The Baker lab did summited “The Brothers” during summer 2014. It was one of my favorite hikes, and also the toughest. Summit post link to the brothers
Functional protein-protein interaction design was first accomplished in 2011 by Fleishman et al[ ]. The method begins by detecting where on the surface of a protein to bind which is done by copying an antibody binding site. From there hotspots are extracted from the antibody and protein scaffolds are selected in the PDB. The proteins are selected based on what shape can accommodate the hot-spots. Additional interactions on the protein scaffold are designed. The protein is then experimentally refined using directed evolution and verified using X-ray crystallography.
High throughput design of protein-protein interactions is now a reality thanks to work by Aaron Chevalier, Chris Bahl and others. Design begins with an antibody identified binding site. Then hotspots or binding site motifs are copied over to a library of de-novo design protein scaffold. The library of designs is expressed on a chip and tested via high-throughput screening. Using this technique it is possible to design therapeutic protein-protein binding proteins quickly, however, the vast majority of proteins are non-functional so ongoing work seeks to improve reliability.