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Market Profile: Circular Dichroism.

Circular dichroism (CD) spectroscopy is an application-specific type of absorption spectroscopy that provides structural information on a variety of biological macromolecules. The term circular dichroism refers to the absorption difference between left- and right-handed circularly polarized light. A CD spectropolarimeter, an extremely sensitive instrument capable of accurately measuring in the 190-170nm range, is used to determine the absorption difference. These instruments cost around $70,000.

Circular dichroism is primarily used in determining the structure of proteins, particularly the secondary structure, though analysis of the tertiary structure is also possible. CD is also used in protein thermodynamics, ligand binding, nucleic acid structure evaluation, and analysis of the protein folding process. CD is best used in analyzing the structural changes that occur in a protein after it has been agitated, and in comparing the structures of engineered and parent proteins.

A drawback to CD is that the results can be unreliable. However, CD is fast and capable of analyzing multiple protein candidates to filter out the most interesting and useful candidates. These samples can then be further analyzed with a more detailed technique such as x-ray crystallography or NMR spectroscopy.

CD instrument vendors include Olis, Aviv Instruments, Applied Photophysics, Jobin Yvon and Jasco. The total market for circular dichroism is around $6-$8 million annually, with a growth rate approaching 10%. The majority of sales are for stability analysis applications.

With the recent development of using synchrotron radiation light sources instead of traditional Xenon arc lamps in CD instruments, more accurate spectra can be measured at lower wavelengths. Though still in its infancy, synchrotron radiation circular dichroism (SRCD) may increase the use of CD, especially in the area of structural genomics.
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Publication:Instrument Business Outlook
Article Type:Brief Article
Date:Jun 15, 2001
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