10.26180/5c61c2d6055c2
EMILIA MARIA MARIJANOVIC
EMILIA MARIA
MARIJANOVIC
Engineering serpin stability and function
Monash University
2019
Protein engineering
Protein folding
Biophysics
Biochemistry
2019-02-11 18:45:39
Thesis
https://bridges.monash.edu/articles/thesis/Engineering_serpin_stability_and_function/7698182
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.