Karol Buda

This study maps substrate-dependent epistasis in phosphotriesterase by analyzing 64 mutation combinations across nine substrates, revealing how intramolecular wiring changes to support promiscuity and functional trade-offs.

This paper investigates the molecular mechanisms of collateral sensitivity in β-lactamase evolution, showing how specific mutations alter enzyme structure and drug resistance profiles.

This paper shows enzyme kinetic parameters exhibit non-specific epistasis due to multi-state catalytic cycles, and provides tools to correct for this effect in mechanistic inference.

This paper shows how evolution improves enzyme function by shifting the rate-limiting step from substrate binding to sub-state interconversion in β-lactamase OXA-48.