The largest database of trusted experimental protocols

Spectrum 1

Manufactured by PerkinElmer
Sourced in United States

The Spectrum 1 is a Fourier Transform Infrared (FTIR) spectrometer designed for laboratory use. It provides accurate and reliable infrared spectroscopy measurements for a variety of applications. The core function of the Spectrum 1 is to analyze the absorption and transmission of infrared radiation by samples, enabling the identification and quantification of chemical compounds.

Automatically generated - may contain errors

8 protocols using spectrum 1

1

ATR-FTIR Analysis of ARTM Solid Dispersions

Check if the same lab product or an alternative is used in the 5 most similar protocols
By using potassium bromide (KBr) disc method (i.e., 0.5–1% of the sample in 200 mg KBr disc), ATR-FTIR spectra of SESDs of ARTM were obtained through Perkin Elmer spectrum 1. The scanning was at 400–4000 cm−1 and a resolution was then 1 cm−1. Instrument calibration was occasionally repeated during these operations.
+ Open protocol
+ Expand
2

FTIR Analysis of Phenytoin-AuPht Conjugates

Check if the same lab product or an alternative is used in the 5 most similar protocols
Pure phenytoin and lyophilized AuPht were prepared into pellets by mixing with KBr. They were then analyzed by the Perkin Elmer Spectrum1 FTIR spectrometer at a resolution of 1 cm-1 at a scan range of 450 to 4000 cm-1. The FTIR of the conjugate suspended in the above-mentioned physiologically relevant media incubated at 37°C for 24 hours at pH 7.4, was also performed to verify the interaction of phenytoin with the colloidal nanogold.
+ Open protocol
+ Expand
3

Comprehensive Analytical Procedures for Compound Characterization

Check if the same lab product or an alternative is used in the 5 most similar protocols
All solvents were purchased from Sigma Aldrich (Hy-Dry anhydrous solvents) and commercially available reagents were used as received. All reactions were followed by TLC analysis (TLC plates GF254, Merck) or LCMS (liquid chromatography mass spectrometry) using a Waters ZQ instrument. IR spectra were obtained on a Perkin Elmer Spectrum 1 machine. Melting points were measured with a Stuart SMP10, 230 V appartus and were uncorrected.
NMR spectra were recorded at ambient temperature using standard pulse methods on any of the following spectrometers and signal frequencies: Bruker AV-400 (1H = 400 MHz, 13C = 101 MHz), Bruker AV-500 (1H = 500 MHz, 13C = 125 MHz). Chemical shifts are reported in ppm and are referenced to tetramethylsilane (TMS) or the following solvent peaks: CDCl3 (1H = 7.27 ppm, 13C = 77.00 ppm), DMSO-d6 (1H = 2.50 ppm, 13C = 39.51 ppm) and MeOH-d4 (1H = 3.31 ppm, 13C = 49.15 ppm). Coupling constants are quoted to the nearest 0.1 Hz and multiplicities are given by the following abbreviations and combinations thereof: s (singlet), d (doublet), t (triplet), q (quartet), m (multiplet), br (broad). Column chromatography was performed on pre-packed silica gel columns (30-90 mesh, IST) using a biotage SP4. For detailed LCMS / MDAP / HRMS methodology see Supplementary Methods.
The purity of all compounds tested was determined by LCMS and 1H NMR to be > 95%.
+ Open protocol
+ Expand
4

Protein Secondary Structure Analysis of Lupin Flour

Check if the same lab product or an alternative is used in the 5 most similar protocols
Fourier Transform Infrared Spectroscopy (FTIR) was used to elucidate the protein secondary structure of the lupin’s flour and isolates. Data were collected using an equipment ATR-FTIR (Perkin Elmer, Spectrum 1, Norwalk, CA, USA), following the procedure described by [23 ] and analyzing Amide I region (1600–1690 cm−1), correspondent to the protein secondary structure, according to Jackson & Mantsch [24 (link)].
+ Open protocol
+ Expand
5

Yeast-Derived Extracellular Polysaccharide Characterization

Check if the same lab product or an alternative is used in the 5 most similar protocols
Extracellular polymeric substance (EPS) was isolated from culture supernatants of yeast species using acetone precipitation technique [25 (link)]. The carbohydrate composition of EPS was also determined using HPLC (chromatograph Waters, Milford, MA, USA) following the method of Simova et al. [26 (link)]. The dialysed EPS was characterized through infrared analysis using FT-IR spectrophotometer (Perkin Elmer Spectrum 1).
+ Open protocol
+ Expand
6

ATR-FTIR Analysis of Dried Crushed Samples

Check if the same lab product or an alternative is used in the 5 most similar protocols
After being dried at 40 °C for six hours, the sample was crushed in a coffee grinder. The sample underwent ATR-FTIR analysis (Spectrum 1, Perkin Elmer, Norwalk, VA, USA). Data on molecular spectrum emissions were gathered, adjusted for the air background, and then examined using the Spectrum program (ver. 5.3.0). The spectra were produced using the mid-IR (about 4000–8000) in absorption mode with a resolution of 4 cm−1 by 20 scans and a half-band width of 15 cm−1. Using published studies (De La Rosa-Millán, 2017; Chávez-Murillo et al., 2018) [33 (link),34 (link)] all chemical functional groups were identified.
+ Open protocol
+ Expand
7

FTIR Analysis of Iron Oxide Nanoparticles and Lawsonia inermis

Check if the same lab product or an alternative is used in the 5 most similar protocols
Fourier Transform Infrared Spectroscopy (FTIR) Spectroscopy was used to investigate the interactions between different species and changes in chemical compositions of the mixtures. The FTIR spectra of iron oxide nanoparticle using Lawsonia inermis leaf powder were recorded in Perkin Elmer spectrum 1 in diffuse reflection mode operating at a resolution of 4cm -1 , recorded between 4000 and 400cm -1
+ Open protocol
+ Expand
8

Analyzing Soy Protein Structure by ATR-FTIR

Check if the same lab product or an alternative is used in the 5 most similar protocols
A freeze-dried sample of SPI, a commercial SPI sample, and a soybean flour sample were analyzed in ATR-FTIR equipment (Perkin Elmer, Spectrum 1, Waltham, MA, USA). The samples were scanned from 650 to 4000 cm-1 at a resolution of 4 cm -1 , and the amide I band (1600-1700 cm -1 ) was evaluated with Spectrum software (v. 5.3.0). The amide I quantification of secondary structures was made according to Long et al. (2015) (link) and Zhao et al. (2008) (link) [37, 38] (link).
+ 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!