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Unity inova spectrometer

Manufactured by Agilent Technologies
Sourced in United States

The Unity Inova spectrometer is a laboratory instrument designed for nuclear magnetic resonance (NMR) spectroscopy. It is used to analyze the structure and properties of chemical compounds by detecting the interactions between the magnetic moments of atomic nuclei and an applied magnetic field.

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30 protocols using unity inova spectrometer

1

PISA Sample Preparation for NMR

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50 uL of PET-RAFT PISA solution was transferred from the reaction cuvette to an Eppendorf tube with 550 uL of methanol-d4 within it. The mixture was vortexed for 5 min and then transferred to an NMR tube. The 1H-NMR spectra of the PISA sample was then measured at 25 °C on a 500 MHz Varian Unity/Inova spectrometer.
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2

Polymer Degradation in Artificial Bodily Fluid

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Degradation of the polymer was examined by 1H NMR spectroscopy. Polymer samples were placed in Falcon tubes and immersed in 5 ml of artificial body fluid solution (0.7 g/dm3 NaCl, 0.5 g/dm3 KCl, 0.26 g/dm3 Na2HPO4, 1.3 g/dm3 NaHCO3, 0.33 g/dm3 KSCN, and 0.13 g/dm3 urea – Across. Poland). Then, they were placed in an incubator at 37 °C and shaken at 60 rpm. The samples were removed at weekly intervals over a period of 28 days. The solution was lyophilized and analyzed by 1H NMR at 25 °C using a CDCl3 solvent. 1H NMR spectra were recorded with a UNITY-INOVA spectrometer (Varian 300 MHz). The internal standard used was tetramethylsilane (TMS).
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3

NMR Spectroscopy of Hydrophilic Cell Extracts

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All one-dimensional 1H-NMR spectra were acquired at 300 K on a Bruker Avance III 600 MHz ultrashielded spectrometer (Bruker Biospin Gmbh, Rheinstetten, Germany) operating at 600.13 MHz for protons (14.09 Tesla) equipped with a double tuned cryo-probe (TCI) set for 5 mm sample tubes. 1H NMR spectra of hydrophilic cell extracts were acquired using a one-dimensional NOESY-presat pulse sequence (RD-90°-t-90°-tm-90°-ACQ). All the experiments were acquired with an acquisition time of 2.73 s, a relaxation delay of 4 s, mixing time of 10 ms, receiver gain of 181, 128 scans, 128 K data points and a spectral width of 18,029 Hz (30.041 ppm). All samples were automatically tuned, matched and shimmed.
Representative samples of treated cell extracts were examined by two-dimensional spectroscopy (JRES, COSY, TOCSY, HSQC and HMBC) to ensure the unambiguous assignment of the metabolites. A 700 MHz Varian Unity Inova spectrometer equipped with a 5 mm 1H{13C/15N} triple resonance probe was used for the acquisition of two-dimensional NMR experiments.
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4

Characterization of Commercial Light-Cured Resins

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1H NMR spectra used to establish the chemical composition of commercially available preparations were recorded with use of a UNITY/INOVA spectrometer (Varian) at a frequency of 300 MHz. A tetramethylsilane (TMS) standard and a solvent (deuterated chloroform – CDCl3) were used.
All resin materials used in the tests were light-cured. A wireless LEDEX WL-070 lamp (Dentmate) was used for polymerization. A 5W LED diode was used as a source of blue light with a wavelength of 440 – 480 nm. The radiation power exceeded 1000 mW/cm2.
Samples were examined with a Hitachi S-4200 scanning electron microscope (Institute of Material Sciences, Silesian University of Technology). This device allows magnification ranging from 20 to 500,000 times and for both qualitative and quantitative analysis of the chemical composition of a material with point, linear, and surface methods. The range of accelerating voltages ranged between 0.5 and 30 kV. The recording of images and results of an X-ray microanalysis was made with use of a Thermo Scientific software package.
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5

Structural Elucidation of E3 Fraction

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Composition of the E3 fraction was investigated by high-resolution Liquid Chromatography-Mass Spectroscopy (LC–MS) using a Thermo LTQ-Orbitrap XL system, and by 1D (1H and 13C) and 2D (COSY, HSQC and HMBC) NMR using a Varian UnityInova spectrometer at 700 MHz equipped with a cryogenic probe. NMR chemical shifts were referenced to the residual solvent signal (CD3OD: δC 49.0, δH 3.31; pyridine-d5 δC 150.3, 135.9 and 123.9, δH 8.73, 7.56 and 7.21).
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6

Cardiac MRI Imaging Protocol

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MR imaging was performed using a Varian 4.7T magnet with a UnityInova spectrometer. A birdcage volume coil (72 mm inner diameter) was used for both transmitting and receiving. An animal monitoring system (Small Animal Instruments Inc., Stony Brook, NY) enabled image acquisition to be gated to ECG and respiration. Throughout imaging, the core body temperature of the animal was maintained at 35–38°C by directing a regulated stream of warm air over the animal, and both heart rate and body temperature were recorded.
Cine MR images at 3 long‐axis (angular spacing = 60°) and 6 short‐axis slices (spacing = 0.6 mm–1.0 mm) were acquired to ensure full coverage of the LV. Each slice was imaged at 18 evenly spaced time‐points through the cardiac cycle. T1‐weighted gradient‐echo cine acquisitions used the following parameters: repetition time, TR = 2 ×  R‐R interval, ~ 280 ms ‐ 360 msec; echo time, TE = 2.2 msec; cardiac phases = 20; flip angle = 20°; slice thickness = 2 mm; averages = 2, field of view = 60 mm × 60 mm; matrix = 128 pixels × 128 pixels; gap between slices = 0.6 mm–1.0 mm according to the size of the heart.
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7

Elemental Analysis and Spectroscopy

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Elemental analyses were performed using a Perkin-Elmer 240CHN elemental analyzer (PerkinElmer Japan Co., Ltd., Tokyo, Japan). Mass spectra were recorded by a JEOL JMS-SX 102 AQQ mass spectrometer (JEOL Ltd., Tokyo, Japan). 1H- and 13C-NMR were measured using a Varian Unity Inova spectrometer (Varian, Inc., Palo Alto, CA, USA), with tetramethylsilane as an internal standard.
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8

Freeze-Drying NMR Sample Preparation

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After removing aliquots for fluorescence microscopy, the remainder of the sample was transferred to a 1.5 mL microcentrifuge tube and freeze-dried. The solids remaining in the tube were then dissolved in an NMR solvent. The proton NMR spectra were acquired in dimethyl sulfoxide-d6 or methanol-d4 at 25 °C on a 500 MHz Varian Unity/Inova spectrometer.
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9

Spectroscopic Analysis of Organic Compounds

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IR spectra were recorded on KBr discs, using a Shimadzu IR Affinity-1 FT-IR instrument. 1H NMR (500 MHz), and 13C NMR (125 MHz) spectra were recorded on Varian UNITY INOVA spectrometer in DMSO-d6 solution. Chemical shifts (δ) were reported in ppm; coupling constants (J) were recorded in hertz (Hz). Mass spectra were obtained on a Finnigan LCQ Advantage Max mass spectrometer. The reactions were monitored by TLC aluminum plates with silica gel Kieselgel 60 F254 thickness 0.25 mm (Merck), using UV light as a visualizing agent. All reagents and solvents were purchased from Merck, Fluka and Sigma-Aldrich and were used without further purification.
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10

NMR Characterization of DNA-Ligand Complexes

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A 700 MHz Varian Unity INOVA spectrometer was employed to perform the NMR experiments. One-dimensional proton spectra were recorded at 7°C using pulsed-field gradient DPFGSE for water suppression. All DNA samples were prepared at 0.2 mM strand concentration in 0.22 mL (H2O/D2O 9:1) buffer solution. DNA/ligand mixtures were obtained by adding aliquots of a stock solution of the six ligands in DMSO-d6 directly to the DNA solution inside the NMR tube (Randazzo et al., 2002 (link); Amato et al., 2017 (link)). NMR data were processed using the iNMR software (www.inmr.net).
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