Many powerful strategies have been devised to create new metalloproteins and metalloenzymes, yet preexisting knowledge of the tertiary and quaternary protein structure is often required to generate suitable platforms for robust metal coordination and activity. We have taken an alternative approach in which folded, monomeric proteins are used as synthons for building supramolecular assemblies and the nascent interfaces in these assemblies are subsequently engineered for building metal-based activities. With chemical and evolutionary expediency in mind, we devised two different strategies, MeTIR (Metal Templated Interface Redesign) and MASCoT (Metal Active Sites through Covalent Tethering), which differ in the way that such supramolecular metalloprotein assemblies are constructed. In this presentation. I will summarize these strategies and some of our results based on them.

Engineering inorganic functions in designed protein assemblies

Fall 2022 abstracts, posters, and presentations will launch in mid-September.

ACS Fall 2022

The official archive and repository for all ACS Meetings & Expositions abstracts and select posters or presentations.