Protein–protein interactions: General trends in the relationship between binding affinity and interfacial buried surface area

Protein–protein interactions play key roles in many cellular processes and their affinities and specificities are finely tuned to the functions they perform. Here, we present a study on the relationship between binding affinity and the size and chemical nature of protein–protein interfaces. Our anal...

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Bibliographic Details
Published in:Protein science 2013-04, Vol.22 (4), p.510-515
Main Authors: Chen, Jieming, Sawyer, Nicholas, Regan, Lynne
Format: Article
Language:English
Subjects:
buried surface area
Databases, Protein
dissociation constant
For the Record
hot spot
Hydrophobic and Hydrophilic Interactions
hydrophobicity
Protein Binding
Protein Conformation
Protein Interaction Mapping
Protein Multimerization
Protein Subunits
Proteins - chemistry
Proteins - metabolism
protein–protein interaction
surface energy density
Surface Properties
Thermodynamics
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Summary:Protein–protein interactions play key roles in many cellular processes and their affinities and specificities are finely tuned to the functions they perform. Here, we present a study on the relationship between binding affinity and the size and chemical nature of protein–protein interfaces. Our analysis focuses on heterodimers and includes curated structural and thermodynamic data for 113 complexes. We observe a direct correlation between binding affinity and the amount of surface area buried at the interface. For a given amount of surface area buried, the binding affinity spans four orders of magnitude in terms of the dissociation constant (Kd). Across the entire dataset, we observe no obvious relationship between binding affinity and the chemical composition of the interface. We also calculate the free energy per unit surface area buried, or “surface energy density,” of each heterodimer. For interfacial surface areas between 500 and 2000 Å2, the surface energy density decreases as the buried surface area increases. As the buried surface area increases beyond about 2000 Å2, the surface energy density levels off to a constant value. We believe that these analyses and data will be useful for researchers with an interest in understanding, designing or inhibiting protein–protein interfaces.
ISSN:0961-8368
1469-896X
DOI:10.1002/pro.2230