Towards the de novo design of metallohydrolases

Conference Dates

September 15-19, 2019


De novo design of proteins has enabled the exploration of vast regions of sequence space previously inaccessible by nature.[1] These proteins are computationally designed based on physical principles of protein structure and folding, and are tailored according to a specific function or property. Great advances have been made in the design of novel highly stable protein folds capable of hosting enzyme active sites.[2] That has in turn allowed us to undertake larger scale efforts of installing various enzymatic activity into these scaffolds. As a proof of principle we have undertaken efforts towards designing hydrolase (esterase and phosphatase) activity into the NTF2[2b] and the TIM-barrel[3] folds through the introduction of metal binding sites.

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