The presentation will cover an introduction into the new SUPR-DSF system from Protein Stable and a brief overview of Chirascan CD spectrometers from Applied Photophysics. Both systems can aid in stability screening of proteins and in the biophysical characterisation of proteins.
Differential Scanning Fluorimetry (DSF) is a valuable and widely-used technique that monitors protein unfolding with increasing temperature by detecting changes in fluorescence. However, the conventional workflow for DSF uses extrinsic dyes that may influence the thermal stability of the protein under investigation. This can affect the quality of your data by generating false positives or negatives during screening. The SUPR-DSF system from Protein Stable measures intrinsic fluorescence of proteins to detect structural changes and avoids the use of additional dyes. The SUPR-DSF provides fluorescence measurement data directly from 384-well plates and with no proprietary consumables. SUPR-DSF reduces operator time and minimizes the risk of errors in multi-step sample preparation while also bringing down the cost of consumables and sample consumption without any compromise to data quality.
Our Chirascan CD spectrometers contribute to a deeper understanding of biomolecular characteristics, mechanisms and interactions. Our system can be used not only to gain insight and detect changes in secondary and tertiary structure but to study folding and unfolding mechanisms during altered physiological parameters. The Chirascan systems can also be fitted with additional accessories to expand its capabilities further.