Summary
The binding affinity between two proteins weakly correlates with buried surface area (1). At least 500 are required for a stable complex to form (2), and the effect levels off at >2000 (1).
Details
For a given buried surface area, affinity can span several orders of magnitude, in part because a small number of hot spot interactions can dominate binding energy (1,3).
Figures
Ref (1); pink and black points represent protein-peptide and protein-protein interactions, respectively
1.
Chen J, Sawyer N, Regan L. Protein–protein interactions: General trends in the relationship between binding affinity and interfacial buried surface area. Protein Science. 2013;22(4):510–5. Available from: https://doi.org/10.1002/pro.2230
2.
Day ES, Cote SM, Whitty A. Binding Efficiency of Protein–Protein Complexes. Biochemistry. 2012;51(45):9124–36. Available from: https://doi.org/10.1021/bi301039t
3.
Clackson T, Wells JA. A Hot Spot of Binding Energy in a Hormone-Receptor Interface. Science. 1995;267(5196):383–6. Available from: https://doi.org/10.1126/science.7529940