Mos 500 spectrophotometer

Manufactured by Bio-Logic

Sourced in France

The MOS-500 is a spectrophotometer designed for accurate and reliable measurements of light absorption and transmission in a variety of samples. It features a wide wavelength range, high-resolution optics, and advanced data processing capabilities. The core function of the MOS-500 is to quantify the concentration of specific analytes in a sample by measuring the amount of light absorbed or transmitted at specific wavelengths.

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Lab products found in correlation

Xevo g2 xs qtof mass spectrometer, by Waters Corporation (1 mentions) Jnm ecz400, by JEOL (1 mentions) Cpl 300 spectrophotometer, by Jasco (1 mentions) Tsq 8000 evo, by Thermo Fisher Scientific (1 mentions) Stadivari diffractometer, by STOE (1 mentions) Uv 6000 spectrophotometer, by Metash (1 mentions)

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MOS-500 (35 citations)

6 protocols using mos 500 spectrophotometer

Conformational Changes of DNA by CK

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CD spectra were recorded on a MOS-500 spectrophotometer (Bio-Logic, Seyssinet-Pariset, France). A total of 10 μM of DNA was dissolved in a buffer containing 40 mM of Tris-HCl (pH 7.6), 8 mM of MgCl₂, and 60 mM of KCl in the absence and presence of 100 μM of CK. Samples were incubated at 90 °C for 5 min and then cooled to 4 °C over 2 h. The CD spectra were recorded in the range of 230 to 350 nm at a scan speed of 100 nm·min⁻¹.
The CD melting experiments were conducted with a MOS-500 spectrophotometer (Bio-Logic, Seyssinet-Pariset, France). In the absence and presence of 100 μM of CK, 10 μM of DNA was dissolved in a buffer containing 40 mM of Tris-HCl (pH 7.6), 8 mM of MgCl₂, and 10 mM of KCl. After incubation at 90 °C for 5 min, all samples were annealed from 90 °C to 15 °C for 2 h. The ellipticities at 260 nm were recorded when samples were heated from 15 °C to 95 °C at a rate of 1 °C·min⁻¹.

Zhang Y., Qiu Z., Zhu M, & Teng Y. (2021). Ginsenoside Compound K Assisted G-Quadruplex Folding and Regulated G-Quadruplex-Containing Transcription. Molecules, 26(23), 7339.

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CD Spectroscopy of DNA-Ligand Interactions

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CD spectra were collected with MOS-500 spectrophotometer (bio-logic, France) at room temperature by using a quartz cuvette with a 1 mm path length. 10 μM DNA oligonucleotides and 20 μM 9CI dissolved in buffer (10 mM K₂HPO₄/KH₂PO₄, 100 mM KCl, pH 7.0) were used in the assay. The spectrum signals between 230 and 320 nm were scanned with 1 nm bandwidth at 1 nm/s.

Zhai Q., Gao C., Ding J., Zhang Y., Islam B., Lan W., Hou H., Deng H., Li J., Hu Z., Mohamed H.I., Xu S., Cao C., Haider S.M, & Wei D. (2019). Selective recognition of c-MYC Pu22 G-quadruplex by a fluorescent probe. Nucleic Acids Research, 47(5), 2190-2204.

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Far-UV CD Spectroscopy of Peptides

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The far-UV CD spectra were recorded in a 1 mm path length quartz cuvette at 25 °C from 190 nm to 240 nm wavelength range at every 0.5 nm. Biologic’s MOS-500 spectrophotometer was used for acquiring the spectral data of all the peptides except NSP11-CoV and NSP11-CoV2 peptides for which JASCO J-1500 spectrophotometer system was employed. In both spectrophotometer, spectral data were acquired by two/three consecutive acquisitions and the averaged spectra is reported. CD spectra of monomeric peptides were measured in their respective solvents (see Supplementary Table 11 for solvents). For DMSO soluble peptides, spectral data of monomers were not obtained due to high HT voltage values. Spectra of aggregated peptides were obtained after removing DMSO by washing the aggregates twice in 20 mM sodium phosphate buffer (pH 7.4). For NSP11-CoV2 peptide, 20 mM sodium phosphate buffer (pH 7.4) containing 50 mM NaCl was used. The spectrum of the buffer was used to normalize the spectrum of respective samples.

Bhardwaj T., Gadhave K., Kapuganti S.K., Kumar P., Brotzakis Z.F., Saumya K.U., Nayak N., Kumar A., Joshi R., Mukherjee B., Bhardwaj A., Thakur K.G., Garg N., Vendruscolo M, & Giri R. (2023). Amyloidogenic proteins in the SARS-CoV and SARS-CoV-2 proteomes. Nature Communications, 14, 945.

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Myosin Secondary Structure Analysis

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The secondary structure of the samples was determined as described previously
(Liu and Zhong, 2013 (link)) using an MOS
500 spectrophotometer (Bio-Logic, Claix, France). The heated samples were
adjusted to 0.1 mg/mL and placed in a quartz absorption cell with a 0.01 cm
optical path length. The spectra of the myosin samples were recorded at
25°C and from 190 to 250 nm at a scanning speed of 100 nm/min, and the
scanning interval time was 2 s. Circular dichroism (CD) is represented by the
average residue ellipticity [θ] (deg·cm²/dmol).
Dicroprot software package (IBCP, Lyon cedex, France) was used to calculate the
percentage content of the myosin secondary structure automatically.

Wei X., Pan T., Liu H., Boga L.A., Hussian Z., Suleman R., Zhang D, & Wang Z. (2020). The Effect of Age on the Myosin Thermal Stability and Gel Quality of Beijing Duck Breast. Food Science of Animal Resources, 40(4), 588-600.

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Physicochemical Characterization of Nanoclusters

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Dichloromethane was used as solvent to dissolve the nanoclusters for UV-vis spectroscopy and a time-dependent UV-vis test was performed using a Metash UV-6000 spectrophotometer. The X-ray photoelectron spectroscopy (XPS) test was performed on an ESCALAB 250 high-performance electron spectroscopy instrument with a monochromatic Al-Kα (1486.8 eV) excitation source. An electrospray ionization mass spectrometry (ESI-MS) test was performed with a Waters Xevo G2-XSQ-TOF mass spectrometer. Single-crystal X-ray diffraction (SCXRD) was carried out on a STOE STADIVARI diffractometer, using graphite-monochromated Cu Kα radiation (λ = 1.54186 Å). Circular dichroism was analysed on a Biologic MOS-500 spectrophotometer. Tests on photoluminescence including fluorescence quantum yield and fluorescence lifetime were measured on an FL-4500 fluorescence spectrometer with a relative optical density of 0.1. Circularly polarized luminescence properties were measured on a JASCO CPL-300 spectrophotometer. Nuclear magnetic resonance (NMR) spectra were measured using a JEOL JNM-ECZ400S. Gas chromatography-mass spectra (GC-MS) were measured using a Thermo Fisher TSQ8000EVO.

Zhou J., Yang X., Zheng P., Li Q., Li X., Chai J., Huang B., Yang S, & Zhu M. (2024). Construction of an Au12Cd2 nanocluster with circularly polarized luminescence by a metal- and ligand-exchange strategy. Chemical Science, 15(13), 4853-4859.

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Circular Dichroism Analysis of LLO Structures

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CD analysis was conducted using a MOS-500 spectrophotometer (Bio-Logic, Seyssinet-Pariset, France) to test the secondary structures of LLO treated with or without CT extract (128 μg/mL) [21 (link)]. The secondary structural changes (e.g., α-helix, beta sheet and beta turnover of LLO protein) were investigated using a BeStSel Web server [47 (link)]. All samples achieved normalized root mean square deviation values lower than 0.1.

Hou X., Sheng Q., Zhang J., Du R., Wang N., Zhu H., Deng X., Wen Z., Wang J., Zhou Y, & Li D. (2023). The Application of Cinnamon Twig Extract as an Inhibitor of Listeriolysin O against Listeria monocytogenes Infection. Molecules, 28(4), 1625.

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