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Spectrum 2000 ft ir spectrometer

Manufactured by PerkinElmer
Sourced in United States

The Spectrum 2000 FT-IR spectrometer is a laboratory instrument designed for the analysis of a wide range of samples. It utilizes Fourier Transform Infrared (FT-IR) technology to measure the absorption or transmission of infrared radiation by a sample, providing information about its molecular composition and structure.

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24 protocols using spectrum 2000 ft ir spectrometer

1

FTIR Analysis of Lipase Film Degradation

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Fourier
transform infrared spectra of the free lipase, CA, CA/IL 3%, and CA/IL5%
films before and after degradation under different conditions were
obtained by a PerkinElmer Spectrum 2000 FTIR spectrometer using the
attenuated total reflectance (ATR) mode. A total of 16 scans were
recorded in the wavenumber range of 600–4000 cm–1.5 (link)
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2

Characterization of Coordination Complexes

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The analyses of carbon, hydrogen, and nitrogen were determined on a Perkin Elmer elemental analyzer (Waltham, MA, USA). Conductivity measurements were measured in freshly prepared 10−3 M DMF solutions at room temperature using a PC 7000 conductivity cell (EUTECH, Tuas, Singapore). The IR spectra were recorded on a Spectrum 2000 FT-IR spectrometer (Perkin Elmer) in the range 4000–400 cm−1. 1H-NMR spectra were recorded with an Advance DPX-600 MHz spectrophotometer (Bruker, Elisabethhof, The Netherlands) in d6-DMSO and reported relative to TMS as an internal standard. Powder X-ray diffraction (XRD) pattern was recorded on a Bruker AXS D8 Advance powder X-ray diffractometer (X-ray source: Cu, λ = 1.5406 Ǻ). Thermal Decomposition of the Complexes were recorded on Thermogravimetric analyzer: TGA 4000 System (Perkin Elmer, Waltham, MA, USA). Electronic spectra were recorded on a model T80+ UV-Vis spectrometer (PG Instruments Ltd., Leicestershire, UK) in the range 200–800 nm. Melting points were recorded with a SMP 10 Melting Point Apparatus (Stuart, Chelmsford, UK).
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3

Isolation and Characterization of Madecassic Acid

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Madecassic acid (1) was purchased from Santa Cruz Biotechnology Inc., in over 95% purity. Other reagents and solvents were purchased from Sigma-Aldrich Co., Merck Co., and VWR Portugal and used without further purification. Solvents were dried over standard drying agents according to the usual procedures. Thin-layer chromatographic (TLC) analysis and preparative TLC were carried out on Kieselgel 60HF254 and Kieselgel 60HF254/Kieselgel 60G from Merck Co., respectively. Column chromatographic separations were performed using Kieselgel 60 (230–400 mesh) from Merck Co. Melting points were determined by using open capillary tubes on a Büchi B-540 melting point apparatus and are uncorrected. 1H, 13C, DEPT-135, HSQC, and HMBC NMR experiments were performed in CDCl3 or C6D6 and recorded on Bruker Avance 400 and Bruker Avance III spectrometers operating at 400 and 600 MHz for 1H and 100 and 150 MHz for 13C, respectively. The Bruker Avance III NMR spectrometer was equipped with a 3 mm cryogenically cooled probe. Spectra were calibrated to residual solvent signals at δH 7.26 and δC 77.16 (CDCl3) and δH 7.16 and δC 128.06 (C6D6). IR spectra were recorded on a PerkinElmer Spectrum 2000 FT-IR spectrometer using NaCl circular cell windows. HRESIMS were performed with an Agilent 6530B Accurate Mass QTOF mass spectrometer.
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4

FT-IR Analysis of Electrospun WG Fibers

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The electrospun WG protein fibers were dried for
at least 72 h using silica gel prior to FT-IR spectroscopy analysis.
The analysis was carried out using a Spectrum 2000 FT-IR spectrometer
(Perkin-Elmer Inc.) equipped with a single-reflection ATR (Golden
Gate, Speac Ltd.). A scanning resolution of 4.0 cm–1 and data from 32 scans were obtained between 4000 and 600 cm–1. Fourier self-de-convoluted curves were obtained
with the Spectrum software using an enhancement factor (γ) and
smoothing factor of 2 and 70%, respectively. A Savitzky–Golay
5-point second-order derivative analysis was done to find the underlying
corresponding peaks in order to determine the specific secondary structure.13 (link),26 (link) Amide I band was baseline corrected and peak fitting was performed
for 8–9 Gaussian peaks using the Fityk software.27 (link)
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5

NMR and FTIR Characterization of Samples

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1H Nuclear magnetic resonance (NMR) spectra were recorded on a JEOL 500 MHz NMR spectrometer (JEOL, Tokyo, Japan) at room temperature. The 1H NMR measurements were carried out with an acquisition time of 4.37 s, a pulse repetition time of 9.37 s and a 90° pulse width. Measurements were done with 16 scans and chemical shifts were referred to the solvent peak (δ = 4.79 ppm for deuterium oxide, D2O).
Fourier transform infrared (FTIR) spectra of the pellet samples were recorded on a Perkin Elmer Spectrum 2000 FTIR spectrometer (Perkin Elmer, Waltham, MA, USA); 64 scans were signal-averaged with a resolution of 4 cm−1 at room temperature. Pellets were prepared by coating the samples with potassium bromide.
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6

Comprehensive Physicochemical Characterization

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Optical rotations were measured on a PerkinElmer 241 polarimeter in a 100 × 2 mm cell. UV and IR spectRa were obtained using a Varian Cary 50 Bio UV–visible spectRophotometer and a PerkinElmer SpectRum 2000 FT-IR spectRometer, respectively. 1H, 13C, COSY, HSQC, HMBC, and ROESY experiments were performed in MeOH-d4 and acetone-d6 using a Bruker Avance III spectRometer operating at 600 MHz for 1H and 150 MHz for 13C and equipped with a 3 mm cryogenically cooled probe. SpectRa were calibrated to residual solvent signals at δH 3.31 and δC 49.0 (MeOH-d4). HPLC was performed using a Varian ProStar 218 solvent delivery module HPLC equipped with a Varian ProStar 325 UV–vis detector, operating under Star 6.41 chromatography workstation software. ESIMS studies were carried out on an Agilent 6130 Quadrapole LC/MS system.
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7

Photoactivatable Cbz-Leu and Boc-Ser Compounds

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All reagents were purchased from commercial suppliers and used as received. Compounds 2[14 (link)] and 3[15 (link)] were prepared by literature procedures from enantioenriched (> 98 %ee) Cbz-Leu-OH and Boc-Ser(OBn)-OH, respectively. NMR spectra were recorded on a Varian FT-NMR Mercury-400 Spectrometer. Mass spectra were recorded on a Waters ZQ2000 single quadrupole mass spectrometer using an electrospray ionization source. IR spectra were recorded on a Perkin Elmer Spectrum 2000 FT-IR Spectrometer. Enzymatic assays were conducted on a Tecan Infinite M200 or Tecan SPECTRAFluor Plus microplate reader. UV-vis spectra were recorded on a Varian Cary 50 spectrophotometer. The photolysis experiments were conducted using a 250 W Tungsten Halogen lamp (Osram Xenophot HLX) powered by a 24 V power source. The irradiation wavelength was selected by placing either a 395 nm long-pass filter (for white light experiments) or a 400 nm bandpass filter with a 345 nm long-pass filter (for quantum yield measurements) between the lamp and the sample, along with a 10 cm water cell to absorb infrared light. All reactions were performed under ambient atmosphere unless otherwise noted. Anaerobic reactions were performed by purging the reaction solutions with Ar or N2.
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8

Synthesis and Characterization of Novel Imidazo[1,2-a]pyridine Derivatives

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The chemical compounds ethyl imidazo[1,2-a]pyridine-2-carboxylate (1a), ethyl 3-nitroimidazo[1,2-a]pyridine-2-carboxylate (1b), imidazo[1,2-a]pyridine-2-carbonitrile (2a) and 3-nitroimidazo[1,2-a]pyridine-2-carbonitrile (2b) were prepared according to previously reported procedures.20 ,21 ,25 ,26
The quantities were scaled up in the range of grams to enable early evaluation in exploratory toxicology studies. The compounds were identified through their physical constants as well as spectroscopic data. IR spectra were obtained on a Perkin Elmer Spectrum 2000 FT-IR Spectrometer. Melting points were determined on an Electrothermal IA9000 melting point apparatus and were uncorrected. 1H and 13C NMR spectra were recorded in either deuterated chloroform (CDCl3) or deuterated dimethyl sulfoxide (DMSO-d6). Spectra were obtained on either a Varian Mercury NMR 300 MHz or a Varian NMR system 500 spectrometer.
The compounds imidazo[1,2-a]pyridine-2-carboxylic acid (3a), 3-nitroimidazo[1,2-a]pyridine-2-carboxylic acid (3b), and 2-(N-cyclopropyl)-3-nitroimidazo[1,2-a]pyridine (4) included in the present study were taken from the same batches reported previously during the investigation of anti-inflammatory activity.23 ,24
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9

Characterization of Platinum Complexes

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The C, H and N contents were determined using a CHN elemental analyzer, Vario Macro Elementary GMBH (Elementar Analysensysteme GMBH, Langenselbold, Germany). The IR spectra were measured on a PerkinElmer Spectrum 2000 FTIR spectrometer (PerkinElmer, Waltham, MA, USA) using KBr (400–4000 cm−1). The UV–Vis measurements for the determination of lipophilicity were obtained on a UVD-2950 UV–Vis spectrophotometer (Labomed, Los Angeles, CA, USA) using 1.0 cm pathlength quartz cuvettes (1.5 mL).
The NMR spectra were recorded at RT in DMF-d7 solutions with a Varian INOVA 500 (Varian Inc., Palo Alto, CA, USA) spectrometer operated at 499.8, 125.7, 50.6 and 107.4 MHz for 1H, 13C, 15N and 195Pt, respectively. The reference standards were TMS for 1H and 13C, CH3NO2 for 15N and K2PtCl6 for 195Pt. Gradient-enhanced IMPACT-HMBC 1H-(15N) correlation spectra [26 (link)] were optimized for a coupling constant of 6 Hz with the following experimental conditions: an acquisition time of 0.2 s, spectral windows of 6000 (F2) and 10,000 (F1) Hz, 1K complex data points, 256 time increments, 30 ms WURST-2 mixing sequence centered within a 60 ms preparation interval (ASAP2) and a 150° Ernst angle as the excitation pulse [27 (link)].
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10

FTIR Analysis of Scaffold Samples

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Scaffolds were analysed with a Spectrum 2000 FTIR Spectrometer (PerkinElmer, Massachusetts, USA) at wave numbers of 4000–650 cm−1 at 10 scans/second under a constant pressure of 120 psi and a single-reflection diamond MIRTGS detector. The stage for the sample was cleaned with methanol prior to analysis, and a background spectrum was obtained. The spectra obtained were plotted on OriginPro, and the formation of amide bonds was confirmed in the region 1600–1700 cm−1.
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