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75 protocols using nicolet 380 ftir spectrometer

1

FT-IR Spectroscopy Analysis of Peptide Secondary Structure

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Fourier‐transform infrared spectroscopy was performed on a Nicolet 380 FT‐IR spectrometer (Thermo Fisher, USA) equipped with an attenuated total reflectance (ATR) accessory. The sample solution used for CD spectroscopy was also used for FT‐IR analysis. Prior to actual measurement, background spectra were obtained under nitrogen gas purging of the detector to minimize interference from other gases such as water vapor and/or CO2. The spectral range collected was 400–4000 cm−1. The resolution and scan number were 4 cm−1 and 256, respectively. For analyzing peptide secondary structure, FT‐IR spectra were processed to the second derivative using OriginPro 8 software with 7‐point smoothing (OriginLab Corp., Northampton, MA, USA) as reported earlier.77, 97
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2

Characterization of Iron Ore Binder

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The binder structure was analyzed by Fourier transform infrared (FTIR) spectrometry and thermogravimetric differential scanning calorimetry (TG-DSC). The binder was measured on a Nicolet 380 FTIR spectrometer (Nicolet 380, Thermo Fisher Scientific, Waltham, MA, USA) using the KBr disc technique. For FTIR measurement, 1 mg binder was mixed with 100 mg anhydrous KBr and was then compressed into thin disk-shaped pellets. The spectra were measured with a resolution of 4 cm−1 between a wave number range of 4000 to 400 cm−1. The thermal analysis of the binder was carried out using TG-DSC (STA449F3, Netzsch, Selb, Germany). The type of crucible of the TG/DSC pan was Al2O3. The sample chamber was purged with nitrogen gas at a rate of 30 mL/min. TG and DSC analyses were performed with a heating rate of 10 °C/min in the temperature range of 28 to 1200 °C. Scanning electron microscopy (SEM, Nova NanoSEM 450, FEI, Columbia, MD, USA) was used to observe the microstructure of binder particles and to gain further knowledge of the iron ore particle structure and morphology after bonding with the binder.
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3

FTIR Analysis of Cellulose Nanocrystals

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FTIR spectroscopy was used to examine the changes in the functional groups of CNCs obtained. The FTIR spectra were collected by using a Nicolet 380 FT-IR Spectrometer (Thermo Fisher Scientific, Hampton, NH, USA) in the transmittance mode. Five mg of powder samples of RF and CNC were dispersed in a matrix of KBr to be mixed and pressed into a pellet. The samples were analyzed in a spectral region between 4000 and 400 cm−1 with a 2 cm−1 resolution, while the obtained spectra were averaged over 32 scans.
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Characterization of Inorganic Materials

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Elemental analysis was performed using a CHNOS vario EL cube analyzer (Elementar Analysensysteme GmbH, Langenselbold, Germany). Cobalt was determined on an energy dispersive X-ray fluorescence spectrometer «X-Art M» (Comita, Moscow, Russian) or atomic absorption spectrometer «MGA-915» (Lumex, St. Petersburg, Russia). The Fourier transform IR (FTIR) spectra were recorded with a Nicolet 380 FTIR spectrometer (Thermo Fisher Scientific, Waltham, MA, USA) from KBr pellets using Softspectra data analysis software (Shelton, CT, USA). X-ray diffraction (XRD) analysis was carried out on a DRON-UM-2 diffractometer (JSC “Burevestnik”, St. Petersburg, Russia) with CuKα radiation (λCu = 1.54184 Å) in the range of 2θ = 5–80° angles 2θ with a scanning speed of 5°/min and a temperature of 25 °C to determine the phase composition and crystallite size. Scanning electron microscopic (SEM) images were obtained using a Zeiss LEO SUPRA 25 device (Carl Zeiss, Jena, Germany) at an accelerating voltage of 3 kV.
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5

FT-IR Characterization of Samples

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FT-IR analysis was conducted using a Nicolet 380 FT-IR spectrometer (Thermo Fisher, Waltham, MA, USA) equipped with an attenuated total reflectance (ATR) accessory. Spectra were collected from 400 to 4000 cm−1 at a 4 cm−1 resolution and 256 scan numbers. Prior to the collection of spectra for the samples, background spectra were scanned first by purging the detector with nitrogen gas to minimize interference by water vapor and CO2. Second derivative data were obtained by OriginPro 8 software, (OriginLab Corp, Northampton, MA, USA) and then processed with 7-point smoothing.
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6

Infrared and Raman Spectroscopy of Samples

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Infrared spectra were recorded with a Thermo Fischer Scientific Nicolet 380 FTIR spectrometer (Madison, WI, USA), controlled by OMNIC software and equipped with a deuterated triglycine sulfate (DTGS) detector with KBr window. A 1 mg sample was gently mixed in an agate mortar with 100 mg spectroscopy-grade KBr (Merck, Darmstadt, Germany) and then pressed into pellet form with a hydraulic press (Specac, Orpington, UK). The FTIR spectra were measured in triplicate in the spectral range of 4000–400 cm–1 with resolution of 2 cm–1 (16 scans). The background spectrum was recorded before each measurement was taken.
The Raman spectra were registered on a Thermo Fisher Scientific DXR SmartRaman spectrometer (Madison, WI, USA), with a Raleigh filter, charge-coupled detector (CCD) and OMNIC software. Measurements in triplicate were performed in the spectral range of 3413–99 cm–1 with a spectral resolution of 2 cm–1. The spectrometer was equipped with 15-mW DXR 780 nm laser (aperture of 25 µm) and samples were exposed to laser light for a period of 1 s.
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7

Comprehensive Characterization of Zirconium Complex

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NMR analysis was undertaken using a JEOL NMR ECS-400 and JEOL Delta v5.02 software. FTIR spectra were obtained using a Thermo Scientific Nicolet 380 FT-IR spectrometer with a Smart Orbit high performance diamond single bounce ATR accessory. CHN analyses were obtained at the University of Kent utilising an A EMA Syst 1106 elemental analyser and at the Science Centre, London Metropolitan University utilising a Carlo Erba Flash 2000 elemental analyser. Raman spectra were obtained using a Horiba LabRAM-HR Raman spectrometer utilising a laser operating at 784 nm. A ×50 objective lens was used giving a beam diameter of approximately 2 µm on the sample. The spectrometer was calibrated against the silicon line at 520.6 cm-1. UV-visible spectra were obtained with a Shimadzu UV-1800 spectrometer.
HPLC was performed using a Dionex Ultimate 3000 system with data processing using Chromeleon 7. For ITLC a 20 mM citrate elutant solution (pH 4.0) was made by the addition of 0.262 g of citric acid and 0.193 g of tri sodium citrate to 100 mL of millipore water. ITLC-SG plates were obtained from Varian. K4[Zr(C2O4)4] was prepared by a literature method.24
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8

Characterizing Engineered Nanoparticle Surface

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The specific surface areas of MSB and MSB-nZVI were analyzed using an ASAP 2020 surface area and porosity analyzer (Micromeritics, Norcross, GA, USA). A scanning electron microscope (SEM, Quanta FEG 250, Hillsboro, OR, USA) coupled with an energy dispersion spectrometer (EDX, X-Max50, Oxford, UK) was used to observe surface morphology and chemical elements of MSB-ZVI before and after reaction with Cr(VI). The surface functional groups of the samples were examined by a Nicolet 380 FTIR spectrometer (Thermo Scientific, Waltham, MA, USA). Mineralogical characterization of MSB-nZVI before and after reaction with Cr(VI) was performed by a powder X-ray diffractometer (XRD, Bruker D8 ADVANCE, Berliln, Germany).
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9

Characterizing Materials via FTIR Spectroscopy

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Infrared spectra were recorded on a Nicolet 380 FT-IR spectrometer (Thermo Scientific, Baltimore, MD, USA) equipped with a commercial attenuated total reflectance accessory. The FT-IR spectra were recorded from 4,000 to 400 cm−1 at 2 cm−1 resolution using an IFS 66v/S spectrometer (Bruker Corporation, Karlsruhe, Germany) and KBr pellets. Spectra were collected by averaging 256 scans at 4 cm−1 resolution.
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10

FTIR Analysis of KcsA Protein in Salts

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For the FTIR absorbance spectra,
approximately 2.5 μL of KcsA sample in different salt conditions
was sandwiched between two 1 mm thick CaF2 windows (CeNing
Optics), separated by a 50 μM PTFE spacer. For each sample,
2048 averages were collected on a Nicolet 380 FTIR spectrometer (Thermo
Scientific) at 1 cm–1 resolution against a background
of dry air at 20 °C. FTIR spectra of each buffer, without protein,
were also collected in order to subtract the background D2O absorption from the KcsA spectra. Difference spectra are calculated
as FTIR spectra of (KcsA in KCl, buffer subtracted) – (KcsA
in NaCl, buffer subtracted).
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