The Circular Dichroism (CD) Spectrometer at the Tsinghua Base of the Protein Science Research (Beijing) Facility (Phoenix Project) has been put into operation._News Center Co., Ltd._The Circular Dichroism (CD) Spectrometer at the Tsinghua Base of the Protein Science Research (Beijing) Facility (Phoenix Project) has been put into operation.,British Applied Optics Physics Company Shanghai Representative Office_British Applied Optics Physics Company Shanghai Representative Office_Zhongshang 114 Industry Resources Network
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Home > News Center Co., Ltd. > The Circular Dichroism (CD) Spectrometer at the Tsinghua Base of the Protein Science Research (Beijing) Facility (Phoenix Project) has been put into operation.
News Center Co., Ltd.
The Circular Dichroism (CD) Spectrometer at the Tsinghua Base of the Protein Science Research (Beijing) Facility (Phoenix Project) has been put into operation.
Publish Time:2022-03-21        View Count:14        Return to List

Tsinghua University's Protein Science Research Facility (Beijing) at the Tsinghua Base (Phoenix Project) has successfully installed and tested its circular dichroism spectrometer as of March 26, 2014, and it is now officially in use.Round and Two ColorsThe CD Spectrometer is a new model from Applied Photophysics, serving various laboratories and research institutes across life sciences and medical disciplines, including the Structural Biology Center, Institute of Biophysics and Structural Biology, Key Laboratory of Biomembrane and Membrane Biotechnology Engineering, Antitumor Protein Engineering Laboratory, Key Laboratory of Protein Science, Key Laboratory of Bioinformatics, Key Laboratory of Protein, Institute of Marine Biotechnology, and Institute of Biochemistry and Molecular Biology at Tsinghua University. It is also open for use by other departments, research institutes, and off-campus laboratories within Tsinghua. The circular dichroism (CD) spectrometer is commonly used to study the structures, three-dimensional information, and structural stability of proteins, DNA, RNA, peptides, and more. This includes research on thermal stability, composition screening, and the chemical factors that may induce structural changes. When using the circular dichroism spectrometer, protein sample volumes typically range from 50ul to 100ul, and smaller volumes of 26ul or less can be used based on the sample's properties.

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