Unityinova nmr spectrometer

Manufactured by Agilent Technologies

Sourced in United States

The UnityINOVA NMR spectrometer is a nuclear magnetic resonance (NMR) instrument manufactured by Agilent Technologies. It is designed to analyze the chemical composition and structure of materials by measuring the magnetic properties of atomic nuclei within the sample.

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Unityinova 500 NMR Spectrometer NMR spectrometer Spectrometers

5 protocols using unityinova nmr spectrometer

Magnetically-Driven Nanoparticle Microsphere Imaging

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The scattering properties of nanoparticle-based microspheres and their displacement in a magnetic field were performed
with 1.0 × 10⁷ microspheres in each sample. MM-OCT imaging of samples was performed with a spectral-domain OCT
system using a Ti:Al₂O₃ femtosecond laser (KMLabs, Inc.) as a light source, which was described previously
[9 (link)]. The light, with a bandwidth of 120 nm centered at 800 nm, provided ~3 Pm
axial imaging resolution. A magnetic field of ~0.08 T and a gradient of ~15 T m was produced within the sample
imaging volume using a water-cooled magnet. The light beam on the sample was scanned through the central bore of the solenoid and
the interference between the reference and sample beams was measured with a custom-made spectrometer, providing 2 mm imaging
depth. MM-OCT imaging was done at 100 Hz and 200 Hz, with a scan rate of 1000 A-scans/sec.
A 14.1 T Varian system with an 89 mm bore size and 600 MHz Varian Unity/Inova NMR spectrometer was used for MRI
measurements. Measurements were taken at four different echo times of 3.3 ms, 5.0 ms, 7.0 ms, and 9.0 ms, and nineteen MRI slices
were taken throughout the full volume of the gel in the capillary tubes to create a standard curve and calculate the relaxation
times (T2*) using a Matlab script.

Marjanovic M., Nguyen F.T., Ahmad A., Huang P.C., Suslick K.S, & Boppart S.A. (2018). Characterization of Magnetic Nanoparticle-Seeded Microspheres for Magnetomotive and Multimodal Imaging. IEEE journal of selected topics in quantum electronics : a publication of the IEEE Lasers and Electro-optics Society, 25(1), 7101314.

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1H-NMR Analysis of Stingless Bee Honey

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The ¹H-NMR spectra of stingless bee honey samples were acquired in duplicates, at 25 °C, on a 500 MHz Unity Inova NMR spectrometer (Varian Inc., California, CA, USA). Each spectrum was acquired over a spectral width of 0–10 ppm, using 64 scans and acquisition time of 256.8 s. The presaturation pulse sequence was used to suppress residual water signal with low power selective irradiation. D₂O was used as internal lock and TMSP-2,2,3,3-d4 was used as reference standard at 0.00 ppm.

Razali M.T., Zainal Z.A., Maulidiani M., Shaari K., Zamri Z., Mohd Idrus M.Z., Khatib A., Abas F., Ling Y.S., Rui L.L, & Ismail I.S. (2018). Classification of Raw Stingless Bee Honeys by Bee Species Origins Using the NMR- and LC-MS-Based Metabolomics Approach. Molecules : A Journal of Synthetic Chemistry and Natural Product Chemistry, 23(9), 2160.

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NMR Analysis of Organic Compounds

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NMR experiments were performed using a 500 MHz Unity INOVA NMR spectrometer (Varian) in DMSO-d₆ at 25°C as the solvent. ¹H NMR measurements were carried out at 500 MHz, while ¹³C NMR experiments were performed at 125 MHz. Proton and carbon chemical shifts were reported on the δ scale in ppm, relative to tetramethylsilane (TMS) (δ= 0.00 ppm) and DMSO (δ = 39.50 ppm) as internal standards in ¹H and ¹³C NMR spectra, respectively. Standard pulse sequences provided by Varian were used for 1D and 2D NMR data.

Prakash L., Himaja M, & Vasudev R. (2014). Isolation, Identification, and Characterisation of Degradation Products and the Development and Validation of a Stability-Indicating Method for the Estimation of Impurities in the Tolterodine Tartrate Formulation. Scientia Pharmaceutica, 83(1), 65-83.

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STD-HSQC NMR Characterization of Biomolecules

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All data were acquired at 10 °C using a 4-channel Varian UnityINOVA NMR spectrometer operating at 14.1 T (600 MHz ¹H) with a 5 mm room temperature HCN probe. 2D ¹³C,¹H-STD-HSQC experiments used a previously published pulse sequence,¹⁴ with Gaussian-based saturation^{19 (link)} at –3 ppm and –30 ppm. These experiments were acquired with 2048 data points (8000 Hz) in the direct F2 dimension and 64 data pairs – 128 points (18 000 Hz) in the indirect F1 dimension. ¹³C,¹H-HSQC spectra for assignment were acquired with 512 complex pairs (1024 points) in F1 and each inversion recovery ¹³C,¹H-HSQC dataset were acquired with 128 complex pairs (256 points) in F1; all with ¹³C spectral width of 18 000 Hz. In addition, inversion recovery experiments utilised a scan recycle delay of 5 seconds.

Sorge J.L., Wagstaff J.L., Rowe M.L., Williamson R.A, & Howard M.J. (2015). Q2DSTD NMR deciphers epitope-mapping variability for peptide recognition of integrin αvβ6 †Electronic supplementary information (ESI) available. See DOI: 10.1039/c5ob01237f Click here for additional data file.. Organic & Biomolecular Chemistry, 13(29), 8001-8007.

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NMR Spectroscopy of NS5A and NS4A Proteins

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2D (¹H-¹⁵N)-BEST-TROSY spectra [25] (link) were recorded at 303.15 K on a Varian ^UnityINOVA NMR spectrometer equipped with a cryogenic Z-axis PFG triple resonance probe operating at a proton frequency of 600 MHz. Data were processed with NMRPipe [26] (link) and analyzed with CcpNmr analysis [27] (link). NMR samples contained 1 mM [¹⁵N] labeled NS5A(1–48) or NS4A(1–48; L6E, M10E), respectively, in 50 mM sodium phosphate buffer (pH 6.8) with 10% (v/v) deuterium oxide and 0.03% (w/v) NaN₃.

Hung Y.F., Valdau O., Schünke S., Stern O., Koenig B.W., Willbold D, & Hoffmann S. (2014). Recombinant Production of the Amino Terminal Cytoplasmic Region of Dengue Virus Non-Structural Protein 4A for Structural Studies. PLoS ONE, 9(1), e86482.

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