Christopher Williams

This paper designs de novo flavoproteins with controlled excited state dynamics using computational methods and experimental validation.

This paper introduces a new cyclisation strategy using a bromomethyl picolinaldehyde linker to expand macrocyclic peptide topologies, leading to more potent and diverse inhibitors.

This paper designs redox proteins with tunable electron transfer properties by replacing heme B with non-natural metalloporphyrins, achieving redox potential modulation of over 400 mV.

This study uses de novo protein design to investigate redox cooperativity in multiheme cytochromes, showing that membrane burial enhances heme-heme electrostatic coupling.

The paper designs and validates de novo proteins with single and multi-heme binding capabilities, achieving atomic-level structural resolution for functional engineering.