Megan Luo Rose Hills
Development Of A Method to Characterize Proteins With Multiple Folds
Most proteins have one known fold with small conformational changes with no dramatic structural differences. “Fold-switching” proteins have two or more folds that can be occupied and the preference can be shifted due to change in local environment. While rare, fold-switching proteins are implicated in diseases including SARS-CoV-2, rabies and cancer, making them potential drug targets. Furthermore, biotechnological applications of fold-switching proteins, such as biosensors, could lead to impacts in many fields. Therefore, it is important to understand the ratio of populations and interconversion rate between both conformations of a fold-switching protein. Current methods to determine these thermodynamic parameters, including NMR, technologically limit the range of proteins that can be studied. Thus new tools are needed to better characterize folding-switching landscapes.
I will study RfaH, a transcription factor in E. coli from the NusG protein superfamily that has a fold-switching domain. The fold-switching landscape of RfaH is well understood making this an ideal system for developing a generalizable method to study any protein that switches folds.
Message To Sponsor
Thank you so much for supporting my SURF project and giving me the opportunity to research over the summer. Your support allows me to contribute to the field of biophysics while also growing as an student in science. I am honored to be a recipient of your generosity and thank you for believing in my project!