Novel Protein Characterization for Biopharma Development
8am PST | 11am EST | 4pm GMT | 5pm CET
Protein stability is one of the most important critical quality attributes for a new biological drug. Unstable or misfolded proteins are prone to aggregation and precipitation, which can lead to lower activity as well as increased immunogenicity. There has been a long-standing interest in renaturing unfolded, misfolded or precipitated proteins.
In this webinar, our expert speakers will demonstrate how thermal and pressure stress changed the structure and melting point of two model proteins and resulted in the discovery of different structural rearrangements.
They will then discuss a novel method for solubilizing and refolding proteins using hydrostatic pressure to generate proteins whose structure matches that of the native protein, as confirmed by microfluidic modulation spectroscopy.
- The implications of stress (thermal and pressure) induced changes to protein structure
- How pressure and thermal stress can lead to different structural rearrangements
- A novel technique for re-solubilizing and re-folding precipitated proteins
- The fundamentals of microfluidic modulation spectroscopy