N. K. Goto

This study computationally redesigns an enzyme's conformational landscape to enhance catalytic efficiency with a non-native substrate, achieving up to 1900-fold selectivity switch.

This study shows how two mutations can create conformational dynamics in a globular protein through synergistic effects on its energy landscape.

This paper designs proteins that exchange between defined conformational states on functional timescales using a new computational method called meta-multistate design.