The asymmetric structure and structure change of WHP was determined by CD spectrum. WHP solution (3 mg/mL) was used in this study. The spectra were recorded in the far UV range (200–250 nm) with a 1 mm quartz cell on a J-810 CD spectrophotometer (JASCO Co., Tokyo, Japan). The setting conditions of CD spectra are as follows: the scanning rate of 60 nm/min, spectral resolution of 1 nm, response of 1 s, and bandwidth of 1 nm.
J 810 cd spectrophotometer
Manufactured by Jasco
Sourced in Japan
The J-810 CD spectrophotometer is a compact and efficient instrument designed for the measurement of circular dichroism (CD) spectra. It is capable of analyzing the absorption of circularly polarized light by chiral molecules, providing valuable information about the structural and conformational properties of various biomolecules, such as proteins and nucleic acids.
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Lab products found in correlation
Prominence uflc system, by Shimadzu (1 mentions)
Esi interface, by Shimadzu (1 mentions)
Nicolet nexus 470 ft ir spectrophotometer, by Thermo Fisher Scientific (1 mentions)
Lichroprep rp c18 gel, by Merck Group (1 mentions)
Silica gel, by Qingdao Marine Chemical (1 mentions)
400 mhz spectrometer, by Bruker (1 mentions)
Uv 2450 spectrophotometer, by Shimadzu (1 mentions)
Lc 20at pump system, by Shimadzu (1 mentions)
Spectra analysis software, by Jasco (1 mentions)
70 230 mesh, by Merck Group (1 mentions)
Microtof q mass spectrometer, by Bruker (1 mentions)
Amazon speed spectrometer, by Bruker (1 mentions)
Jms 600h mass spectrometer, by JEOL (1 mentions)
U 3200, by Hitachi (1 mentions)
8900 ft ir spectrophotometer, by Shimadzu (1 mentions)
Sephadex lh 20, by Cytiva (1 mentions)
Avance 400, by Bruker (1 mentions)
Avance 600, by Bruker (1 mentions)
Avance 500, by Bruker (1 mentions)
Quartz cuvette, by Jasco (1 mentions)
23 protocols using j 810 cd spectrophotometer
1
Circular Dichroism Analysis of WHP
2
Comprehensive Analytical Characterization
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Optical rotations were measured on a Rudolph Autopol IV automatic polarimeter (NJ, USA). ECD spectra were recorded on a JASCO J-810 CD spectrophotometer (JASCO, Japan). UV spectra were scanned using a Shimadzu UV-2450 spectrophotometer (Tokyo, Japan). IR spectra were obtained using a Thermo Nicolet Nexus 470 FT-IR spectrophotometer (MA, USA) with KBr pellets. The 1 H, 13 C, and 2D NMR spectra were obtained on a Bruker 400 MHz spectrometer (Bruker-Biospin, NEO, USA). The HRESIMS data were acquired from an LCMS-IT-TOF system equipped with a Prominence UFLC system and an ESI interface (Shimadzu, Kyoto, Japan). Silica gel (200-300 mesh, Qingdao Marine Chemical Inc., Qingdao, People's Republic of China), LiChroprep RP-C 18 gel (40-63 μm, Merck, Germany), and Sephadex LH-20 (Pharmacia, LA, USA) were employed for open column chromatography (CC). HPLC was carried out on a Shimadzu LC-20AT pump system (Shimadzu Corporation, Tokyo, Japan) equipped with an SPD-M20A photodiode array detector monitoring at 230 and 280 nm. A semi-preparative HPLC CAPCELL PAK C 18 column (250 × 10 mm, 5 μm), a CHIRALPAK IC column (4.6 × 150mm, 5 μm) and a CHIRALCEL OJ-H column (4.6 × 150mm, 5 μm) were employed for the isolation. TLCs were performed using pre-coated GF 254 plates. All purified compounds submitted for bioassay were at least 95% pure as judged by HPLC and supported by 1 H NMR analysis.
3
Circular Dichroism Analysis of RhaB1
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Circular dichroism (CD) spectra were acquired at the Research Technical Services from the University of Alicante, with a JASCO J-810 CD spectrophotometer at 25 ºC. Free RhaB1, GOC-RhaB1, GO-RhaB1 and GN-RhaB1 were prepared in sodium phosphate buffer 25 mM (pH 6.5)
and the spectra was recorded from 200 to 450 nm using 1 mm path length quartz cells, with a scan rate of 50 nm min '1 .
and the spectra was recorded from 200 to 450 nm using 1 mm path length quartz cells, with a scan rate of 50 nm min '1 .
4
CD Spectroscopy Analysis of 2AP DNA Constructs
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Samples containing 10 μm of the appropriate (2AP)2 DNA construct (Table 2 ), 50 mm Tris-HCl, pH 7.5, 100 mm KCl, 1 mm DTT and, where appropriate, 12.5 μm protein and either 10 mm CaCl2 or 10 mm CaCl2 + 25 mm EDTA were prepared with subsequent acquisition of CD spectra (300–480 nm) at 20 °C using a JASCO J-810 CD spectrophotometer as described in detail (17 (link)). The CD spectra were plotted as Δϵ per mol 2AP residue versus wavelength. Each measurement was independently repeated typically in triplicate.
5
Protein Structural Characterization by CD
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The recombinant proteins were dialyzed overnight at 4°C against CD-buffer (10 mM Tris pH 8.0 and 100 mM NaF). The samples were filtered through a 0.45 μm pore size filter (Spin X Costar) to remove precipitate and diluted to a final concentration of 0.15 mg/ml. Data was collected on a J-810 CD spectrophotometer (Jasco) at 25°C using a 1 mm path length cuvette using the following settings: sensitivity 100 mdeg, datapitch 0.5 nm, scan speed 50 nm/min, response 2.0 s, bandwidth 1 nm, accumulation three scans, units CD mdeg. Three sample scans were recorded and averaged. Three scans of buffer were also recorded, averaged and subtracted.
6
Circular Dichroism Spectroscopy of Mammalian RBD
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CD spectra were recorded in a J-810 CD spectrophotometer from Jasco analytical instruments equipped with a temperature-controlled Peltier system at 37±0.2°C. Spectra were measured in 0.2 mm path length cuvettes (50 μL of sample) and recorded using a scan rate of 100 nm/min, in high sensitivity mode between 200–250 nm (1.0 nm intervals). Total number of accumulations per spectra was set as five. The equipment is routinely calibrated with camphorsulfonic acid. A mammalian RBD standard was used as a reference protein for the CD analysis and secondary structure calculation (Cat: Pro1151-3, National Research Council, Ottawa, Canada). Secondary structural analyses were carried out using the BeStSel analysis server [19 (link)].
7
G4 DNA Structural Analysis by CD
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Each RNA was annealed 24 h before the CD study by heating the sample to 90 °C for 5 min in a buffer (10 mM Tris–HCl pH 7.0 and various concentrations of KCl) then slowly cooled to room temperature over 3 h and stored at 4 °C overnight. After adding each G4 ligand, samples were thoroughly mixed and equilibrated for 1 h before CD measurements. CD spectra were collected on a JASCO J-810 CD spectrophotometer using a quartz cuvette with a 1.0 mm path length. Each trace was the result of the average of four scans taken with a step size of 0.5 nm, a time-per-point of 1.5 s and a bandwidth of 2 nm. Using the JASCO Spectra Analysis software, spectra were converted to mean residue molar ellipticity and smoothed by the means-movement method using a convolution width of five. A blank sample, consisting only of buffer, was treated in an identical manner and subtracted from the collected data.
8
Thermal Unfolding Analysis of Proteins
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CD thermal unfolding measurements were performed using a Jasco J810 CD Spectrophotometer fitted with a computer-controlled Peltier temperature control unit, using protein solutions at 0.25 mg mL−1 in 100 mM NaPi pH 7.0 containing 1 mM NADPH cofactor. The protein solution was heated through a 5 °C ramp with a 5 min relaxation time between the recording of CD spectra at different temperatures from 20 to 80 °C. The unfolding curves were built by using the CD signal at 220 nm to obtain melting temperature values.
9
Far-UV CD Spectroscopy of Proteins
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Far‐UV CD spectra were collected on a JASCO model J810 CD spectrophotometer. All samples were buffered with 10 mM KPi, pH 7.2 at 30°C. Measurements were taken in a 0.5 cm path length curvette with a bandwidth of 2.5 nm and a step size of 0.5 nm from 210 to 260 nm. Three spectra were collected, averaged, and buffer subtracted for each sample with a total averaging time of 3 s per wavelength. A protein concentration of ~3 μM was used for wavelength scans.
10
Biophysical Characterization of Protein ETT 388_594
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LC ESI-TOF analysis was performed by the IBS-ISBG mass spectrometry platform on an Agilent Technologies 6210 spectrometer coupled to a capillary HPLC system (1100 series). The far-UV CD spectrum (from 190 nm to 260 nm) was collected on a JASCO J-810 CD spectrophotometer. The ETT 388_594 sample at 6.5 µM in Tris 5 mM pH 8.5 1 mM TCEP was scanned ten times at 20 °C in a 1 mm path-length cuvette. After subtraction of baseline buffer values, the CD signal, expressed in mdeg, was converted to mean molar residue ellipticity (expressed in deg.cm2.dmol-1). Data were plotted using Prism (GraphPad Software, San Diego). The thermal stability analysis involved heating ETT 388_594 in the same buffer used for CD for 20, 40 and 60 min, followed by centrifugation at 13,000 g, 10 min. Supernatants were loaded on SDS-PAGE with an unheated centrifuged reference sample, electrophoresed and analysed after staining with InstantBlue.
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