The CD measurements were implemented with a MOS-500 CD spectrometer (Bio-Logic, Grenoble, France), with a 1-mm light path cell, at room temperature. The CD spectra were recorded using a 2-mm bandwidth in the far-UV region (190–250 nm). The protein concentration was 0.1 mg/ml in 0.15 M phosphate buffer, pH 6.5. The UV–VIS spectra were obtained in the 200–700 nm region at room temperature using a DU 730 UV spectrophotometer (Beckman Coulter, Brea, CA, USA), and the protein concentration was 0.5 mg/ml in 0.15 M phosphate buffer, pH 6.5.
Mos 500 cd spectrometer
Manufactured by Bio-Logic
Sourced in France
The MOS-500 CD spectrometer is a laboratory instrument designed to measure circular dichroism (CD) in samples. It is used to analyze the structural characteristics of molecules, particularly proteins and other biomolecules. The MOS-500 CD spectrometer provides accurate and reliable data on the secondary structure and folding of these molecules.
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9 protocols using mos 500 cd spectrometer
1
Protein Characterization by CD and UV-VIS
2
Spectroscopic Characterization of Dye-Decolorizing Peroxidases
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Far-UV CD spectra measurements were implemented with a MOS-500 CD spectrometer (Bio-Logic, Grenoble, France), with a 1-mm light path cell. The protein concentration was 0.1 mg mL−1 in 0.15 M phosphate buffer at pH 6.5. The CD spectra were recorded using a 2-mm bandwidth in the far-UV region (190–250 nm) at room temperature.
UV–Vis spectra were obtained in the 200–700 nm region at room temperature using a DU 730 UV spectrophotometer (Beckman Coulter, Brea, CA, USA); the Il-DyP4 concentration was 0.58 mg mL−1 in 0.1 M phosphate buffer at pH 6.0 and that of Il-MnP6 was 1.26 mg mL−1 in 0.1 M sodium acetate buffer at pH 5.9.
UV–Vis spectra were obtained in the 200–700 nm region at room temperature using a DU 730 UV spectrophotometer (Beckman Coulter, Brea, CA, USA); the Il-DyP4 concentration was 0.58 mg mL−1 in 0.1 M phosphate buffer at pH 6.0 and that of Il-MnP6 was 1.26 mg mL−1 in 0.1 M sodium acetate buffer at pH 5.9.
3
Circular Dichroism Spectroscopy of YbiB and ObgE
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For CD measurements, a MOS-500 CD spectrometer (BioLogic) was used. Spectra were recorded using a 1 mm cuvette and a slit bandwidth of 1 nm. All measurements were performed at 25°C in a buffer containing 20 mM Tris pH 7.5, 150 mM NaCl and 5 mM MgCl2. For each sample, three repeat measurements were collected. The spectra of the YbiB and ObgE peptide1 (SBL-OBGE-01, Supplementary Table S3 ) samples were measured at a concentration of 13.3 μM, while the complex sample was prepared by mixing 13.3 μM YbiB with 13.3 μM peptide1. The final CD spectra (expressed in ellipticity θ) were obtained after subtraction of the buffer spectrum.
4
Secondary Structure Analysis of ZHs
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The change in the secondary structure of ZHs was measured using an MOS-500 CD spectrometer (Bio-Logic, Seyssinet-Pariset, France) under a constant nitrogen atmosphere in a quartz cuvette with a 0.1 cm path length over a scanning range of 180–260 nm. The step resolution was 1 nm, and the scanning speed was 60/min. The value of the 10 mmol/L PBS solution was subtracted from all CD spectral data. The change in the secondary structure of ZHs was calculated using CdtoolX (version 2.01) secondary structure estimation software [55 (link)].
5
Conformational Study of BmADK Enzyme
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CD spectra were collected on a MOS-500 CD spectrometer (BioLogic, Seyssinet-Pariset, France) with a 0.05 cm quartz cuvette at 25 °C in 190–250 nm using standard procedures. BmADK was dissolved in 20 mM Tris-HCl, 150 mM NaCl, pH 8.0 buffer to 0.345 mg/mL. The effects of pH on the secondary structure of BmADK were recorded in the pH range of 3.0–11.0. The thermal denaturation of BmADK was performed from 10 to 87.5 °C at an incremental step of 2.5 °C. The mean residue ellipticity at 222 nm was used to characterize the structural changes of BmADK induced by temperature and pH after subtraction of baseline corrections. Each test was repeated in triplicate. The mean residue ellipticity was the arithmetic mean of three independent tests.
6
Circular Dichroism Analysis of Protein-Nanoparticle Complex
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CD measurements were performed on a BioLogic scanning MOS-500 CD spectrometer using a quartz cuvette of 1 mm path length. The final protein concentration of 5 μM protein and 0.025 nM Ag IMNPs in 20 mM sodium phosphate buffer pH 7.4 was used for recording the data. The spectra were averaged over three scans and blank subtracted data were plotted using Origin software.
7
Circular Dichroism Analysis of Protein Hydrolysate
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After resuspending the T. molitor protein hydrolysate (0.01%, w/v) in deionized water, the secondary structure of the protein peptides was analyzed by a MOS-500 CD spectrometer (Bio-Logic, Seyssinet-Pariset, France) in the range of 190–250 nm. The scan speed was 100 nm/min, and the path length was 1 mm. The ellipticity (θ) was measured in millidegrees (mdeg).
8
Circular Dichroism Spectroscopy of DNA-Ligand Interactions
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Circular dichroism (CD) spectra were recorded on a MOS-500 CD spectrometer (Bio-Logic Science Instruments, France) using a quartz cuvette with a path length of 2 mm. The scanning speed was 200 nm/min, and the response time was 0.5 s. The presented spectra were the average of three scans. The DNA solution was mixed with ligand at the specified concentration in 0.02 M Tris–HCl buffer (pH 7.0) containing 0.1 M KCl or LiCl, and the resulting solution was incubated for 30 min at room temperature before the CD measurement.
9
Structural Characterization of YCH Biopolymer
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The YCH was structurally characterized using circular dichroism (CD) spectroscopy using a MOS-500 CD spectrometer (Bio-Logic Science Instruments). The YCH solution (0.1 mg/mL) was prepared in deionized water. Parameters were as follows: wavelength range, 190-250 nm; scan speed, 100 nm/min; path length, 1 mm. Ellipticity (θ) was measured in millidegrees (mdeg).
The conformational change of the YCH was assessed by ANS fluorescence spectroscopy. The YCH was dissolved in phosphate buffer (pH 7.0, 10 mM) at a concentration of 1 μg/mL. Then, 20 μL of 8 mM ANS was mixed with 1.5 mL of the YCH solution, and the fluorescence spectrum was recorded using an F-2500 fluorescence spectrometer (Hitachi Ltd.) in a wavelength range from 400 to 700 nm.
The molecular weight distribution of the YCH was further analyzed, as described previously (Sun et al., 2021) (link). In brief, the mobile phase was composed of acetonitrile, water, and trifluoroacetic acid (45/55/0.1, vol/vol/vol). The YCH was dissolved in the mobile phase and filtered through a 0.45-μm filter. Then, the YCH solution was loaded on a TSK gel G2000 SWXL (300 × 7.8 mm internal diameter) column (Tosoh) for separation at a flow rate of 0.5 mL/min under a detection wavelength of 220 nm. The standards of cytochrome C, aprotinin, bacitracin, Gly-Gly-Tyr-Arg, and Gly-Gly-Gly were used to prepare a calibration curve of molecular weight.
The conformational change of the YCH was assessed by ANS fluorescence spectroscopy. The YCH was dissolved in phosphate buffer (pH 7.0, 10 mM) at a concentration of 1 μg/mL. Then, 20 μL of 8 mM ANS was mixed with 1.5 mL of the YCH solution, and the fluorescence spectrum was recorded using an F-2500 fluorescence spectrometer (Hitachi Ltd.) in a wavelength range from 400 to 700 nm.
The molecular weight distribution of the YCH was further analyzed, as described previously (Sun et al., 2021) (link). In brief, the mobile phase was composed of acetonitrile, water, and trifluoroacetic acid (45/55/0.1, vol/vol/vol). The YCH was dissolved in the mobile phase and filtered through a 0.45-μm filter. Then, the YCH solution was loaded on a TSK gel G2000 SWXL (300 × 7.8 mm internal diameter) column (Tosoh) for separation at a flow rate of 0.5 mL/min under a detection wavelength of 220 nm. The standards of cytochrome C, aprotinin, bacitracin, Gly-Gly-Tyr-Arg, and Gly-Gly-Gly were used to prepare a calibration curve of molecular weight.
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