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. 2020 Sep 20;18:2687–2698. doi: 10.1016/j.csbj.2020.09.017

Fig. 4.

Fig. 4

Differences in protein interaction networks among different phosphorylation states. (A) Salt-bridges of the activation segment residues ILE250–ALA264 with their interaction frequencies (%). Only the salt-bridges with > 20% differences in their interaction frequencies among systems are shown. (B) Selected hydrophobic interactions of MKK4 and their interaction frequencies among different systems. The locations of the Cα-atoms of the hydrophobic residues are shown in spheres, which are coloured according to different hydrophobic clusters that exhibit linked interactions.