Circular Dichroism.

Circular Dichroism (CD) is by far the most commonly employed chiroptical technique for the characterization of biomolecules and the analysis of chiral substances. For example, the far-UV Circular Dichroism spectrum of proteins can reveal important characteristics relating to their secondary structure such as the percentage of alpha helix, beta-sheet or beta-turns conformation, when near-UV, will provide information about the direct surrounding environment of the chiral chromophores.

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Visible and NIR-CD spectroscopy is a useful technique to study metal-protein interactions and to resolve individual d–d electronic transitions, but has also proved to be a highly performant tool for enantiomeric excess determination in asymmetric synthesis.

 

A modern spectropolarimeter.

The MOS-500 is a spectropolarimeter optimized for steady state and rapid kinetics applications. The circular dichroism spectrometer delivers outstanding performance in sensitivity, precision, speed and modularity from far-UV to NIR region. Optics and technology have been chosen to ensure that no wavelength range is discriminated. The MOS-500 uses an innovative patented three stage wavelength selection system to bypass the limitation of prism-based monochromators. The Biokine software platform also ensures a great user-experience and provides high-performance tools for the analysis of chemical and thermal denaturation of proteins.