Joe A. Kaczmarski

This study maps the sequence space of bacterial chitinases to show how domain composition and catalytic core evolve differently based on functional roles.

The paper examines how thermodynamic binding strategies in proteins evolved in response to temperature changes, showing a shift from entropy-driven to enthalpy-driven binding over time.

This paper introduces LASE, a method using ancestral sequence reconstruction to train protein language models with higher accuracy and faster computation than large models.

The paper identifies and characterizes a bacterial periplasmic solute-binding protein that specifically binds L-amino acid amides, revealing structural and functional insights into bacterial nutrient uptake.

This study shows how an enzyme evolved from a solute-binding protein through structural and catalytic changes, highlighting mechanisms of de novo enzyme emergence.