Rebecca L. Frkic

This study investigates the molecular basis and evolutionary constraints of organophosphate resistance in dipteran carboxylesterases, revealing sequence context-dependent success of a mutation and trade-offs between affinity and turnover.

This study uses fragment-based drug design to identify novel heparanase inhibitors, resulting in compounds with improved potency for potential therapeutic applications.

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

This study uses ancestral sequence reconstruction to explore PET-degrading cutinase sequence space, revealing diverse evolutionary pathways and the effectiveness of LASE in mapping fitness landscapes.

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 study isolates and characterizes a bacterial strain capable of detoxifying malachite green, identifying an azoreductase responsible for its degradation.

This paper introduces 4-cyano-tryptophan (4-CN-Trp) as a fluorescent amino acid that preserves protein structure and enables detection of ligand binding sites through fluorescence changes.

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.