The largest database of trusted experimental protocols

124 protocols using nicolet is50 spectrometer

1

FTIR Analysis of Photopolymerization Kinetics

Check if the same lab product or an alternative is used in the 5 most similar protocols
FTIR spectra were taken before and after UV irradiation using a Thermo Fisher Scientific NicoletTM iS50 Spectrometer (Thermo Fisher Scientific, Waltham, MA, USA) in attenuated total reflection (ATR) mode. All spectra were acquired in the range of 4000–500 cm−1 by 32 scans and a resolution of 4 cm−1. The measurement of the degree of conversion of the acrylate C=C bond of TMPTA was obtained by considering the area under the C=C band (approx. 1640 cm−1) of the reactive group ( AC=C ) with respect to the area of a reference signal in the spectra, namely the C=O band at 1720 cm−1 ( AC=O ), before irradiation (at time t = 0) and after UV-irradiation (at time t). Percent C=C conversion is calculated as indicated in Equation (1): Conversion %=1AC=CAC=OtAC=CAC=Ot=0×100
The value of conversion for each sample was provided as an average value ± standard deviation of three repetitions.
The insoluble fraction of the samples PEO-XL-E and PEO-XL-C was evaluated through the gel content experiment. Samples were wrapped in a metallic mesh with ultrafine pores and soaked in distilled water, which is a suitable solvent for uncured PEO polymer as well as for TMPTA unreacted monomer. Samples were soaked for 24 h and subsequently were left drying in laboratory conditions for 48 h, and afterwards the mass loss of the samples was calculated.
+ Open protocol
+ Expand
2

Characterization of Crystalline Powder Samples

Check if the same lab product or an alternative is used in the 5 most similar protocols
Powder diffractograms were obtained using an X-ray diffractometer (X'Pert Panalytical, Philips, Cambridge, MA) with CuKa radiation at a scanning rate of 1.228 min À1 from 5 to 50 with a measurement step of 0.017 , applying 45 kV at 40 mA to observe the crystallinity of the sample.
2.3.5. Differential scanning calorimetry Differential scanning calorimetry (DSC) measurements were carried out using a DSC-Q200 thermal analyzer (TA Instrument, Guyancourt, France) in a temperature range of 20-210 C (heating rate 5 C.min À1 ) under nitrogen gas with a flow rate of 50 mL min À1 . Samples of raw material and milled powder (2.8-5.5 mg) were placed in a hermetically closed aluminum pan. The heat of fusion (DH F ) and melting temperature (T m ) were calculated using the DSC software (Platinum V R ). The residual crystallinity (v c ) was calculated using Equation ( 1), taking into account the melting enthalpy of 100% crystalline sample (raw material) and ground one (Kumar et al. 2018) .
2.3.6. Fourier-transform infrared (FTIR) spectroscopy FTIR spectra were recorded on a Thermo Scientific Nicolet TM iS50 spectrometer, using Omnic V R software to analyze the data. The samples were placed on the diamond window. The data were recorded in ATR mode in a scan range of 4000-400 cm À1 with a resolution of 4 cm À1 .
+ Open protocol
+ Expand
3

FTIR Analysis of Irradiated Specimens

Check if the same lab product or an alternative is used in the 5 most similar protocols
Specimens for the FTIR study were analyzed after exposure to 70 Gy radiation (IR group) and the corresponding control treatment (C group). FTIR spectra were acquired using a Nicolet iS50 spectrometer (Thermo Fisher Scientific, Waltham, MA, USA) in a spectral range of 4000–400 cm−1 and a spectral resolution of 4 cm−1. The specimens were dried in a vacuum at room temperature for 7 days and fixed on an attenuated total reflectance (ATR) diamond crystal using a special press. The window of the ATR accessory sampled a circular area (d = 2.5 mm) from the center of each specimen. One spectrum per specimen was acquired by averaging 40 consecutive scans.
+ Open protocol
+ Expand
4

Analyzing Protein Structure in Decellularized Samples

Check if the same lab product or an alternative is used in the 5 most similar protocols
The protein secondary structure of native and decellularized samples was studied using Fourier transform infrared spectroscopy (FTIR). NBPs, DBPs, NPPs, and DPPs flaps (10 × 10 mm2, n = 3 for each group) were cut and equilibrated for 3–4 h in deuterium oxide (Janssen, Beerse, Belgium) to reduce the contribution of interfering water bands in the amide-I region [42 (link)]. FTIR investigations were performed using the Nicolet iS-50 spectrometer (Thermo Fisher Scientific, Waltham, MA, USA) in the attenuated total reflectance (ATR) mode. The instrument was equipped with a diamond/ZnSe crystal and pressure arm. The transmittance of both samples and background was each measured using 64 scans and infrared spectra were collected within the 4000–500 cm−1 range, at room temperature. Spectra were then overlapped using a Matlab® script (Mathworks, Natick, MA, USA) [43 ] to compare the composition of the investigated materials. Amide-I and amide-II bonds, respectively at 1630 cm−1 and 1550 cm−1 [40 (link),43 ], were selected to evaluate the integrity of ECM proteins. Peak transmittance ratio (R) was calculated dividing the intensity of the amide-I peak by the intensity of the amide-II peak.
+ Open protocol
+ Expand
5

FTIR Analysis of Control and Samples

Check if the same lab product or an alternative is used in the 5 most similar protocols
FTIR spectra of the control and obtained samples were recorded using a Nicolet iS50 spectrometer (Thermo Fisher Scientific Co., Hillsboro, OR, USA). Each measurement was performed using a built-in attenuated total reflectance (ATR) accessory. The analysis was carried out in the wavelength range of 4000–400 cm−1.
+ Open protocol
+ Expand
6

Comprehensive Nanomaterial Characterization by TEM, FTIR, Raman, and XPS

Check if the same lab product or an alternative is used in the 5 most similar protocols
Transmission electron microscopy (TEM) images were acquired by Tecnai G2 F30 transmission electron microscope (FEI, Hillsboro, OR, United States). BP NSs were observed after being dropped onto a copper grid-coated carbon membrane and air-dried. Fourier transform infrared (FTIR) spectra were recorded with Nicolet iS 50 spectrometer (Thermo Scientific, United States). Raman spectra were recorded at room temperature by LabRAM HR800 high-resolution confocal Raman microscope (HORIBA, United States). X-ray photoelectron spectroscopy was performed with Axis HSi X-ray photoelectron spectroscope (Kratos Ltd., United Kingdom) employing Al Kα radiation (150 W, 1486.6 eV photons) as the excitation source. Zeta potential and size were measured by Malvern Mastersizer 2000 particle size analyzer (Zetasizer Nano ZS90, Malvern Instruments Ltd., United Kingdom). All measurements were conducted three times independently and averaged.
+ Open protocol
+ Expand
7

Probing Rhombohedral BiFeO3 by FTIR and AFM-IR

Check if the same lab product or an alternative is used in the 5 most similar protocols
To have a first glimpse of the IR absorption for rhombohedral BiFeO3, FTIR was carried out based on a Nicolet iS50 spectrometer (Thermo Fisher) under grazing incidence mode with IR beam polarized vertical to the substrate plane. Accordingly, we observed strong absorption at ~500 cm−1, for the rhombohedral continuous thin film. To further distinguish the IR absorption for rhombohedral BiFeO3 nanocrystals with upward, downward quad-domains and the Solomon topological polar structure, AFM-IR with an ultra-high spatial resolution is carried out as shown in Fig. 4 in the main text.
+ Open protocol
+ Expand
8

FT-IR Spectroscopy of Powdered Samples

Check if the same lab product or an alternative is used in the 5 most similar protocols
Prior to measurements, powders were blended with dried KBr particles (95 °C, 4 h) and pressed as transparent pellets. Spectra were obtained with a Thermo Fisher Nicolet iS50 spectrometer in transmission mode from 400 to 4000 cm−1 with a spectral resolution of 4 cm−1, with 16 scans per spectrum.
+ Open protocol
+ Expand
9

Characterization of Pt-Ni Nanoparticles

Check if the same lab product or an alternative is used in the 5 most similar protocols
TEM images were conducted
on a FEI Tecnai G2 spirit operated at an accelerating voltage
of 120 kV. The real metal loading and composition of the Pt–Ni
NPs was measured by ICP optical emission spectrometry (ARCOS II MV
SPECTRO). XRD patterns were collected on a D8 ADVANCE-diffractometer
(Bruker) equipped with a LynxEye detector and KFL Cu 2K X-ray tube.
UV/vis spectroscopy was carried out on an Agilent Cary 5000 spectrometer.
The FTIR spectra were measured on a Thermo Scientific Nicolet iS50
spectrometer by placing a few drops of the solution on the surface
of a diamond cell.
+ Open protocol
+ Expand
10

FTIR Characterization of Porcine SIS Tissue

Check if the same lab product or an alternative is used in the 5 most similar protocols
Native (n = 3) and decellularized (n = 3) porcine SIS tissues were processed for Fourier transform infrared spectroscopy (FTIR) using a Nicolet iS-50 spectrometer (Thermo Fisher Scientific, Waltham, MA, USA) with an Attenuated Total Reflectance (ATR) accessory. The instrument was equipped with diamond/ZnSe crystal and pressure arm. Infrared spectra of the samples and background were collected using 64 scans in the range of 4000-500 cm−1 to characterize the composition of each group of samples.
Data were analysed using a Matlab® script (Mathworks, Natick, MA, USA) [108 ].
+ Open protocol
+ Expand

About PubCompare

Our mission is to provide scientists with the largest repository of trustworthy protocols and intelligent analytical tools, thereby offering them extensive information to design robust protocols aimed at minimizing the risk of failures.

We believe that the most crucial aspect is to grant scientists access to a wide range of reliable sources and new useful tools that surpass human capabilities.

However, we trust in allowing scientists to determine how to construct their own protocols based on this information, as they are the experts in their field.

Ready to get started?

Sign up for free.
Registration takes 20 seconds.
Available from any computer
No download required

Sign up now

Revolutionizing how scientists
search and build protocols!