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Circular dichroism (CD) spectroscopy measures differences in the absorption of left-handed polarized light versus right-handed polarized light that arise due to structural asymmetry. The absence of regular structure results in zero CD intensity, while an ordered structure results in a spectrum which can contain both positive and negative signals. It is an effective analytical instrument for studying the asymmetry of molecular structure.
Applications
Determination if a protein is folded
Characterization of secondary structure (α-helix,β-sheet)
Detection of changes in structure upon mutagenesis
Studying conformational stability of proteins: pH stability, denaturant stability (urea, guadinium hydrochloride), temperature, buffers, addition of stabilizers
Detection of Changes in the conformation of a protein upon protein: protein interaction
Specifications
Specifications-J815 CD Spectropolarimeter
Light source
150W air-cooled xenon lamp
Spectral range(standard detector)
163-900nm
Spectral range(optional detector)
163-1100nm
Spectral bandwidth
0.01-15nm
CD measurement range
±10, 200, 2000 mdeg
Stray light
less than 0.0003% (200 nm)
Scanning method
automatic response, continuous, stepping
Scanning speed
1~10000nm/min
Strengths
Wide range of wavelengths.
Multi-channel measurement.
Convenient measurement and analysis system that can be used for data conversion between models.