All peptides were stored in tetrafluoroethylene (TFE) after synthesis, which was removed by evaporation using Nitrogen gas prior to use. To ensure complete removal of the TFE, the sample was then put under vacuum for one hour. The dried peptide was re-constituted in 10mM KH2PO4, 100mM KCl at pH 7.5, and prepared for CD data collection. All CD experiments were performed on a Jasco J-815 CD Specrometer (Annapolis, MD) using a 0.1cm quartz cuvette at ~150µM peptide concentration. Concentrations of the peptide samples were determined using a Nanodrop Spectrometer. To display helical content and the presence of an isodichroic point ellipticity was measured between 200nm to 260 nm in 1nm increments from −2°C to 60°C for a FM, FM (ox), FA, AM, AM (ox) and AA. Once these characteristics were established for each construct, one data point was collected at 222nm at each 0.5°C or 2°C change as temperature increased from −2°C to 60°C. Cooling melts were also collected, recording the signal at 222nm, on all peptides as temperature decreased from 60°C to −2°C. All collected data points were averaged from 3 acquisitions of the recorded ellipticity.
J 815 cd specrometer
Manufactured by Jasco
The J-815 CD Spectrometer is a laboratory instrument designed to measure the circular dichroism (CD) of samples. It is used to analyze the structural properties of various biomolecules, such as proteins, nucleic acids, and small molecules. The J-815 CD Spectrometer operates in the UV-vis wavelength range and provides accurate and reliable measurements of CD signals.
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Lab products found in correlation
2 protocols using j 815 cd specrometer
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Circular Dichroism Analysis of Peptides
2
Circular Dichroism Analysis of Peptides
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All peptides were stored in tetrafluoroethylene (TFE) after synthesis, which was removed by evaporation using Nitrogen gas prior to use. To ensure complete removal of the TFE, the sample was then put under vacuum for one hour. The dried peptide was re-constituted in 10mM KH2PO4, 100mM KCl at pH 7.5, and prepared for CD data collection. All CD experiments were performed on a Jasco J-815 CD Specrometer (Annapolis, MD) using a 0.1cm quartz cuvette at ~150µM peptide concentration. Concentrations of the peptide samples were determined using a Nanodrop Spectrometer. To display helical content and the presence of an isodichroic point ellipticity was measured between 200nm to 260 nm in 1nm increments from −2°C to 60°C for a FM, FM (ox), FA, AM, AM (ox) and AA. Once these characteristics were established for each construct, one data point was collected at 222nm at each 0.5°C or 2°C change as temperature increased from −2°C to 60°C. Cooling melts were also collected, recording the signal at 222nm, on all peptides as temperature decreased from 60°C to −2°C. All collected data points were averaged from 3 acquisitions of the recorded ellipticity.
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