1H NMR (Bruker AVIII-600 MHz) was used to verify the addition of vinyl groups from the methacrylation reaction. Lyophilized GelMA polymer was dissolved in deuterium oxide (−) at a concentration of 10 mg/mL, and samples were run at 40 °C. Data was analyzed using Bruker TopSpin3.5 software.
Aviii 600 mhz
Manufactured by Bruker
Sourced in Germany
The AVIII-600 MHz is a high-performance NMR spectrometer produced by Bruker. It is designed to provide efficient and accurate nuclear magnetic resonance analysis capabilities for research and industrial applications.
Automatically generated - may contain errors
Lab products found in correlation
Topspin 3, by Bruker (2 mentions)
Aviii 500 mhz, by Bruker (2 mentions)
Aviii 700 mhz, by Bruker (2 mentions)
Topspin2 1 topspin3, by Bruker (1 mentions)
Topspin 3 x, by Bruker (1 mentions)
Cpqci cryoprobe, by Bruker (1 mentions)
Chemdoc xrs, by Bio-Rad (1 mentions)
Synergy h1 multi mode reader, by Agilent Technologies (1 mentions)
Uv 2550 uv vis spectrophotometer, by Shimadzu (1 mentions)
Cary eclipse fluorescence spectrophotometer, by Agilent Technologies (1 mentions)
9 protocols using aviii 600 mhz
1
1H NMR Characterization of GelMA
2
CPEB4 RRM1-RRM2 Binding Assay
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Experiments were recorded at 303 K using a Bruker AVIII 600 MHz spectrometer equipped with a 5 mm TXI cryprobe, z-gradient. Protein samples of the CPEB4 RRM1 and the CPEB4 RRM1–RRM2 were equilibrated in a buffer containing 20 mM Tris-d11, 130 mM NaCl and 5% DMSO-d6. All samples were supplemented with 10% D2O and pH adjusted to value 7. Spectra were acquired using 200 μM 15N-labeled protein samples equilibrated together with progressively increasing amounts of the unlabeled RNA fragments until saturation was achieved. Chemical shift perturbation analyses were performed on CcpNmr Analysis (22 (link)) with a 0.15 weighting of 15N with respect to 1H.
3
NMR Spectroscopy of TDP-43 NTD Backbone
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The following NMR spectrometers were used for measuring the NMR experiments in this study—Bruker AVIII-500 MHz, AVIII-600 MHz, AVIII-700 MHz, and Avance-900 MHz that were equipped with cryoprobes. TopSpin2.1/TopSpin3.0 (Bruker) was used to perform data processing while the analysis was done in Sparky (http://www.cgl.ucsf.edu/home/sparky ). For TDP-43 NTD backbone assignments, the following NMR experiments were measured (in H2O)—two-dimensional (2D) 15N–1H HSQC, 2D 13C–1H HSQC, three-dimensional (3D) HNCA, 3D HNCOCA, 3D CACBCONH, 3D HCcH TOCSY, 3D hCCH TOCSY, 3D 15N-, and 13C-edited Nuclear Overhauser SpectroscopY (NOESYs).
4
NMR Analysis of Separated Peaks
5
NMR Spectroscopy of Biomolecular Complexes
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All NMR spectroscopy measurements were done in 20 mM Na2HPO4 (pH 7), 100 mM NaCl, 1 mM DTT, 10% D2O at 298 K using Bruker AVIII-500 MHz, AVIII-600 MHz (equipped with cryoprobes), and AVIII-750 MHz. NMR data were processed with TopSpin 3.1 (Bruker), and the analysis was performed using SPARKY 3 (T. D. Goddard and D. G. Kneller, University of California, San Francisco). For more details, see SI Appendix .
6
NMR Analysis of Pt-tripod-Tel26 Complexes
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All NMR experiments were performed on the Bruker AVIII 600 MHz and AVIII 700 MHz (equipped with a cryprobe) spectrometers. 25 mM K-phosphate and 70 mM KCl buffer (pH 7.0) in D2O/H2O (10%/90%) or D2O (99.8%) were used to prepare DNA samples. The final concentrations of DNA samples were 0.1–2.5 mM. The 1H-15N HMQC experiments were used to assign the hydrogen bonding thymine imino protons. 2D NMR experiments, including COSY, TOCSY and NOESY, were collected at different temperatures of 5, 15, and 25 °C in H2O and D2O solution for the 1:1 and 4:2 Pt-tripod‒Tel26 complexes. The mixing times of NOESY were set from 50‒300 ms, and TOCSY at 40 ms. WATERGATE or presaturation water suppression techniques were used for water NMR samples. Peak assignments and integrations were made using Sparky (UCSF).
7
NMR Characterization of Selectively Labeled Proteins
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Experiments were measured on Bruker AVIII-600 MHz with CPQCI cryoprobe, and consisted of repeating series of 1D 1H-watergate (spectral width (SW) 22 ppm; acquisition time (AQ) 0.62 s; D1 (interscan delay) 1 s; number of scans (NS) 128), 2D 1H-TOCSY (SW 10 / 9 ppm; AQ 0.17 / 0.018 s; D1 0.5 s; NS 4), 1D 31P (SW 50 ppm; AQ 0.66 s; NS 256; carrier –8.22 ppm; D1 0.8 s), 1D 1H-SOFAST (SW 24 ppm; AQ 0.053 s; D1 0.1 s; NS 1536; 1H excitation with Pc9 pulse, 5 ppm wide, centered at 12.9 ppm) and 2D 1H15N-SOFAST-HMQC (H/N: SW 16 / 23.5 ppm; AQ 0.106 / 0.035 s; D1 0.2 s; NS 24; 15N carrier 117.8; 1H excitation with Pc9 pulse, 4 ppm wide, centered at 7.95 ppm). BEST-TROSY 2D HN(CO) for analysis of selectively labeled proteins was provided by Frank Lohr (BMRZ, Goethe Universitat Frankfurt) and measured with (H/N: SW 12 / 16 ppm; AQ 0.107 / 0.090 s; D1 0.2 s; NS 16; 15N carrier 117.8; 1H excitation with Pc9 pulse, 4.2 ppm wide, centered at 8.5 ppm). NMR spectra were sorted, processed and analyzed using TopSpin 3.x (Bruker), custom-built Python and MATLAB scripts and the rbnmr routine (Nyberg N., RBNMR, MATLAB Central File Exchange #40332, (2013)). Chemical shifts of protein residues in 2D HN spectra were traced in CARA (cara.nmr.ch ).
8
Characterization of BSA-Au Nanoclusters
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PAGE was performed on a DYY-6C electrophoresis analyzer (Liuyi Instrument Company, China) and imaged on a Bio-rad ChemDoc XRS (Bio-Rad, USA). The fluorescence kinetics were collected on the Synergy H1 Multi-Mode Reader (BioTek, USA). Ultraviolet-visible (UV-Vis) spectra of BSA-Au NCs was obtained with a UV-2550 UV-Vis spectrophotometer (Shimadzu, Japan). Fluorescence spectra of BSA-Au NCs was recorded using a Cary Eclipse fluorescence spectrophotometer (Agilent Technologies, USA). BSA-Au NCs in aqueous solution and mixed in polyacrylamide gel were identified by high-resolution transmission electron microscopy (HRTEM; FEI Tecnai G2 F20 S-Twin, USA). 1H NMR spectra was recorded using a Bruker AVIII 600 MHz (Germany) at 25 °C.
9
Polymer Characterization via NMR and GPC
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The spectra of nuclear magnetic resonance (1H NMR) were performed on a Bruker AVIII 600 MHz (Bruker, Karlsruhe, Germany). Number-average molecular weight (Mn), weight-average molecular weight (Mw), polydispersity (PDI), and (η) were determined by gel permeation chromatography (GPC) (Malvern Instruments Ltd., Malvern, PA, USA) which was equipped with RI detector, two-angle light scattering detector and viscosity detector. The system was calibrated with polyethylene oxide std-PEO22K and eluted with 0.1 M NaNO3 solution with a flow rate of 1 mL·min−1 at 30 °C. The calibration was performed at 30 °C and a flow rate of 1 mL·min−1. The samples were dissolved in 0.1 M NaNO3 solution and passed through 0.2 μm filter before measurement.
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