Marco Mravic

This study provides structural insights into DHODH catalysis and drug resistance by analyzing conformational changes and resistance mutations.

This paper designs synthetic proteins that inhibit TLR4 signaling by binding its transmembrane domain, demonstrating the importance of transmembrane interactions in immune signaling.

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

The paper develops a platform to measure and engineer membrane protein-protein interactions using split nanoluciferase, improving assay accuracy and compatibility with protein engineering.

The paper uses protein design to investigate the structural principles of common antiparallel transmembrane motifs, revealing how sequence patterns stabilize membrane protein architectures.