J 1500 cd spectrometer

Manufactured by Jasco

Sourced in Japan, United States, Germany, United Kingdom

The J-1500 CD spectrometer is a laboratory instrument designed for the measurement of circular dichroism (CD) spectra. It provides accurate and reliable CD data across a wide wavelength range. The J-1500 is capable of measuring the differential absorption of left and right circularly polarized light by chiral molecules, which is a fundamental property of many biological and chemical samples.

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Close spelling variants of this product

J-1500 (162 citations) J-1500 spectrometer (62 citations) CD spectrometer (22 citations) Jasco 1500 CD spectrometer (6 citations) J-1500 CD (5 citations) J-1500 High Performance CD spectrometer (5 citations) J-1500 KS CD spectrometer (2 citations)

165 protocols using j 1500 cd spectrometer

Thermostability and pH-dependent Structure of TaTPI

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Temperature of maximum heat capacity (or half-denaturation temperature, Td) of TaTPI was measured by CD spectroscopy. Experimental sample was prepared following purification and concentration of TaTPI proteins to 0.4 mg ml^-1 containing 50 mM HEPES, pH 7.5. CD traces of TaTPI were obtained at 222 nm using the J-1500 CD spectrometer (JASCO) at a scanning rate of 1°C min^-1. The denaturation curve of TaTPI was analyzed by Kaleidagraph (Synergy Software) based on John and Weeks’s protocol [22 (link)].
Effect of pH variation on the secondary structure of TaTPI was also monitored by CD spectroscopy. pH of protein solutions containing 20 mM Tris-HCl and 200 mM NaCl was adjusted to desired values between pH 1.0 and pH 7.0 with HCl for CD measurements. The baseline signal was measured with a buffer containing 20 mM Tris-HCl, pH 7.5, and 200 mM NaCl. CD spectra of pH-titrated TaTPI were recorded and averaged over two scans between 200 to 260 nm using J-1500 CD spectrometer (JASCO). The secondary structure contents of TaTPI were calculated by Multivariate SSE Program (JASCO).

Park S.H., Kim H.S., Park M.S., Moon S., Song M.K., Park H.S., Hahn H., Kim S.J., Bae E., Kim H.J, & Han B.W. (2015). Structure and Stability of the Dimeric Triosephosphate Isomerase from the Thermophilic Archaeon Thermoplasma acidophilum. PLoS ONE, 10(12), e0145331.

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Spectroscopic Characterization of Tistrellabactin

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UV–visible spectra
were obtained on an Agilent Technologies Cary 300 UV–vis spectrometer.
NMR spectroscopy was carried out at 25 °C on a Bruker 500 MHz
spectrometer equipped with a Prodigy cold probe (¹H, ¹³C, ¹H–¹³C multiplicity edited
HSQC, ¹H–¹H COSY, ¹H–¹³C HMBC, ¹H–¹⁵N HMBC, ¹H–¹⁵N HSQC, TOCSY, NOESY). NMR spectra for characterization
were collected in DMSO-d₆, and spectra
of the photoproduct were collected in 50 mM Na₂HPO₄-buffered D₂O (pD 8.0). Spectra were indirectly
referenced by the residual solvent peak or ²H lock. MS
analysis was carried out on a Waters Xevo G2-XS QTOF with positive
mode electrospray ionization coupled to an AQUITY UPLC-H-Class system
with a Waters BEH C18 column. Samples were run with a linear gradient
of 0% to 100% acetonitrile (0.1% formic acid) in ddH₂O
(0.1% formic acid) over 10 min. IR data were collected on a Bruker
Alpha FTIR spectrophotometer. CD data were collected on a JASCO J-1500
CD spectrometer on tistrellabactin A (71 μM) and tistrellabactin
B (52 μM) in Na₂HPO₄ (pH 8). CD data was
referenced to the buffer and collected with a scan rate of 20 nm/min,
DIT 8 s bandwidth of 1 nm, and data pitch of 0.5 nm. Deionized water
was dispensed from a Milli-Q IQ 7000 water purification system (Resistivity
18.2 MΩ). All glassware was acid-washed with 4 M HCl and subsequently
rinsed with Milli-Q water.

Makris C., Leckrone J.K, & Butler A. (2023). Tistrellabactins A and B Are Photoreactive C-Diazeniumdiolate Siderophores from the Marine-Derived Strain Tistrella mobilis KA081020-065. Journal of Natural Products, 86(7), 1770-1778.

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Circular Dichroism Analysis of Protein Thermostability

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CD experiments were performed on a Jasco J-1500 CD spectrometer using 300 µl cuvettes with 1 mm path length. All measurements were acquired in 20 mM sodium phosphate buffer at pH 8.0 or pH 5.5 at 10 µM protein concentration. Spectra were recorded from 260 to 185 nm, first at 25°C, then after heating for 15 min at 95°C and finally after cooling down to 25°C. 5 scans were recorded for each temperature to calculate an average spectrum. For temperature melting curves, the CD intensity at 222 nm was monitored between 25 and 95°C with 1°C/min increase.

Šede M., Fridmanis J., Otikovs M., Johansson J., Rising A., Kronqvist N, & Jaudzems K. (2022). Solution Structure of Tubuliform Spidroin N-Terminal Domain and Implications for pH Dependent Dimerization. Frontiers in Molecular Biosciences, 9, 936887.

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Far-UV CD Spectroscopy of Peptides

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CD studies were performed with a Jasco J-1500 spectrometer (ABL and E-JASCO Polska, Cracow, Poland). Far-UV CD experiments were performed using a J-1500 CD spectrometer (Jasco). The samples were prepared in a phosphate buffer solution, pH 7.2, concentration 0.1 mg/mL (1 mg of each analyzed peptide was dissolved in 10 mL of buffer solution). All studies were carried out at ambient temperature. The dissolved samples were loaded in a rectangular quartz cuvette (1 mm path length, Hellma). Spectra were collected in the range of 190–270 nm. Other experimental settings were as follows: Data pitch, 5 nm; scanning mode, continuous; scanning speed, 100 nm/min; bandwidth, 3 nm; integration time, 1 s.

Swiontek M., Fraczyk J., Wasko J., Chaberska A., Pietrzak L., Kaminski Z.J., Szymanski L., Wiak S, & Kolesinska B. (2019). Search for New Aggregable Fragments of Human Insulin. Molecules, 24(8), 1600.

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Thermal Stability and Kinetics of Enzyme

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Protein was concentrated to 10 μM in 50 mM sodium phosphate buffer. Absorbance was measured at 222 nM using a Jasco J-1500 CD Spectrometer at temperature increments of 2 °C from 22 °C to 60 °C, with 2 min of equilibration per temperature. Absorbance was measured twice per temperature, and this procedure was repeated 3 times on separate days. Proportion of folded protein and T_m were estimated using a 2-state 5-parameter logistic regression curve. Initial reaction rates were measured as reduced nicotinamide-adenine dinucleotide (NADH) coproduct formation (340 nm) for the first 90 s of reaction after enzyme addition at saturating conditions (500 nM NADH, 1 mM NAD, 200 mM alcohol, 50 mM KaPO4 buffer, pH 7.6). Effect of reaction temperature was assessed by incubating the reaction mixture for 1 h at 22 °C, 30 °C, or 37 °C and then adding the enzyme, which had been incubated at 22 °C. Effect of heat treatment on activity was measured by first incubating enzyme at temperatures ranging from 22 °C to 50 °C for 1 h and then adding the enzyme to reaction mixtures that had been incubated at 22 °C; 10 to 15 replicates were assessed for each enzyme−temperature combination. Effects of genotype, temperature, and genotype−temperature interaction on reaction rate were estimated by linear regression (lm() function) in R.

Siddiq M.A, & Thornton J.W. (2019). Fitness effects but no temperature-mediated balancing selection at the polymorphic Adh gene of Drosophila melanogaster. Proceedings of the National Academy of Sciences of the United States of America, 116(43), 21634-21640.

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Circular Dichroism Analysis of Aptamer-OTC Interactions

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CD measurements were performed on a Jasco J-1500 CD Spectrometer in photometric mode. The measurement range was 200–320 nm, with 2 nm bandwidth and spectra taken at 50 nm/min scanning speed during the OTC titration experiments. The sample holder was thermostated at 25 °C. Buffer solutions without any aptamer or OTC were used for baseline correction. The denaturation measurements were performed without baseline correction. The scanning speed was set at 100 nm/min, the temperature was increased at a rate of 2 °C/min between 4 and 100 °C and spectra were taken at every 2 °C.
For titration, 500 µL of 5 µM aptamer solution was pipetted into a 5 mm quartz cuvette. An aqueous solution of OTC was pipetted into the aptamer solution to obtain concentrations of 2.5, 5, 10, 20 and 40 µM. Before the CD measurement, the solutions were gently shaken and incubated at room temperature for 5 min.
Denaturation experiments were carried out using 1000 µL of 5 µM aptamer solution alone and with 40 µM OTC in a 5 mm quartz cuvette with a PTFE lid. In addition, 100 µL paraffin oil was layered on top of the solution to minimize evaporation.

Jakab K., Melios N., Tsekenis G., Shaban A., Horváth V, & Keresztes Z. (2023). Comparative Analysis of pH and Target-Induced Conformational Changes of an Oxytetracycline Aptamer in Solution Phase and Surface-Immobilized Form. Biomolecules, 13(9), 1363.

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Circular Dichroism Analysis of Protein Structure

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Secondary structures of MSlys and Pal were analyzed by circular dichroism (CD) spectroscopy in the far-UV region (190−260 nm), using a Jasco J-1500 CD spectrometer as performed previously [22 (link)]. Secondary structure estimation was made using CDSSTR [23 (link)] and CONTINLL [24 (link)] routine of the DICHROWEB [25 (link)], and the analysis complemented using PSIPRED [26 (link)].

Silva M.D., Oliveira H., Faustino A, & Sillankorva S. (2020). Characterization of MSlys, the endolysin of Streptococcus pneumoniae phage MS1. Biotechnology Reports, 28, e00547.

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Analysis of secondary structure in MPs-fermentation-stinky compound complexes

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The samples were prepared with the same treatment as the above fluorescence samples. In particular, the 8 mg/L samples were used to render the changes in the relative percentage of the secondary structure. The secondary structure (α-helix, β-sheet, β-turns, and random coil) of MPs-fermentation-stinky compound complexes was determined using the J-1500 CD spectrometer (JASCO, Tokyo, Japan). The scan range was 200–260 nm at 297 K. High-purity nitrogen was purged from gas at a rate of 5 L/min. The HT voltage was 300–600 V. The secondary structures of α-helix, β-sheet, β-turns, and random coils of MPs-fermentation-stinky compound complexes were calculated using Yang’s method [22 (link)].

Chen J.N., Zhao H.L., Zhang Y.Y., Zhou D.Y., Qin L, & Huang X.H. (2023). Comprehensive Multi-Spectroscopy and Molecular Docking Understanding of Interactions between Fermentation-Stinky Compounds and Mandarin Fish Myofibrillar Proteins. Foods, 12(10), 2054.

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Circular Dichroism Spectroscopy of Proteins

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Lyophilized protein constructs were weighed and dissolved in a 20 mM sodium phosphate, 100 mM NaCl buffer at pH 7.4 to make a 200 μM stock. The stock was diluted into a concentration series to measure the CD spectra. CD spectra were measured using a JASCO J-1500 CD spectrometer with a 1 cm quartz cell for 1 μM and 2 μM protein concentration and 0.1 cm quartz cell for other concentrations (Starna Cells) using a 0.1-nm step size, a bandwidth of 1 nm and a scan speed of 200 nm min⁻¹ between 260 nm and 190 nm. Each spectrum was measured seven times and averaged to increase the signal-to-noise ratio. The buffer control spectrum was subtracted from each protein spectrum. CD spectra were normalized using UV 280 nm absorbance to eliminate the small concentration difference between different protein constructs.

Moses D., Guadalupe K., Yu F., Flores E., Perez A.R., McAnelly R., Shamoon N.M., Kaur G., Cuevas-Zepeda E., Merg A.D., Martin E.W., Holehouse A.S, & Sukenik S. (2024). Structural biases in disordered proteins are prevalent in the cell. Nature Structural & Molecular Biology, 31(2), 283-292.

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Far-UV CD Spectroscopy of Peptides

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A Jasco J1500 CD spectrometer was used to measure the far-UV CD spectra for the peptide solutions (100 μM) at pH 3.6, 7.4, and 11.7. The CD spectra were recorded in the range of 250–195 nm using a cuvette with a 2 mm path length at 25 °C. An average of three measurements for each sample was performed, and the CD signals were measured at a scan rate of 100 nm min⁻¹, with a data integration time of 4 s and a bandwidth of 2.5 nm.

Natarajan A., Vadrevu L.R, & Rangan K. (2024). DRGD-linked charged EKKE dimeric dodecapeptide: pH-based amyloid nanostructures and their application in lead and uranium binding. RSC Advances, 14(13), 9200-9217.

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