Projects

We study bacterial GNATs of unknown function and develop chemical tools to obtain crystal structures with ligands bound to the acceptor sites for improved computational predictions of protein function.

We study polyamine N-acetyltransferases across all domains of life to determine why some are allosteric and others are not, why some adopt diverse oligomeric states, and why their structures and substrate specificity are not conserved within and across domains of life.

We study lysine acetyltransferases and how they post-translationally modify a multitude of proteins found within the bacterial cell.

We study bacterial GNATs that modify antibiotics to gain a greater understanding of how their specific amino acid residues contribute to catalysis and substrate specificity or promiscuity.