Protein–protein interactions (PPIs) play vital roles in numerous biological processes . The supramolecular nature of these interactions differs based on the composition and affinity of the involved peptide strands and in the dynamics of the proteins . Rational approaches towards the recognition of protein surfaces such as co‐crystallization of proteins along with their counterparts or mutational analysis of the protein–protein interfaces provides better insight into the structural epitopes involved in PPIs, providing important clues for biomimetic strategies. In the following section, we will review physical and chemical properties of protein surfaces involved in PPI, in the context of designing synthetic receptors discussed in the later sections.
10.2 Structural Properties of Protein Surfaces
In nature, there are distinct families of protein–protein complexes. There are heterodimeric protein–protein complexes, such as hormone–receptor or antigen–antibody complexes, in which each protein has its own stable identity upon isolation. Homo‐dimeric/oligomeric protein complexes, on the other hand, consist of multiple identical proteins that do not have a stable identity on their own.
10.2.1 Protein–Protein Interfacial Areas