Andrew C. McShan

The paper reports the solution structure of a Nif11-LP leader peptide and shows how its tertiary structure mediates protein-protein interactions with a RiPP biosynthetic enzyme.

This study designs de novo proteins that selectively inhibit alpha-synuclein aggregation by targeting specific intermediates, with one binder preferentially inhibiting oligomer formation and secondary nucleation.

The paper identifies ligands that bind beyond a known hydrophobic pocket at the HBV core protein interface using molecular dynamics and fragment mapping.