An Avance 700 MHz NMR spectrometer (Bruker Inc., USA) equipped with a cryogenic probe was used to record 2D 1 H-15 N-HSQC spectra at +20 °C of 92.4 μM monomeric 15 N-labeled Aβ40 peptides (500 μl), either in only 20 mM sodium phosphate buffer at pH 7.35 (90/10 H2O/D2O), or in phosphate buffer together with 50 mM SDS (sodium dodecyl sulphate) detergent. As the critical micelle concentration (CMC) for SDS is around 8 mM (Österlund et al., 2018b) , most of the SDS was present as micelles. Both samples were titrated, first with additions of pure DMSO, and then by 6-gingerol dissolved in DMSO. The NMR data was processed with the Topspin version 3.6.2 software, and the Aβ40 HSQC crosspeak assignment in buffer (Danielsson et al., 2006) and in SDS micelles (Jarvet et al., 2007) is known from previous work.
Avance 700 mhz nmr spectrometer
Manufactured by Bruker
Sourced in United States
The Avance 700 MHz NMR spectrometer is a high-resolution nuclear magnetic resonance (NMR) instrument designed for advanced chemical analysis. It operates at a frequency of 700 MHz, providing high-quality spectroscopic data for the identification and structural elucidation of organic and inorganic compounds.
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Lab products found in correlation
Maxis q tof mass spectrometer, by Bruker (1 mentions)
Gel ods a, by YMC (1 mentions)
Chirascan circular dichroism spectrometer, by Applied Photophysics (1 mentions)
Pack ods a, by YMC (1 mentions)
Ods series column, by YMC (1 mentions)
Gf254, by Qingdao Marine Chemical (1 mentions)
Accutrend plus, by Roche (1 mentions)
9 protocols using avance 700 mhz nmr spectrometer
1
NMR Spectroscopy of Amyloid-beta Peptides
2
Comprehensive Spectroscopic Analysis of Compounds
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One-dimensional and two-dimensional (2D) nuclear magnetic resonance (NMR) spectra were measured on a Bruker Avance 700 MHz NMR spectrometer (Fällanden, Switzerland) with Tetramethylsilane as an internal standard. High-resolution electrospray ionization mass spectrometry (HRESIMS) data were recorded on a maXis Q-TOF mass spectrometer in positive ion mode (Bruker, Fällanden, Switzerland). Electronic circular dichroism (ECD) and ultraviolet (UV) spectra were measured with a Chirascan circular dichroism spectrometer (Applied Photophysics). Optical rotations were measured using an MCP-500 polarimeter (Anton, Austria). High-performance liquid chromatography (HPLC) was performed on Hitachi Primaide with YMC ODS SERIES column (YMC-Pack ODS-A, YMC Co. Ltd., Kyoto, 250 × 10 mm I.D., S-5 μm, 12 nm). Column chromatography was carried out on silica gel (200–300 mesh, Jiangyou Silica Gel Development Co., Yantai, China), YMC Gel ODS-A (12 nm, S-50 μm YMC, MA, United States), and Sephadex LH-20 (40–70 μm, Amersham Pharmacia Biotech AB, Uppsala, Sweden). Spots were detected under UV light by heating after spraying with the mixed solvent of saturated vanillin and 5% sulfuric acid in water. The thin layer chromatography plates with silica gel GF254 (0.4–0.5 mm, Qingdao Marine Chemical Factory, Qingdao, China) were used for analysis and preparation.
3
NMR Analysis of α-Synuclein-S100A9 Interaction
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A Bruker Avance 700 MHz NMR spectrometer equipped with a triple-resonance cryoprobe was used to perform NMR measurements. 2D 1H,15N heteronuclear single quantum coherence (HSQC) spectra of 77 μM isotope-labeled α-syn in 10 mM phosphate buffer, pH 7.35, and 10 °C were recorded before and after addition of 2.5 mM S100A9. The spectra were referenced to the water signal, and the assignment of α-syn amide cross-peaks was used from previous work [36 (link)].
4
NMR Characterization of PKG Iβ Conformations
5
NMR-Based Metabolite Profiling Protocol
6
NMR Spectroscopy of PKG Iβ 92-227
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The PKG Iβ 92–227 construct was expressed with an N-terminal His tag, in BL21(DE3) E. coli cells grown at 37°C in 15N M9 media. Expression was induced with 0.5 mM IPTG at an OD600 of 0.8, and the cells were grown for 16 hr at 18°C. PKG Iβ 92–227 was purified as reported (VanSchouwen et al., 2015b (link)). NMR samples were prepared in 50 mM Tris, pH 7.0, 100 mM NaCl, 1 mM 1,4-dithiothreitol (DTT), 0.2% (wt/vol) NaN3. An apo sample was prepared by concentrating the purified PKG to 100 μM, and adding 5% (vol/vol) D2O, phosphodiesterase (PDE), 1 mM ATP, and 10 mM MgCl2. A cGMP-bound sample was prepared similarly, with the addition of 1 mM cGMP to the apo protein solution. All HSQC spectra were recorded with 16 scans and 1-s recycle delay. The spectra included 128 (t1) and 2048 (t2) complex points with spectral widths of 38.0 and 16.2 ppm for the 15N and 1H dimensions, respectively. Carrier frequencies of 1H and 15N were set at the water and central amide region, respectively. All spectra were acquired at 300 K with a Bruker Avance 700 MHz NMR spectrometer equipped with a 5 mm TCI cryoprobe. The spectra were processed with TOPSPIN and analyzed using Sparky (Lee et al., 2015 (link)).
7
High-Resolution 1H NMR Spectroscopy
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1H NMR spectra were performed on a Bruker avance 700 MHz NMR spectrometer equipped with a triple resonance 5 mm PATXI 1H-13C/15N/D Z-GRD probe (Bruker, Billerica, MA, USA). The samples were dissolved in D2O, and the NMR spectra were recorded at 30 °C. The free induction decay acquisition time was 2.9 s, the number of time points was 65,536, the spectrum sweep width was 15.9 ppm, and the number of scans was8. The residual HOD water signal was not suppressed to avoid distortion of the integral values. 1H chemical shifts were calibrated relative to the HOD chemical shift (4.7 ppm).
8
Metabolomic Analysis of Blood Samples
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For the analysis of lactate and glucose concentrations, blood samples were taken from the facial vein [90 (link)] and analyzed by a portable biochemical analyzer Accutrend Plus (Roche Diagnostics, Basel, Switzerland). For complete NMR analysis of metabolome, blood was collected by cardiac puncture [91 (link)] from animals anesthetized by isoflurane inhalation. Plasma was separated by centrifugation and used immediately for metabolite extraction by methanol and chloroform 1:1 mixture. Water layer was removed and dried. Before NMR measurements, the solid metabolites were dissolved in 50 mM sodium phosphate at pH 7.0, 0.107 mM d6-DSS, 0.13 mg/mL NaN3 in D2O. NMR spectra were acquired at 35 °C on a Bruker Avance 700 MHz NMR spectrometer equipped with a Z-axis-gradient 5 mm HCN Prodigy cryoprobe. One-dimensional 1H NMR spectra were acquired from each sample using the standard 1D NOESY-presat experiment. A total of 400 scans were accumulated for plasma samples. 1H,13C-HSQC spectra were measured for one sample from each group to confirm the metabolites assignments. All steps of 1D spectra processing and metabolite identification were performed using Chenomx NMR Suite program. 1H,13C-HSQC spectra were analysed in TopSpin program.
9
NMR Characterization of Peptides with Unnatural Amino Acids
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Samples of peptides containing γ-carboxyglutamic acid and carboxymethyl lysine as residue ‘X’ were prepared as above and the pH was adjusted to pH 2.0 with HCl. NMR spectra were acquired at the Centre for Advanced Imaging (The University of Queensland) on an Avance 700 MHz NMR spectrometer (Bruker BioSpin, Germany) with a cryoprobe. At pH 2.0 and at pH 9.0, 1H, 1H–1H TOCSY, 1H–15N HSQC, 1H–13C HSQC and 1H–13C HMBC spectra were acquired to enable assignment of the 1H, 15N and 13C resonances at the extreme pH values. The pH was then increased in ~ 0.5 steps using 0.1 M HCl and 0.1 M NaOH and 1H and 1H–1H TOCSY spectra were acquired at each step to provide 1H chemical shifts. Spectra were processed, referenced and assigned as above.
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