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. Author manuscript; available in PMC: 2015 Apr 1.
Published in final edited form as: Curr Opin Struct Biol. 2014 Mar 22;0:98–103. doi: 10.1016/j.sbi.2014.02.004

Figure 1.

Figure 1

A dynamical network analysis [35•] of the protein dimer HisH-HisF with bound effector molecule, PRFAR (effector not shown). The residues predicted to assist in propagating the allosteric signal between two residues of interest, Glu180:HisH (top) and Leu50:HisF (bottom), are depicted as white spheres along suboptimal signaling pathways, depicted as cyan lines. Expanding signaling pathways with lengths in network space near that of the optimal pathway are believed to facilitate an allosteric signal and may provide insight into differences between allosterically active and inactive forms.