer chromatography (TLC) was performed on TLC Silica gel 60 F254 (Merck, MO, USA) and visualized under a UV cabinet lamp.
3
Equilibrium Constant Determination via NMR
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Cyclobutanone 3y was massed to 2–3 mg and the exact mass was recorded. Compound 3y was then dissolved in the appropriate amount of deuterated solvent (DMSO-d6 or CDCl3) and vortexed. The appropriate amount of deuterium oxide (0%, 2%, 10%, 20%, or 30%) was added to the sample and the sample was vortexed. The sample was inserted into the Bruker 500 MHz NMR and data were collected for 64 scans. The raw data were analyzed with the Mnova NMR program, and the Keq was calculated via the method described by the Wiberg group [32 (link),40 ].
4
1'S-1'-Acetoxychavicol Acetate NMR Analysis
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10 mg of dried 1′S-1′-Acetoxychavicol acetate was exchanged in a Chloroform-D1 0.03 col.% TMS. One-dimensional NMR spectroscopy (1H NMR and 13C NMR) and two-dimensional NMR (COSY, HMBC, and HMQC) were performed using a Bruker 500 MHz NMR (Bruker, Yokohama, Japan).
5
Comprehensive Characterization of Novel Materials
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Nuclear magnetic resonance (NMR) spectra were recorded by 500 MHz NMR (Bruker). SEM images were obtained by JEOL 7500F FESEM. The HRTEM images were obtained using JEM‐ARM200CF, JEOL system with an accelerating voltage of 200 kV. Raman and Photoluminescence measurements were obtained using an NTE‐GRA spectra instrument (NT‐MDT) equipped with a 532 nm laser at room temperature. For FTIR, a Vertex 70 (Bruker) instrument was used in transmission mode. The absorption measurement was measured by UV−vis/NIR spectrometer (Jasco, V770). XPS measurement is conducted by Thermo VG Microtech ESCA 2000 with a monochromatic Al‐Kα X‐ray source at 100 W. The binding energy scale was calibrated by referencing C 1s to 284.5 eV. UPS was performed under high vacuum conditions by ESCALAB250 (Thermo‐Scientific, U.K.) instrument. AFM measurements were carried out using DFM mode of AFM SPA400, SEIKO system.
6
Thiol-Functionalized Hyaluronic Acid Synthesis
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Thiol groups were introduced into HA by standard EDC chemistry. Briefly, EDC (380 mg) and 1-hydroxybenzotriazole (284 mg) were added to a solution of HA (500 mg) in 50 mL DDW (final concentration = 10 mg/mL). After 30 min, cysteamine hydrochloride (284 mg) was added to the reaction solution. The reaction was allowed to proceed for 12 h, and the pH was adjusted to about 6.5. The synthesized HA–SH was purified by dialysis (SpectraPor 3.5 kDa MWCO; Spectrum Laboratories) and lyophilized. The synthesis and chemical structures of HA–thiol were determined by 1H NMR spectroscopy (500 MHz NMR; Bruker), as previously reported [22 (link)].
7
Characterization of Crosslinked Polymeric Nanoparticles
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1H NMR was used to characterize the polymer structures and the degree of crosslinking. The polymers were dissolved in deuterated DMSO (DMSO-d6) and nanoparticles were first lyophilized and then dissolved in DMSO-d6 for characterization using a Bruker 500 MHz NMR and analyzed using TopSpin 3.6 software. To determine the degree of crosslinking, the acrylate peaks, which are used to form crosslinks upon exposure to UV in the presence of the photoinitiator Irg, were integrated and normalized to protons peaks in the PBAE backbone.
GPC was used to characterize the molecular weight of polymers relative to linear polystyrene standards using a refractive index detector (Waters, Milford, MA). To measure the molecular weight after crosslinking, nanoparticles were formed as described above, and then lyophilized to remove aqueous buffer. Prior to characterization, samples were dissolved in butylated hydroxytoluene-stabilized THF, filtered through a 0.2 μm polytetrafluoroethylene filter.
GPC was used to characterize the molecular weight of polymers relative to linear polystyrene standards using a refractive index detector (Waters, Milford, MA). To measure the molecular weight after crosslinking, nanoparticles were formed as described above, and then lyophilized to remove aqueous buffer. Prior to characterization, samples were dissolved in butylated hydroxytoluene-stabilized THF, filtered through a 0.2 μm polytetrafluoroethylene filter.
8
Metabolite Profiling of Freeze-Dried Cells
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Freeze-dried cells (25 mg) were extracted with a ratio 1:1 of CD3OD and KH2PO4 buffer. The latter was prepared in D2O, adjusted pH to 6.0, and added 0.01% (w/w) trimethylsilyl propanoic acid (TMSP) as internal standard. The mixture was vortexed for 10 s, sonicated for 10 min, and centrifuged for 15 min (14,000 rpm). Samples were analyzed using 500 MHz NMR (Bruker, Karlsruhe, Germany). NMR spectra were manually phased, baseline corrected, and calibrated to TMSP resonance at 0.0 ppm using XWIN NMR version 3.5 (Bruker). AMIX software (Bruker) was used for bucketing (width δ 0.04) and data reduction of the 1H-NMR spectra (δ 0.40–10.00) using total intensity scaling. Multivariate data analysis was performed with the SIMCA software version 12.0 (Umetrics, Umeå, Sweden). Analysis of variance (ANOVA) followed by Duncan’s Multiple Range Test (DMRT) was performed on IBM SPSS Statistics 20 (SPSS Inc., Chicago, IL, USA) to determine statistical differences (P < 0.05) between means of groups.
9
Heparin Binding Characterization of Proteins
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Heteronuclear single quantum coherence (HSQC) spectroscopy was performed on a Bruker 500 MHz NMR equipped with cryoprobe. The protein samples were isotopically labeled with 15N as a result of expression in M9 minimal media containing 15NH4Cl. All NMR experiments were acquired at 25 °C using a protein concentration of 300 μM using 2 K × 256 data points. Protein samples were prepared in 90% H2O 10% D2O solution containing 10 mM sodium phosphate buffer containing100 mM NaCl and 25 mM (NH4)2SO4 (pH 7.2). The total chemical shift perturbation per residue (Δδtotal) was calculated using the following equation: √ [ (2ΔδNH)2 + (ΔδN)2]. All NMR data was analyzed using Sparky 3.114 software [37] . 1H–15N chemical shift perturbation at the residue level, caused due to binding of heparin, were carefully tracked by acquiring a series of 1H–15N HSQC spectra at different heparin to protein ratio's. Despite our efforts, we could not unambiguously follow the 1H–15N chemical shift perturbation of few residues and these residues were not considered in the final 1H–15N chemical shift perturbation data presented.
10
NMR Analysis of Amyloid-Beta Peptide
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Uniformly 15N-labeled recombinantly expressed Aβ42 (rPeptide, GA, USA) was prepared following the manufacturer’s instructions and stored at −80 °C until use. Samples were prepared using 50 µM protein in the absence and presence of 50 µM trodusquemine (5 mM sodium phosphate, pH 7.5). While trodusquemine is highly soluble in water, its solubility in 5 mM sodium phosphate is limited above 50 µM. Eight scans were taken for each spectrum using a 500 MHz NMR (Bruker) at 5 °C, and the assignments were obtained from previous spectra69 (link).
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