The effect of hydrophobicity on affinity is particularly pronounced in this group.
The interface areas of CHL4-OKP1, CHL4-MCM16, CHL4-NKP1 and CHL4-CSE4 are relatively small and flat. There are only a few residues in these interfaces. Therefore, the impact of conformational entropy on the affinity between these chains is quite low.
These four interfaces are flat because they have only a few residues.
CHL4-NKP1 and CHL4-OKP1 are showing here as an example, OKP1 and NKP1 are very elongated structure proteins and that accounts for this flat interface.
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