%0 Thesis %A MARIJANOVIC, EMILIA MARIA %D 2019 %T Engineering serpin stability and function %U https://bridges.monash.edu/articles/thesis/Engineering_serpin_stability_and_function/7698182 %R 10.26180/5c61c2d6055c2 %2 https://bridges.monash.edu/ndownloader/files/14327522 %K Protein engineering %K Protein folding %K Biophysics %K Biochemistry %X Protein engineering was performed to create an a1-antitrypsin-like serpin that is thermostable while remaining functional. The base molecule for this engineering is a consensus-designed serpin, conserpin, which exhibits extreme thermostability while also being functional as a protease inhibitor. Engineering was performed in two ways: conserpin was engineered to function like a1-antitrypsin while remaining thermostable, and regions of the conserpin were grafted onto a1-antitrypsin to increase thermostability without compromising function. The folding pathway of conserpin was also investigated to provide insight into how thermostable serpins fold under extreme temperatures. %I Monash University