Date of Award
Chemistry and Biochemistry
Protein crystallization is fundamental to modern research efforts given its ability to determine a protein’s structure as well as the interactions that structure allows and relies upon. This process, though lacking direct application, provides necessary information for subsequent research efforts for which applicationsmay be explored. As such, efforts were taken to crystallize nickel-binding protein (NBP) reengineered from Copper Storage Protein 1 (Csp1) in its apo and metal bound form, Bovine Serum Albumin (BSA) in its apo and gold bound form (Au-BSA), and an artificial de novo tetramer hydrogenase mimic peptide to better inform future research actions for these respective molecules. Efforts yielded apo-NBP crystals of sufficient quality from which a structure could be determined. Apo-BSA crystals were formed; however,their morphology was unsuitable for structure determination. Au-BSA, Ni-NBP, and the de novo tetramer currently are undergoing condition optimization to more efficiently develop crystals for structure elucidation.
Crane, Skyler, "Crystallization Efforts for an Engineered Nickel-Binding Protein, Gold-Bovine Serum Albumin Nanoclusters, and an Artificial De Novo Tetramer Hydrogenase Mimic" (2020). Honors Theses. 1377.
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