Hb spectra were recorded in a JASCO-815 spectrometer (Tokyo, Japan) at 25°C using a 0.1 cm light path cuvette (200 µL) as described previously [30 (link)]. The Hb concentration was 5.2 µM in heme for measurement at the far UV-CD range from 200 to 250 nm. All experiments were carried out in PBS buffers.
815 spectrometer
Manufactured by Jasco
Sourced in Japan
The 815 spectrometer is a laboratory instrument designed to measure the absorption or transmission of light at specific wavelengths. It is a core analytical tool used in various scientific applications to identify and quantify the composition of samples.
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19 protocols using 815 spectrometer
1
Far-UV CD Spectra of Hemoglobin
2
Structural and Optical Characterization of a-C Thin Films
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The images of the C1 to C3 samples were obtained through HRTEM (JEOL‐JEM2010) with a standard focused ion beam, which can be used to perform Ga milling at 5–30 kV. XRD measurements were obtained using a Cu target for studying the structural properties of the samples. Furthermore, the MOA was obtained by using the JASCO 815 spectrometer. A 450‐W xenon lamp was used for irradiation, and the sample was set up in the middle of an electromagnet. To obtain the absolute spectra of the samples, the data were subtracted from the substrate and background signals. The MPC data were obtained using a two‐point electrode with a potential of 1 V in a Zahner Ennium electrochemical station. Raman spectroscopy was used to obtain information on the intensity of I(D)/I(G) for a‐C through a 532 nm Diode‐Pumped Solid‐State laser. The Zn K‐edge XANES spectra of bare ZnO NWs and the C1 to C3 specimens were collected using the BM‐Materials X‐ray study SP12B1 beamline at SPring‐8, Japan
3
Circular Dichroism Analysis of DksA
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DksA used for CD spectroscopy was oxidized or reduced as described in the pull-down assay section above. CD spectroscopy of 0.2 mg/mL DksA recombinant protein in 200 μL of 50 mM Tris⋅HCl buffer, pH 7.5, was performed at the Biophysics Core of the University of Colorado School of Medicine using a Jasco 815 spectrometer (Jasco) with constant nitrogen flushing at 37 °C. Each spectrum is the average of three independent scans.
4
Circular Dichroism Spectroscopy of Peptides
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Circular dichroism (CD)
spectra were recorded on a Jasco 815 Spectrometer using a 2 mm quartz
cell at 25 °C. Peptides (0.2 mg/mL) in CHCl3 were
prepared for measurements. All the spectra were obtained in the wavelength
region between 180 and 260 nm.
spectra were recorded on a Jasco 815 Spectrometer using a 2 mm quartz
cell at 25 °C. Peptides (0.2 mg/mL) in CHCl3 were
prepared for measurements. All the spectra were obtained in the wavelength
region between 180 and 260 nm.
5
Quadruplex-Chelerythrine Binding Dynamics
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Circular dichroism spectra were recorded on a Jasco 815 spectrometer at 25 °C. The CD spectra were recorded within a wavelength range 320 nm to 210 nm with a scan speed of 100 nm/min and step size of 1 nm. The band width was 1 nm. All measurements were carried out using a 1 mm path length cuvette in a reaction volume 350 μL. 10 μM of each quadruplex sequences (BCL2, KRAS and VEGFA) were titrated with increasing concentration (10 μM, 20 μM and 30 μM) of Chelerythrine upto a ratio of 1:3. Readings were noted 5 mins after each addition to ensure complete complex formation. DNA melting experiments were performed using the same cuvette and reaction mixture with the temperature being varied from 10 °C to 90 °C at an interval of 5 °C. 1:2 ratio of quadruplex-Chelerythrine (quadruplex: Chelerythrine = 1:2) complex were used for the CD melting experiment. All the CD melting experiments were repeated twice.
6
CD Spectroscopy of α-Synuclein Filaments
7
Thermal Melting Analysis of G-Quadruplexes
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Thermal melting analysis of all GQs was performed using circular dichroism (CD). CD spectra were recorded on a Jasco 815 spectrometer equipped with a Peltier-type temperature controller (CDF-4265/15) under nitrogen atmosphere to avoid water condensation. Scans were performed over wavelength range of 220-500 nm with a speed of 100 nm/min, and each spectrum represent an average of three scans with a band width of 1 nm. All measurements were carried out using 10 mm path-length cuvette. 2 μM of each GQ was added to TGP18 at a stoichiometry ratio of 1:1 and incubated for 10 min before spectra were recorded. DNA melting experiments were performed by varying temperature from 20 °C to 90 °C at an interval of 5 °C. All the CD melting experiments were repeated thrice. A blank sample containing 20 mM PBS solution (100 mM KCl, pH = 7.4) was used for baseline correction. For thermal denaturation of duplex (DM7) DNA, the absorption at 260 nm was monitored in the absence or presence of TGP18 over 20-90 °C (1 °C min-1, 5 °C intervals) using variable temperature mode in absorption spectroscopy. Melting temperature (Tm) was calculated from the first derivative of the absorption/temperature curve. Final analysis of the data was carried out by using Origin Pro 8.0.
8
Circular Dichroism Analysis of M-CoV-S Spike Protein
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Circular dichroism (CD) was used to monitor the secondary structure. All the major secondary structures of protein have a characteristic CD spectrum. M-CoV-S prefusion spike at a concentration of 200 µg/ml was used for CD spectroscopy using JASCO 815 spectrometer, Japan. The instrument was flushed with nitrogen for 2 minutes and the lamp was allowed to warm for 10 minutes. The temperature controller was set to 4°C. Spectrum was recorded at a bandwidth of 1 nm with a step size of 1 nm. Three measurements were made and then Yang’s reference spectra were used to estimate the relative proportions of different secondary structures using Spectra Manager software from JASCO. Further, for thermal analysis, the temperature was increased to respective temperature,20 ,21 (link) and spectra were recorded.
9
CD Spectra of Aβ Oligomers
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CD spectra were recorded on a Jasco 815 spectrometer from 190 to 250 nm with a data pitch of 0.2 nm, a bandwidth of 2 nm, and a scan speed of 50 nm/min with a 4-s response time. A 1-cm cell was used. After GdnHSCN-SEC fractionation using three columns in series equilibrated in 10 mM sodium phosphate at pH 8.5, spectra for CL Aβ40 and Aβ42 dimers, and trimers were acquired at 4 °C. CD data were analyzed using the SpectraManager program.
10
CD Analysis of Pu27-TPP Complex
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The CD spectra of Pu27 and the Pu27–TPP complex were monitored
using a Jasco 815
spectrometer. Pu27 (20 μM) was dissolved in
10 mM phosphate buffer containing 100 mM KCl at pH 7.0. CD titrations
of Pu27 with increasing concentration of TPP were
carried out at 25 °C using a cuvette of 0.1 cm path length. To
attain equilibration and ensure complete complex formation, each spectrum
was recorded after 5 min of addition of TPP. Each spectrum was scanned
from 220 to 310 nm with a scan speed of 100 nm/min. The data interval
was set at 1 nm with an average of 3 scans. All spectra were base
line corrected. To check the stabilization effect of TPP over Pu27, CD melting experiments were carried out. Pu27 (20 μM) was annealed separately in 10 mM phosphate buffer
containing 100 mM KCl at pH 7.0 and water (K+ < 1.5
mM) to find out the Tm of unbound-Pu27.
To conduct the melting of the Pu27–TPP complex
both in phosphate buffer containing 100 mM KCl and in water, TPP was
mixed with Pu27 in a 3:1 molar ratio. The thermal
melting was recorded from 20 to 95 °C for the Pu27–TPP complex in phosphate buffer and from 20 to 90 °C
for the Pu27–TPP complex in water. The temperature
interval was 5 °C with a ramp rate of 2.5 °C min–1. The sample was equilibrated for 3.0 min at each temperature before
data acquisition.
using a Jasco 815
spectrometer. Pu27 (20 μM) was dissolved in
10 mM phosphate buffer containing 100 mM KCl at pH 7.0. CD titrations
of Pu27 with increasing concentration of TPP were
carried out at 25 °C using a cuvette of 0.1 cm path length. To
attain equilibration and ensure complete complex formation, each spectrum
was recorded after 5 min of addition of TPP. Each spectrum was scanned
from 220 to 310 nm with a scan speed of 100 nm/min. The data interval
was set at 1 nm with an average of 3 scans. All spectra were base
line corrected. To check the stabilization effect of TPP over Pu27, CD melting experiments were carried out. Pu27 (20 μM) was annealed separately in 10 mM phosphate buffer
containing 100 mM KCl at pH 7.0 and water (K+ < 1.5
mM) to find out the Tm of unbound-Pu27.
To conduct the melting of the Pu27–TPP complex
both in phosphate buffer containing 100 mM KCl and in water, TPP was
mixed with Pu27 in a 3:1 molar ratio. The thermal
melting was recorded from 20 to 95 °C for the Pu27–TPP complex in phosphate buffer and from 20 to 90 °C
for the Pu27–TPP complex in water. The temperature
interval was 5 °C with a ramp rate of 2.5 °C min–1. The sample was equilibrated for 3.0 min at each temperature before
data acquisition.
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