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Engineering serpin stability and function

thesis
posted on 11.02.2019 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.

History

Principal supervisor

Ashley Buckle

Year of Award

2019

Department, School or Centre

Biochemistry and Molecular Biology

Course

Doctor of Philosophy

Degree Type

DOCTORATE

Faculty

Faculty of Medicine Nursing and Health Sciences

Exports

Exports