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Engineering serpin stability and function
thesisposted on 11.02.2019, 18:45 by EMILIA MARIA MARIJANOVIC
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.