Nicholas F. Polizzi

This paper designs an orthogonal self-labeling protein, LUCI-tag, using deep learning, which enables rapid and payload-agnostic labeling of proteins in live cells.

The paper identifies leucine as the substrate for SFXN1 and reveals its alternating-access transport mechanism using structural and biochemical analyses.

This paper designs de novo proteins that undergo small-molecule-induced conformational changes, demonstrating strong binding affinity and specificity for exatecan.

This study adapts Edman degradation and amino acid recognition to expansion microscopy gels to demonstrate in situ protein sequencing principles using synthetic constructs.

This paper introduces a method using two neural networks to design drug-binding proteins with high affinity, surpassing current state-of-the-art methods.

This paper designs synthetic transmembrane subunits to stabilize and expand membrane proteins, demonstrating their utility in structural biology and disease treatment.

This study shows how a designed generalist binding protein can evolve into specific functions like a fluorophore binder and an efficient enzyme through weak, promiscuous interactions.

The paper determines the structure of MreC-MreD complex and shows how MreD controls MreC conformation, essential for bacterial cell shape and antibiotic targeting.

This paper designs de novo proteins to modify nanopore complexes, creating customized structural and functional properties for enhanced sequencing applications.

This paper designs drug-binding proteins with low nanomolar affinity and predictable specificity using computational methods, validated by experimental measurements and structural analysis.

AF2BIND predicts ligand-binding sites using AlphaFold2's pairwise representation without requiring a ligand, outperforming other models and linking bait amino acids to ligand properties.