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. 2011 Dec 12;108(51):20279–20280. doi: 10.1073/pnas.1118084109

Fig. 1.

Fig. 1.

Applying the ER/K α-helix to studying conformational changes and network characterization. (A) A protein in two possible conformations. Detection of a FRET signal may be dependent on a change in conformation. The semicircle below each conformation represents the linker. (B) Two representations of a protein–protein interaction network. Left: This network is a conventional node-and-edge depiction. Quantifying the interaction affinities may enable the addition of interaction strength as a property of the network, yielding a network with weighted edges (Right). Colored interaction schematics above and below the central arrow correspond to examples of mapped high- and low-affinity interactions between similarly colored nodes in the affinity-based network.