Structure-based Thermodynamic Stability of Proteins
Speaker: Prof. Dr. George Nounesis
Biomolecular Physics Laboratory
National Centre for Scientific Research “Demokritos”
153 10 Aghia Paraskevi, Greece
Date/Time: Dec 18, 2013 Wednesday @ 13:40
Place: Sabanci University, G035
Chemical and heat-induced denaturation of proteins in solution are employed to determine their thermodynamic stability.
A combination of high-accuracy techniques including, adiabatic differential scanning calorimetry, circular dichroism and fluorescence spectroscopy are carried out towards resolving complex, non-equilibrium protein unfolding processes and reveal associations with structural conformations at the
molecular level that may be important for protein engineering and biotechnology.
Examples will be presented from recent studies of the TIM barrel functional domain of chitinases
The association of thermodynamic stability to the pathogenicity of single point mutations will also be presented in the case of the BRCT functional domain of the protein BReast CAncer 1 (BRCA1), which has been linked to hereditary breast/ovarian cancer. Understanding the thermodynamics of the BRCT interactions with small phosphopeptides in solution is shown to be crucial for discovering the protein’s functional pathways. This can be efficiently performed by using high-resolution isothermal titration calorimetry.