Thermodynamic Stability of DNA Photolyase
Presentation Type
Poster
Faculty Advisor
Yvonne Gindt
Access Type
Event
Start Date
26-4-2024 12:45 PM
End Date
26-4-2024 1:44 PM
Description
The thermodynamic stability of a protein is greatly influenced by the presence of cosolvents or small organic molecules such as sugars and alcohols. In this work, we focus on understanding cosolvent, protein, and water interaction as a function of temperature. Our protein of interest is DNA photolyase, a protein found throughout the kingdom of life including in thermophilic and mesophilic organisms. Since DNA photolyase is a flavin adenine dinucleotide (FAD)-containing protein, the FAD can serve as a reporter of the protein structure. In the DNA photolyases, the FAD cofactor emission increases as the protein is unfolded. This work tests the hypothesis that the mechanism by which cosolvent stabilizes protein structure will change as the temperature of the system changes. The thermodynamics of protein unfolding as a function of the cosolvent, trehalose, will be measured as a function of temperature for both thermophilic and mesophilic DNA photolyase. Results show that higher concentrations of Trehalose have been associated with an elevation in denaturation temperature.
Thermodynamic Stability of DNA Photolyase
The thermodynamic stability of a protein is greatly influenced by the presence of cosolvents or small organic molecules such as sugars and alcohols. In this work, we focus on understanding cosolvent, protein, and water interaction as a function of temperature. Our protein of interest is DNA photolyase, a protein found throughout the kingdom of life including in thermophilic and mesophilic organisms. Since DNA photolyase is a flavin adenine dinucleotide (FAD)-containing protein, the FAD can serve as a reporter of the protein structure. In the DNA photolyases, the FAD cofactor emission increases as the protein is unfolded. This work tests the hypothesis that the mechanism by which cosolvent stabilizes protein structure will change as the temperature of the system changes. The thermodynamics of protein unfolding as a function of the cosolvent, trehalose, will be measured as a function of temperature for both thermophilic and mesophilic DNA photolyase. Results show that higher concentrations of Trehalose have been associated with an elevation in denaturation temperature.