Michael C. Thompson

This paper introduces multistate enzyme design to optimize active sites across reaction coordinates, achieving higher catalytic efficiency and enantioselectivity than single-state designs.

This study determines two distinct structures of soybean lipoxygenase-1 from a single experiment, showing that conformational flexibility is influenced by crystal solvent content.

This study uses NMR peak intensity analysis to identify functional dynamics hotspots in proteins, showing that specific structural flexibility correlates with function in red fluorescent proteins.

The paper investigates how distal mutations in a retro-aldolase affect loop dynamics and catalytic efficiency, showing an epistatic effect when combined with active-site mutations.

This paper designs artificial enzymes with high catalytic efficiency using crystallography-enhanced computational methods, achieving improvements comparable to directed evolution.