CD spectra of HSA in the absence and presence of SSD/PF were measured by a MOS 450 automatic spectropolarimeter (BioLogic Science Instruments, Claix, France). HSA at a concentration of 1 μM was used. The ratio of HSA, SSD and PF was 1:1:1. A scan rate was set as 30 nm per minute with a response time of 4 s.
Mos 450
Manufactured by Bio-Logic
Sourced in France
The MOS-450 is a laboratory equipment designed for analytical applications. It features a multi-channel data acquisition system capable of monitoring and recording various electrical signals.
Automatically generated - may contain errors
Lab products found in correlation
Ar 1500ex, by TA Instruments (2 mentions)
Synapt g2 qtof mass spectrometer, by Waters Corporation (2 mentions)
Lc 6ad, by Shimadzu (2 mentions)
Bi 200sm, by Malvern Panalytical (1 mentions)
Zetapals, by Brookhaven Instruments (1 mentions)
Uv 2550, by Shimadzu (1 mentions)
Jem 100cx, by JEOL (1 mentions)
Phi 5000c esca system, by PerkinElmer (1 mentions)
Tensor 27, by Bruker (1 mentions)
Jem 2100f, by JEOL (1 mentions)
Avance 600 nmr spectrometer, by Bruker (1 mentions)
Pharmaspec uv 1700 uv visible spectrophotometer, by Shimadzu (1 mentions)
Avance 400, by Bruker (1 mentions)
Ifs 55 spectrometer, by Bruker (1 mentions)
Cary eclipse, by Agilent Technologies (1 mentions)
Fts 6000 spectrometer, by Bio-Rad (1 mentions)
Uv 1800 spectrophotometer, by Shimadzu (1 mentions)
Tcc 240a uv vis spectrophotometer, by Shimadzu (1 mentions)
Avance 400 mhz nmr spectrometer, by Bruker (1 mentions)
Dsc 204, by Netzsch (1 mentions)
35 protocols using mos 450
1
CD Spectra of HSA with SSD/PF
2
CD Measurements of HSA with and without SSC
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CD measurements of HSA with and without SSC were recorded using a MOS 450 automatic spectropolarimeter (BioLogic Science Instruments, Claix, France) equipped with 1.0 cm quartz cells at 26 °C, over the scan range of 200–350 nm, at a scan rate of 30 nm/min with a response time of 4 s. Data were corrected using the signal of the buffer solution.
3
Far-UV CD Analysis of Protein Structures
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CD spectra were scanned at the far-UV range (190–250 nm) with a CD spectrometer (Model: MOS-450, Bio-Logic Science Instruments) in a 10-mm-pathlength quartz CD cuvette at 4°C and 37°C. The protein concentrations for the CD analysis were 94.5 μg/ml (MBP-Q25) and 104.2 μg/ml (MBP-Q72), respectively. The recombinant proteins were dissolved in 10 mM NaH2PO4/Na2HPO4 buffer (pH 7.4). Three scans were averaged to obtain one spectrum. The CD results were expressed in terms of mean molar ellipticity [θ] (degrees·cm2·dmol−1) plotted against the wavelength. The collected data were then analyzed by DICROPROT software23 (link) and the estimation of the secondary structure was done by the linear regression method developed by Chang et al.19 (link) and integrated into the DICROPROT program.
4
Hydrogel Characterization and Stability
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The size distribution, UV‐vis absorption spectra, zeta potential, and CD spectra of hydrogels were measured on a dynamic light scattering spectrometer (BI‐200SM; Malvern), UV‐vis spectrophotometer (UV‐2550; Shimadzu), zeta potential analyzer (ZetaPALS; Brookhaven), and BioLogic (MOS‐450) system, respectively. The rheology test was used to study the formation, stability, and viscoelasticity by a rheometer (AR 1500ex; TA Instruments). Moreover, the micromorphology was characterized by TEM. Then PM‐nano was dispersed and incubated in serum at 37°C for 24 hours. The mixture was imaged by TEM at the predetermined time point to evaluate the structure stability.
5
Characterizing Lira Secondary Structures
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The secondary structures of Lira with or without copolymers were characterized by circular dichroism instrument (Bio-Logic MOS-450, Bio-Logic). Spectra were recorded from 200 to 280 nm using a bandwidth of 1 nm and a scanning rate of 1 nm/s. Aqueous polymer solutions without Lira were also scanned in the same wavelength range as the blank background.
6
Multimodal Characterization of Materials
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TEM images were collected using the JEM-100 CX (Jeol Ltd., Tokyo, Japan) instrument. The XPS measurements were obtained by a PHI-5000 CESCA system (PerkinElmer) with radiation from an Al Kα (1486.6 eV) X-ray source. Element mapping images results were collected by a JEM-2100F (Jeol Ltd., Tokyo, Japan) transmission electron microscope. IR spectra were obtained by a IR spectrophotometer (TENSOR 27, Bruker, German). The CD spectra were obtained by a spectropolarimeter system (BioLogic, MOS-450).
7
Circular Dichroism Analysis of Protein
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8
Circular Dichroism Analysis of UCU-CAT Interaction
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Circular dichroism changes of UCU (in the absence or presence of CAT) or its ESU (or ESUC) in buffer-A to -D was determined using a CD spectrophotometer (MOS-450, Bio-Logic). Briefly, UCU (200 μg/mL) or UCU in the presence of CAT (i.e., the mixture of 100 μg/mL UCU and 100 μg/mL CAT) was separately determined. The emission fluorescence intensity was recorded from 185–260 nm. For the enzymosome of UCU in the absence or presence of CAT, chloroform was added and it was tested in the way described above.
9
Protein Secondary Structure Analysis
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CD spectra were used to evaluate the secondary structures and structural changes of proteins. The secondary structures of purified PHTI dissolved in deionized water with Fe3+ (0 to 100 μM) were measured by Bio-Logic MOS-450 (Grenoble, France) at room temperature. The spectra were recorded from 190 nm to 250 nm, with a response time of 2 s and scan speed of 100 nm/min. Quartz cuvettes of 1 cm were used. CDPro software was used to analyze the secondary structure and the data of all CD measurements were calculated in triplicate.
10
Spectroscopic Characterization of Compounds
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UV spectra were recorded on a Shimadzu UV-1700 PharmaSpec UV-visible spectrophotometer. The 1H, 13C, and 2D nuclear magnetic resonance (NMR) spectra were measured by a Bruker AVANCE-600 NMR spectrometer (Rheinstetten, Germany) with tetramethylsilane (TMS) as an internal standard. HRESIMS data were acquired using a Waters Synapt G2 QTOF mass spectrometer (Milford, CT, USA). ECD spectra were taken on a Biologic MOS-450. Optical rotations were measured using a JASCO VP-1020.
For column chromatography (CC), silica gel (100–200 and 200–300 mesh, Qingdao, China), Sephadex LH-20 (Uppsala, Sweden) and ODS (60–80 μm, Tokyo, Japan) was used. The analytical HPLC was obtained with an Agilent 1200 (CA, USA) with a DAD detector using a reversed-phase C18 column (5 μm, 250 × 4.60 mm). Semi-preparative HPLC was performed on a Shimadzu LC-6AD (Kyoto, Japan) equipped with a UV SPD-20A detector using a reversed-phase C18 column (5 μm, 250 × 10 mm).
For column chromatography (CC), silica gel (100–200 and 200–300 mesh, Qingdao, China), Sephadex LH-20 (Uppsala, Sweden) and ODS (60–80 μm, Tokyo, Japan) was used. The analytical HPLC was obtained with an Agilent 1200 (CA, USA) with a DAD detector using a reversed-phase C18 column (5 μm, 250 × 4.60 mm). Semi-preparative HPLC was performed on a Shimadzu LC-6AD (Kyoto, Japan) equipped with a UV SPD-20A detector using a reversed-phase C18 column (5 μm, 250 × 10 mm).
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