Rapid Protein Analysis Using Circular Dichroism
14 Sep 2011

Applied Photophysics has introduced their Chirascan™-plus CD Spectrometer used for the rapid determination of the secondary structure of proteins. It is also capable of investigating their tertiary structure which is achieved by measuring the Circular Dichroism induced in the aromatic side-chains and disulphide bonds of the peptide backbone. The Applied Photophysics Chirascan™-plus CD Spectrometer offers:

 Results up to 70 times faster than with ordinary CD spectrometers
 Broader bandwidths from DiQuartz™ dual prism, dual polarizing monochromator
 Large F/7 aperture for greater light collection and greater image size
 More data available thanks to very high sensitivity in the far-UV range to 165 nm

Protein secondary and tertiary structures change under stress, for example with temperature or change in pH. Circular dichroism is used to assess conformational stability with changing environment, including continuous temperature changes with measurements at all wavelengths in parallel. Used in this way, it has an important role to play in biotherapeutic drug development and formulation testing where it can help to optimise buffer conditions that enhance product longevity. Circular dichroism is also used in bio-comparability studies to demonstrate conformational equivalence of material from different processes or sources and for determining that novel proteins are correctly folded. Up to 5 detection channels operating simultaneously ensure comprehensive, accurate analysis.

Chirascan CD spectrometers have a light output of 1.5xe13 photons/sec at 180 nm for a 1 nm bandwidth gives Chirascan exceptional performance in the far UV region which is particularly important in drug analysis. A movable detector optimises data collection from light scattering samples, e.g., membrane proteins.

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Applied Photophysics Ltd



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