M. Heyne

Climbing up and down binding landscapes: a high-throughput study of mutational effects in homologous protein-protein complexes

This study quantifies mutational effects on binding affinity in three homologous protease-inhibitor complexes, revealing distinct binding landscapes and epistasis patterns.

Generating quantitative binding landscapes through fractional binding selections, deep sequencing and data normalization

The paper introduces a method to quantify binding free energy changes for thousands of protein mutants using randomization, sequencing, and normalization, applied to BPTI and Bovine Trypsin interactions.