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J 1500 high performance cd spectrometer

Manufactured by Jasco

The J-1500 High Performance CD Spectrometer is a laboratory instrument designed for precise circular dichroism (CD) measurements. It provides accurate and reliable data on the structural and conformational properties of biomolecules, such as proteins, nucleic acids, and small molecules. The core function of the J-1500 is to measure the differential absorption of left-handed and right-handed circularly polarized light by optically active samples, allowing for the analysis of their secondary structure and folding characteristics.

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5 protocols using j 1500 high performance cd spectrometer

1

Circular Dichroism Analysis of Cytochrome c

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To obtain CD spectra of the samples and evaluate irreversible procedure-induced changes in the Cyt c structure, we nanoprecipitated Cyt c and HA as mentioned before but without adding the crosslinker. Samples were centrifuged and placed in a desiccator overnight to remove the organic solvent. The NPs were then re-dissolved in water in order to measure the absorbance of the loaded Cyt c. We used a JASCO J-1500 High Performance CD spectrometer at room temperature to obtain the spectra of the samples placed in 10 mm quartz cuvettes. Changes in the protein tertiary structure were observed at 260–350 nm and changes in the Soret band (heme group) were observed at 380–450 nm. The nanopure water blank was subtracted from each sample that was scanned thrice to obtain an averaged spectrum.
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2

Circular Dichroism Spectroscopy of Cytochrome c

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CD spectra were recorded using a JASCO J-1500 High Performance CD spectrometer at room temperature. The protein (Cyt c, Cyt c NPs, or SPDP-Cyt c NPs) was dissolved in nanopure water. CD spectra were acquired from 260 to 350 nm (tertiary structure) at a concentration of 1 mg/ml using a 10 mm quartz cuvette. Each spectrum was obtained by averaging two scans. Spectra of nanopure water blanks were measured prior to the samples and subtracted from the sample spectra.
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3

Circular Dichroism Analysis of Cytochrome c

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To obtain CD spectra of the samples and evaluate irreversible procedure-induced changes in the Cyt c structure, we nanoprecipitated Cyt c and HA as mentioned before but without adding the crosslinker. Samples were centrifuged and placed in a desiccator overnight to remove the organic solvent. The NPs were then re-dissolved in water in order to measure the absorbance of the loaded Cyt c. We used a JASCO J-1500 High Performance CD spectrometer at room temperature to obtain the spectra of the samples placed in 10 mm quartz cuvettes. Changes in the protein tertiary structure were observed at 260–350 nm and changes in the Soret band (heme group) were observed at 380–450 nm. The nanopure water blank was subtracted from each sample that was scanned thrice to obtain an averaged spectrum.
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4

Probing Cyt c Structural Changes

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To observe changes in Cyt c structure after DDS construction, CD spectra were obtained for each sample. Cyt c and Cyt c-HA bioconjugates were dissolved in 10 mM PBS at pH 7.4 to obtain a final Cyt c concentration of 0.09 mg/ml. CD spectra were obtained using a JASCO J-1500 High Performance CD spectrometer at room temperature. Near-UV spectra were measured from 260–350 nm to observe the protein tertiary structure and the Soret region (heme group) was measured from 380–450 nm using a 10 mm quartz cuvette. Each sample was scanned twice to obtain an averaged spectrum from which the background of a nanopure water blank was subtracted.
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5

Probing Cyt c Structural Changes

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To observe changes in Cyt c structure after DDS construction, CD spectra were obtained for each sample. Cyt c and Cyt c-HA bioconjugates were dissolved in 10 mM PBS at pH 7.4 to obtain a final Cyt c concentration of 0.09 mg/ml. CD spectra were obtained using a JASCO J-1500 High Performance CD spectrometer at room temperature. Near-UV spectra were measured from 260–350 nm to observe the protein tertiary structure and the Soret region (heme group) was measured from 380–450 nm using a 10 mm quartz cuvette. Each sample was scanned twice to obtain an averaged spectrum from which the background of a nanopure water blank was subtracted.
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