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Nicolet nexus spectrometer

Manufactured by Thermo Fisher Scientific
Sourced in United States

The Nicolet Nexus spectrometer is a versatile analytical instrument designed for a wide range of spectroscopic applications. It is capable of performing Fourier-transform infrared (FTIR) spectroscopy, a technique used to identify and analyze the chemical composition of various materials. The Nicolet Nexus spectrometer is renowned for its high-performance optical components, advanced data processing algorithms, and user-friendly software interface.

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12 protocols using nicolet nexus spectrometer

1

Multifunctional Ag@MSNs-Tf Nanosystem Synthesis

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Ag@MSNs-Tf nanosystem was synthesized as previously described [20 (link)]. Briefly, AgNPs were synthesized in a CTAB-containing medium prior to mesoporous silica shell formation. Then, Ag@MSNs were functionalized to display carboxylic acid groups (-COOH) onto their surface (Ag@MSNs-COOH). Finally, transferrin (Tf) was covalently grafted on the nanosystem via carbodiimide chemistry (Ag@MSNs-Tf). The nanosystem preparation was monitored after each synthetic step by thermogravimetric and differential thermal analysis (TGA and DTA) in a PerkinElmer Pyris Diamond TG/DTA analyzer, Fourier transform infrared (FTIR) spectroscopy using a Thermo Nicolet Nexus spectrometer, electrophoretic mobility measurements to calculate the values of the zeta-potential (ζ), and dynamic light scattering (DLS) performed in a Zetasizer Nano ZS Malvern instrument and transmission electron microscopy acquired in a JEOL JEM 1400 microscope.
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2

Comprehensive Materials Characterization Protocol

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FTIR was performed on a Thermo Nicolet Nexus spectrometer with a Smart Orbit (Waltham, MA, USA) in the range of 400–4000 cm−1.
The crystallinity study was carried out by powder X-ray diffraction (PXRD), Bruker D8 Advance powder XRD (Billerica, MA, USA) using CuKα radiation (λ = 0.15406 nm) at 40 kV and 40 mA.
The thermal stability and decomposition were done by TGA/DTG analysis, Mettler-Toledo 851e (Columbus, OH, USA) at a heating rate of 10 °C min−1 in 150-µL alumina crucibles in the range of 30–900 °C.
The hydrodynamic particle size distribution was determined by the dynamic light scattering (DLS) method using a particle size analyzer Nano Series Nano-ZS (Malvern Panalytical Ltd., Malvern, United Kingdom).
The internal morphology and particle size diameter were studied using HRTEM, FEI Tecnai G2 F20 S-TWIN (Hillsboro, OR, USA).
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3

Solid-state FTIR Characterization

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ssFTIR measurements were conducted in attenuated total reflectance mode using a Nicolet Nexus spectrometer (Thermo Scientific, Waltham, MA) equipped with a Smart iTR accessory. Powders were loaded and compressed against the diamond by a metal anvil. The spectra were collected in the absorbance mode in the range of 800 to 4000 cm−1, with 120 scans and 4 cm−1 resolution. Using OPUS 6.5 analysis software (Bruker, Billerica, MA), the results were processed using baseline correction, smoothing, normalization, and second derivatization.
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4

Infrared Spectroscopy of Particles

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A Nicolet Nexus spectrometer (Thermo Fisher Scientific) equipped with a Smart Golden Gate attenuated total reflectance (ATR) accessory was used. Measurements were carried out with 5 mg of the corresponding particles.
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5

Protein Secondary Structure Analysis via ATR-FTIR

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Attenuated total reflectance (ATR) mode on a Nicolet Nexus spectrometer (Thermo Scientific, Waltham, MA, USA) equipped with Smart iTR accessory was used to obtain the ssFTIR spectra for the protein secondary structural analysis. A range of 800 to 4000 cm−1 in absorbance mode at 4 cm−1 resolution was used to collect the data. All spectra were corrected for moisture content and CO2. OPUS 6.5 analysis software (Bruker, Billerica, MA, USA) was used to process the spectra with baseline correction, smoothing, normalization, and second derivatization.
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6

FTIR Spectroscopic Analysis of Enzyme Immobilization

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The presence of functional groups on the enzyme and support before and after immobilization was evaluated by FTIR spectroscopy. The analysis was done using a Nicolet "Nexus" spectrometer (ThermoFisher) equipped with a diamond ATR "Golden Gate" plate. The scan range was 400-4000 cm -1 using 128 scans per spectrum with a resolution of 4 cm -1 .
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7

Attenuated Total Reflectance FTIR Analysis

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Measurements were conducted with a Thermo Scientific Nicolet Nexus spectrometer (Waltham, MA) in the attenuated total reflectance mode. Samples were loaded onto a Smart iTR™ accessory and compressed against the diamond by a metal anvil. Spectra were collected in absorbance mode with 120 scans in the range of 800 to 4000 cm−1 with a 4 cm−1 resolution. Results were processed with OPUS 6.5 analysis software (Bruker, Billerica, MA) using baseline correction, smoothing, normalization, and second derivatization.
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8

Protein Secondary Structure Analysis by FTIR

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Attenuated total reflectance (ATR) mode on a Nicolet Nexus spectrometer (Thermo Scientific, Waltham, MA, USA) equipped with Smart iTR accessory was used to obtain the ssFTIR measurements for the protein secondary structural analysis. A range of 800 to 4000 cm−1 in absorbance mode at 4 cm−1 resolution was used to collect the data. All spectra were corrected for moisture content and CO2. OPUS 6.5 analysis software (Bruker, Billerica, MA, USA) was used to process the spectra with baseline correction, smoothing, normalization, and second derivatization.
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9

Protein Secondary Structure Characterization by ATR-FTIR

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A Nicolet Nexus spectrometer (Thermo Scientific, Waltham, MA) equipped with Smart iTR accessory was used in attenuated total reflectance (ATR) mode to conduct the ssFTIR measurements for secondary structural analysis. After the samples were loaded and compressed against the diamond, spectra were collected in the range of 800 to 4000 cm−1 in absorbance mode with co-addition of 120 scans obtained at 4 cm−1 resolution. The resulting spectra were processed using OPUS 6.5 analysis software (Bruker, Billerica, MA) with baseline correction, smoothing, normalization and second derivatization.
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10

Comprehensive Characterization of PAL

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The chemical composition of PAL was determined using a Minipal 4 X-ray fluorescence spectrometer (PANalytical, The Netherlands, Germany). Morphological evolution of the samples was observed using a field emission scanning electron microscopy (SEM, JSM-6701F, JEOL, Tokyo, Japan) and a transmission electron microscope (TEM, JEM-1200EX, JEOL, Tokyo, Japan). X-ray diffraction (XRD) patterns were acquired on an X’ Pert PRO diffractometer equipped with a Cu Kα radiation source, 40 mA, and 40 kV at a scanning rate of 0.02° per second. Fourier Transform infrared (FTIR) spectra were measured on a Nicolet NEXUS spectrometer (Thermo Fisher Scientific, Waltham, Massachusetts, America) in the range of 4000–400 cm−1 using potassium bromide pellets. Nitrogen adsorption–desorption isotherms were recorded using the Brunauer–Emmett–Teller analysis (BET, Micromeritics, Norcross, Georgia, America). Thermogravimetric analyses (TG) were performed on the simultaneous thermal analyzer (STA6000, PerkinElmer, America), operating from 30 °C to 800 °C, with a heating rate of 10 °C/min in a nitrogen atmosphere.
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