Computational design of novel protein–protein interfaces is a test of our understanding of
protein interactions and has the potential to allow modification of cellular physiology …

Highlights•Many computationally designed protein–protein interactions were reported over
the past two years.•Recent design goals include heterodimers, homodimers …

The computational design of proteins that bind small molecule ligands is one of the
unsolved challenges in protein engineering. It is complicated by the relatively small size of …

The computer-based design of protein–protein interactions is a rigorous test of our
understanding of molecular recognition and an attractive approach for creating novel tools …

Protein–protein interactions can be designed computationally by using positive strategies
that maximize the stability of the desired structure and/or by negative strategies that seek to …

The de novo design of protein-protein interfaces is a stringent test of our understanding of
the principles underlying protein-protein interactions and would enable unique approaches …

Protein–protein interfaces regulate many critical processes for cellular function. The ability to
accurately control and regulate these molecular interactions is of major interest for …

Homodimers are the most common type of protein assembly in nature and have distinct
features compared with heterodimers and higher order oligomers. Understanding …

Background Few existing protein-protein interface design methods allow for extensive
backbone rearrangements during the design process. There is also a dichotomy between …

Computational protein design strategies have been developed to reengineer protein–
protein interfaces in an automated, generalizable fashion. In the past two years, these …