Metallohydrolases are responsible for the hydrolytic cleavage of a variety of biologically relevant substrates, including esters, organophosphates, polynucleotides, peptides, and carbon dioxide. We have recently observed that DFsc (Due Ferri single chain), a de novo computationally designed four-helix bundle protein, is capable of performing hydrolysis reactions on a range of substrates, including p-nitrophenyl acetate (pNPA) and DNA, in the presence of a variety of metal ions. The proteins are characterized using a range of biophysical techniques (e.g., circular dichroism and UV-visible absorption spectroscopy). Factors that influence the reactivity (e.g., metal identity, active site composition, and pH) are systematically explored.

Hydrolytic activity of Due Ferri single chain proteins

2019 Spring National Meeting

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