Understanding protein, cosolvent and water interaction
Presentation Type
Abstract
Faculty Advisor
Yvonne Gindt
Access Type
Event
Start Date
25-4-2025 9:00 AM
End Date
25-4-2025 9:59 AM
Description
Biotherapeutics play an important role in modern medicine; stabilizing biotherapeutics is a major challenge due to their temperature sensitivity. In nature, thermophiles use small sugar molecules called cosolvents to stabilize the protein structure at high temperatures. In this study, we investigate the effect of temperature on protein, cosolvent, and water interactions using Sulfolobus solfataricus DNA photolyase (SsPL) as our model protein. The specific cosolvent used is Trehalose, a small sugar commonly used as a protein structure stabilizer. SsPL is a thermophilic protein that repairs UV-damaged DNA. SsPL contains flavine adenine dinucleotide (FAD) in its active site, that can serve as a reporter of the protein structure. In this study, we developed the technique of fluorescence anisotropy to monitor structural changes in the protein.
Understanding protein, cosolvent and water interaction
Biotherapeutics play an important role in modern medicine; stabilizing biotherapeutics is a major challenge due to their temperature sensitivity. In nature, thermophiles use small sugar molecules called cosolvents to stabilize the protein structure at high temperatures. In this study, we investigate the effect of temperature on protein, cosolvent, and water interactions using Sulfolobus solfataricus DNA photolyase (SsPL) as our model protein. The specific cosolvent used is Trehalose, a small sugar commonly used as a protein structure stabilizer. SsPL is a thermophilic protein that repairs UV-damaged DNA. SsPL contains flavine adenine dinucleotide (FAD) in its active site, that can serve as a reporter of the protein structure. In this study, we developed the technique of fluorescence anisotropy to monitor structural changes in the protein.
Comments
Poster presentation at the 2025 Student Research Symposium.