Christoph Küng

This study uses deep mutational learning to identify myoglobin variants with enhanced peroxidase activity, showing the role of electron-hole hopping in catalytic efficiency.

The paper uses enzyme proximity sequencing to map how mutations affect substrate specificity of DAOx, identifying key positions and combinations that enhance selectivity.

This study uses deep mutational scanning to identify mutations that enhance thermostability in human myoglobin, discovering a de novo disulfide bond and combinatorial mutations that significantly increase stability.