Author

Daniel Sawyer

Date of Award

2014

First Advisor

David Myers

Second Advisor

Erin McMullin

Abstract

Domain swapping is a mechanism in which proteins oligomerize by the mutual exchange of complementary protein domains. Though this mechanism plays important roles in nature, it is of particular interest because it can be engineered into a wide variety of proteins with high selectivity and specificity. Previous studies have demonstrated that certain synthetic fusion proteins known as domain-swapped modules (DSMs) can be used to create functional hydrogels from protein polymers. In this study, we investigate the incorporation of two new functionalities into the DSM design: ligand dependent selfassembly and post-translational attachment of functional molecules. Our results show that, by using an “adaptor” protein, both monomers and oligomers of our DSM construct can be decorated with a fluorescent protein while in solution. We also show that our construct exhibits some ligand-dependent structural changes, though modifications are necessary to generate an inducible trigger for reliable polymer self-assembly.

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