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Tensor 27 fourier transform spectrometer

Manufactured by Bruker
Sourced in Germany

The Tensor 27 is a Fourier-transform spectrometer manufactured by Bruker. It is a compact and robust instrument designed for routine infrared spectroscopy measurements. The Tensor 27 utilizes Fourier-transform infrared (FTIR) technology to obtain infrared spectra of solid, liquid, and gaseous samples.

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6 protocols using tensor 27 fourier transform spectrometer

1

Infrared Spectroscopy of HoxG Protein

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HoxG protein solutions were transferred into a homemade, gas-tight, and temperaturecontrolled (10°C) transmission cell equipped with two sandwiched CaF2 windows separated by a Teflon spacer with an optical pathlength of 50 μm. Spectra with a resolution of 2 cm−1 were recorded on a Tensor 27 Fourier-Transform spectrometer (Bruker) equipped with an MCT (liquid nitrogen-cooled mercury-cadmium-telluride) detector. The cell compartment was purged with dried air. For a single spectrum 200 individual scans were averaged. A buffer spectrum was used as reference for calculating the corresponding absorbance spectra. OPUS software version 7.5 from Bruker was used for data analysis. For the cofactor-stability experiments, IR spectra of as-isolated HoxG protein solution 35 mg/ml (500 μM) and a threefold higher concentrated sample were recorded consecutively for 7 h.
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2

Infrared Spectroscopy of KBr Pellets

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The infrared spectra were recorded on a Tensor 27 Fourier-transform spectrometer Bruker (Ettlingen, Germany) in a range of 4000–400 cm−1 with an optical resolution of 4 cm−1 and an accumulation of 32 scans using KBr pressed pellets.
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3

Optical and Thermal Characterization of Solar Selective Coatings

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The reflectanceI) solar spectrum range (0.3–2.5 μm) of the coating was obtained by a Shimadzu UV3600 UV/VIS/NIR spectrophotometer with an integration sphere (module 150 mm), while the reflectance spectra in the range of 2.5–25 μm were measured by a Bruker Tensor 27 Fourier Transform spectrometer equipped with an integrating sphere (A562-G/Q) using a gold plate as a standard. Then, the absorptance α and emittance ε were obtained by Equations (1) and (2): α=0.32.5Isλ1Rλdλ0.32.5Isλdλ
ε=2.525Ibλ1Rλdλ2.525Ibλdλ
where λ is the wavelength, Is(λ) is the solar radiation power at AM1.5, R(λ) is the spectral reflectance of sample, and Ib(λ) is the spectral black body emissive power at room temperature.
The thermal stability of the solar selective absorbing coating was evaluated by the performance criterion (PC), which was calculated from the obtained α and ε according to the following Equation (3):

where Δα = α(aged) − α(unaged) and Δε = ε(aged) − ε(unaged). Once the PC increases to be higher than 0.05, the solar selective absorbing coating is identified as having failed.
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4

NMR and FTIR Characterization Protocol

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NMR spectra were recorded at 300 K on a Bruker Avance III Ascend 500 (500 MHz) spectrometer with a delay time (d1) set to 8 s by using deuterated chloroform (CDCl3) as the solvent, and tetramethylsilane (TMS) as the insternal standard. FTIR spectra were recorded on Bruker Tensor 27 Fourier Transform Spectrometer.
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5

Ruthenium-Catalyzed Hydrophosphination Reactions

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All reactions and manipulations were performed under dry high-purity nitrogen using standard Schlenk techniques. Ru3(CO)12 and 1–6 were synthesized according to the literature procedures.25 (link) The solvents used in the experiments were purified, dried and distilled from sodium under a nitrogen atmosphere prior to use. Preparative TLC was performed on 20 × 20 cm glass plates coated with silica gel (Merck GF254, 0.5 mm thick). FT-IR spectra were recorded on a Bruker Tensor 27 Fourier-transform spectrometer. 1H and 13C{1H} NMR spectra were performed on a Bruker Avance 400 MHz spectrometer unless indicated. ESI was recorded on a Thermo DecaMax (LC-MS) mass spectrometer with an ion-trap mass detector. While high-resolution mass spectra were recorded in ESI mode on a Waters UPLC-Q-TOF mass spectrometer.
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6

Infrared Spectroscopy of MBH Protein

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A volume of 10 µl with MBH protein concentration of 0.3 mM was transferred into a gas‐tight, homemade, temperature‐controlled (10°C), transmission cell equipped with sandwiched CaF2 windows and a Teflon spacer (optical path length of 50 µm). Spectra with 2 cm‐1 resolution were recorded on a Tensor 27 Fourier‐Transform spectrometer (Bruker) equipped with a liquid N2‐cooled mercury cadmium telluride (MCT) detector. For a single spectrum, 200 scans were averaged. The sample compartment was purged with dried air. A buffer spectrum was taken to calculate the corresponding absorbance spectra. Bruker OPUS software 7.5 was used for data analysis.
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