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Dmx 400 mhz spectrometer

Manufactured by Bruker
Sourced in Germany

The DMX 400 MHz spectrometer is a nuclear magnetic resonance (NMR) instrument designed for analytical and research applications. It operates at a frequency of 400 MHz and provides high-resolution spectroscopic data for the identification and characterization of chemical compounds.

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8 protocols using dmx 400 mhz spectrometer

1

Amide H/D Exchange Kinetics

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Spectra for H/D exchange experiments were acquired with a DMX 400 MHz spectrometer from Bruker (Billerica, MA) in the National Magnetic Resonance Facility at Madison (NMRFAM). H/D exchange experiments were performed by co-dissolving AcDegNHMe and AcDegOMe, or AcGlyNHMe and AcGlyOMe in DMSO-d6 to a final concentration of 50 mM each. Aliquots (0.50 mL) of the resulting solutions were transferred to NMR tubes. Exchange was initiated by the addition of 10 μL of D2O at time t = 0. Samples were mixed thoroughly by repeated inversion for 30 s before collection of the first spectrum. 1H NMR spectra were collected by averaging 16 individual scans to provide adequate signal to noise. Integrations were determined from the area of the calculated fit of the amide region (7.2–8.0 ppm for diethylglycines or 7.6–8.4 ppm for glycines), as determined with the program MestReNova 9.0 from MestreLab Research (Escondido, CA). Experiments were performed in triplicate.
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2

Amide H/D Exchange Kinetics

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Spectra for H/D exchange experiments were acquired with a DMX 400 MHz spectrometer from Bruker (Billerica, MA) in the National Magnetic Resonance Facility at Madison (NMRFAM). H/D exchange experiments were performed by co-dissolving AcDegNHMe and AcDegOMe, or AcGlyNHMe and AcGlyOMe in DMSO-d6 to a final concentration of 50 mM each. Aliquots (0.50 mL) of the resulting solutions were transferred to NMR tubes. Exchange was initiated by the addition of 10 μL of D2O at time t = 0. Samples were mixed thoroughly by repeated inversion for 30 s before collection of the first spectrum. 1H NMR spectra were collected by averaging 16 individual scans to provide adequate signal to noise. Integrations were determined from the area of the calculated fit of the amide region (7.2–8.0 ppm for diethylglycines or 7.6–8.4 ppm for glycines), as determined with the program MestReNova 9.0 from MestreLab Research (Escondido, CA). Experiments were performed in triplicate.
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3

NMR, IR, TGA, and CD Characterization Protocol

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Solution 1H NMR and 13C NMR spectra were recorded on a Bruker DMX 400 MHz spectrometer. 13C CP‐MAS NMR spectra were recorded on a Bruker Avance III (100.6 MHz) 400 NMR spectrometer; 4 mm zirconia rotors with stirring speeds of 5 kHz were used, with 5,000 to 10,000 number of scans. FT‐IR spectra were obtained from a Bruker FT‐IR Tensor27 system using the attenuated total reflection (ATR) technique via a Pike miracle ATR cell. Thermogravimetric analysis (TGA) was performed using a TGA Q500 (TA Instruments). Samples were heated from ambient temperature to 800 °C at a heating rate of 10 °C/min under a nitrogen atmosphere. Circular dichroism (CD) spectropolarimetry measurements were conducted using an OLIS spectrophotometer.
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4

Characterization of Polymers by NMR and GPC

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Proton nuclear magnetic resonance (1H NMR) spectra of PZL and PCPZL were collected at room temperature using a Bruker DMX 400 MHz spectrometer (Bruker, Karlsruhe, Germany) using deuterated dimethyl sulfoxide (DMSO-d6) as the solvent. The molecular weight parameters of the polymers were analyzed using a gel permeation chromatography (GPC) system from Waters (Milford, CT, USA), which consisted of a Waters 515 HPLC pump and a Waters 2414 refractive index detector. The samples were analyzed using dimethylformamide (DMF) as the eluent and linear poly(methyl methacrylate) (PMMA) as the calibration standard.
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5

Characterization of chiral liquid crystal GNRs

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Transmission electron microscopy (TEM) analysis was performed with a FEI Tecnai TF20 TEM instrument at an accelerating voltage of 200 kV. Samples were prepared by evaporating a drop of dilute GNR solutions in chloroform onto carbon-coated copper TEM grids (400 mesh, TED PELLA, Inc.), which were allowed to dry for 24 h prior to imaging. Freeze-fracture TEM (FF-TEM) images were obtained either on a FEI Tecnai TF30 ST TEM instrument at an accelerating voltage of 300 kV or a JEOL JEM-100S at 100 kV. The FF-TEM samples, replicas of fractured surfaces of the LC-GNR composites, were prepared following a procedure described elsewhere51 (link). UV-Vis absorption and solution circular dichroism (CD) spectropolarimetry measurements were done using an OLIS spectrophotometer (1 cm path length quartz cuvettes). 1H NMR spectra were recorded in CDCl3 on a Bruker DMX 400 MHz spectrometer and referenced internally to residual solvent peaks at 7.26 ppm. Polarized optical microscopy (POM) observations of the induced chiral nematic liquid crystals (N*-LCs) were recorded and photographed using an Olympus BX-53 polarizing microscope equipped with a Linkam LTS420E heating/cooling stage. Differential scanning calorimetry (DSC) was performed using a Pyris 1 DSC instrument (Perkin Elmer). Thermogravimetric analysis (TGA) was performed using a TGA Q500 (TA Instruments).
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6

Spectroscopic Analysis of Compounds

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1H NMR and 13C NMR spectra were obtained on a Bruker DMX-400 MHz spectrometer. ESI-MS spectra were taken on a Brucker APEX IV(7.0T) FT_MS. Elemental analysis results were obtained on a vario MICRO cube. UV-vis absorption spectra were recorded on a Shimadzu UV-2450 spectrophotometer. Fluorescence emission spectra were run on a Hitachi F-4600 fluorescence spectrophotometer. IR data was collected on Varian Excalibur 3100.
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7

Evaluating β-GPA Transport and Effects in Fish Muscle

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31P-NMR was used to evaluate whether β-GPA can be transported into fish muscle fibers and be phosphorylated, and to examine the effect that phosphorylated β-GPA has on the intracellular high energy phosphates (HEPs). To do this, 5 fish from each group were selected randomly and ~0.1 g of muscle tissue was excised immediately postmortem, freeze clamped in liquid N2, and weighed. Sample preparation followed that of Ross et al. (2017) (link). Once prepared, the supernatant was immediately analyzed by 31P-NMR spectroscopy, since HEPs can be degraded over time. Supernatants were transferred to a 5 mm NMR tube and 31P-NMR spectra were collected at 162 MHz on a Bruker 400 MHz DMX spectrometer. 750 scans were collected for each spectrum using a 45° excitation pulse with a 0.6 s relaxation delay, resulting in a total acquisition time of 7.5 min. The relative peak areas of α-, β-, and γ-ATP, PCr, inorganic P (Pi), and P-GPA were integrated using Xwin-NMR software (Fig. 1B). Fractional peak area for each compound was calculated as a percent of the total peak area for each specimen. A one-tail Student’s t-test was used to test for a significantly reduced fractional peak area of HEPs, as well as a significantly increased fractional peak area of P-GPA in treatment groups.
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8

Gastrocnemius Muscle Metabolites by 31P-NMR

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Gastrocnemius supernatants were transferred to 5‐mm NMR tubes and 31P‐NMR spectra were collected at a frequency of 162 MHz on a Bruker 400 MHz DMX Spectrometer. Two thousand four hundred scans were collected for each spectrum using a 45° excitation pulse with a 0.6 sec relaxation delay, resulting in a total acquisition time of 30 min. The relative peak areas of α‐, β‐, and γ‐ATP, PCr, Pi, and P‐GPA were integrated using Xwin‐NMR software, and relative amounts of each compound were determined from the relative peak area.
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