The circular dichroism (CD) was used to monitor the folding of the peptides using a JASCO J-810 CD spectropolarimeter (Jasco Inc.) (Easton, MD, USA) over three scans between 190 and 260 nm using solutions of peptides (25 μM) in phosphate buffer (20 mM, pH 7.2) at room temperature. The data pitch and bandwidth were set to 1 nm with the scan rate 100 nm/min and a 1 s digital integration time. Temperature scans were performed using the same setting with a 2 °C temperature interval from 4 to 90 °C with a temperature gradient of 2 °C/min and an equilibration time of 60 s for scans at each temperature. Helicity (%)was calculated from the mean residue ellipticity (MRE) at 222 nm using the following equation: % helix = 100([ϴ]222/(−39,500(1 − 2.57/n))), where n is the number of residues [22 (link)].
J 810 cd spectropolarimeter
Manufactured by Jasco
Sourced in Japan, United States
The J-810 CD spectropolarimeter is a laboratory instrument used for measuring the circular dichroism (CD) of samples. It provides quantitative analysis of the structural and conformational properties of molecules, particularly proteins and other biomolecules. The instrument operates by measuring the difference in absorption of left and right circularly polarized light by the sample.
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Lab products found in correlation
Spectrum 100 ftir spectrometer, by PerkinElmer (2 mentions)
6545 quadrupole time of flight q tof mass spectrometer, by Agilent Technologies (1 mentions)
Uv 2450 uv vis spectrophotometer, by Shimadzu (1 mentions)
P 1030 polarimeter, by Jasco (1 mentions)
Spectrum bx, by PerkinElmer (1 mentions)
Lambda 40, by PerkinElmer (1 mentions)
Aqua c18 column, by Phenomenex (1 mentions)
Hplc system, by Waters Corporation (1 mentions)
Kinetex c18 column, by Phenomenex (1 mentions)
Pfd 425s, by Jasco (1 mentions)
Fft filter function, by Jasco (1 mentions)
Sigmaplot 12, by Merck Group (1 mentions)
1 mm quartz cuvette, by Hellma (1 mentions)
0.1 cm path length quartz cell, by Hellma (1 mentions)
Lambda, by PerkinElmer (1 mentions)
Spectra manager program, by Jasco (1 mentions)
Dynapro titan tc, by Wyatt Technology (1 mentions)
Dip 370 digital polarimeter, by Jasco (1 mentions)
Spectrum two ft ir spectrophotometer, by PerkinElmer (1 mentions)
Microtof electrospray mass spectrometer, by Bruker (1 mentions)
50 protocols using j 810 cd spectropolarimeter
1
Peptide Folding Monitored by Circular Dichroism
2
Circular Dichroism of BMAA and Aptamers
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Samples consisting of 10 μM BMAA, 10 μM aptamers (full-length and minimers), and aptamer/target mixtures (1 : 1 molar ratio, 30 min incubation at room temperature) were prepared in SB. Circular dichroism (CD) spectra were recorded on a Jasco J-810 CD spectropolarimeter (Jasco, Inc., Easton, MD) from 320 to 210 nm in a 1 mm path-length quartz cuvette at room temperature. Data gathered were the average of 5 scans collected in units of millidegrees (mdeg) versus wavelength at a scanning rate of 100 nm min−1. Scan of SB buffer alone was subtracted from the average scans of all samples.
3
Circular Dichroism Analysis of DDX1 Protein
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Secondary structure of DDX1 protein constructs was predicted with psipred (55 (link)) and analyzed by recording circular dichroism (CD) spectra from 200 to 260 nm using a Jasco J-810 CD spectropolarimeter (Jasco Corp.). A typical measurement was performed with 5 μM ( = 0.42 mg/ml) protein in 200 μl total volume of storage buffer and the cuvette was thermostated to 298 K. Melting curves were recorded at 222 nm by heating the sample cuvette from 293 K to 368 K at a rate of 1 K per min and potential refolding was monitored by returning to the start temperature. Melting curves were fitted to a two-state-unfolding equation (56 (link)).
4
Peptide Folding Monitored by Circular Dichroism
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The circular dichroism (CD) was used to monitor the folding of the peptides using a JASCO J-810 CD spectropolarimeter (Jasco Inc.) (Easton, MD, USA) over three scans between 190 and 260 nm using solutions of peptides (25 μM) in phosphate buffer (20 mM, pH 7.2) at room temperature. The data pitch and bandwidth were set to 1 nm with the scan rate 100 nm/min and a 1 s digital integration time. Temperature scans were performed using the same setting with a 2 °C temperature interval from 4 to 90 °C with a temperature gradient of 2 °C/min and an equilibration time of 60 s for scans at each temperature. Helicity (%)was calculated from the mean residue ellipticity (MRE) at 222 nm using the following equation: % helix = 100([ϴ]222/(−39,500(1 − 2.57/n))), where n is the number of residues [22 (link)].
5
CD Spectroscopy of Biomolecules
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CD spectra were recorded between 190-280 nm on Jasco J-810 CD spectropolarimeter (Jasco, Tokyo, Japan) using a quartz cell with 1 mm pathlength (Hellma Micro Absorption Cuvettes Z800015). The scan speed was set to 50 nm min -1 and the response time was 0.5 seconds. 5 successive spectra were recorded and averaged by the computer. All spectra were corrected for background contributions by subtracting appropriate buffer blanks. All experiments were performed at room temperature.
6
Spectroscopic Characterization of Organic Compounds
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Optical rotation was obtained on a JASCO P1030 polarimeter using a micro-cell (light path 1 cm). IR spectrum was taken on a PerkinElmer Spectrum 100 FT-IR spectrometer. UV spectra were recorded on Shimadzu UV-2450 UV–Vis spectrophotometer. CD spectra were taken on a JASCO J-810 CD Spectropolarimeter. HRMS spectra were measured on an Agilent 6545 Quadrupole-Time-of-Flight (Q-TOF) mass spectrometer. 1H, 13C, and 2D-NMR spectra were recorded on a Bruker 400 MHz and Varian VNMRS 700 MHz spectrometers and calibrated using residual non-deuterated solvent (CD2Cl2: δH = 5.32 ppm, δC = 53.84 ppm) as an internal reference.
7
Far-UV CD Spectroscopy of ClpC2 Variants
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Far-UV CD spectra of ClpC2 WT and ClpC2 variants R57A and R185A/R189A were recorded on a JASCO J-810 CD spectropolarimeter at a concentration of 8 µM. The spectra were measured at 23 °C in 50 mM Na2HPO4-NaH2PO4 (pH 7.4), 150 mM KCl in a 0.1 cm quartz cuvette. The recorded spectra were averages of 10 measurements and were corrected for buffer background.
8
Circular Dichroism Spectroscopy of Peptides
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CD spectra were obtained on a JASCO J-810 CD spectropolarimeter at room temperature as described previously [24 (link)]. Spectra representing the average of 16 scans from 250 to 190 nm were measured and all spectra were corrected for the baseline by subtracting control spectra of buffer alone. The molar ellipticity per residue was calculated as [mol deg x 100]/[no. of amino acids x pathlength (cm) x peptide concentration (moles/L)].
9
Circular Dichroism Spectroscopy of Proteins
10
CD Spectroscopy of Peptide Structure
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CD spectra of the peptides were recorded using quartz cells of 0.1 cm path length with a JASCO J-810 CD spectropolarimeter at 25°C, in the 260−190 nm spectral range, 1 nm bandwidth, 4 accumulations, and 50 nm/min scanning speed. The peptides were dissolved in H2O:TFE 1:1 (v/v) at a concentration of 200 μM. The secondary structure content of the peptides was predicted using the online server for protein secondary structure analyses BestSel (Miesonai et al., 2018 (link)).
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