L. M. Miller

This paper designs reconfigurable asymmetric protein assemblies using implicit negative design principles, enabling stable subunit exchange and diverse complex formations.

This paper designs small, stable proteins that bind to diverse target proteins using only structural information, achieving nanomolar to picomolar affinities.

The paper designs picomolar SARS-CoV-2 miniprotein inhibitors using computational methods and experimental validation, showing high potency and structural similarity to computational models.