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. 2009 May 15;5(5):e1000389. doi: 10.1371/journal.pcbi.1000389

Figure 7. Aromatic packing stabilizes the spectrin repeats under torsion.

Figure 7

A) Surface representation of amino acid residues W381, Y417, and W453 near terminus B of a single α-actinin rod domain monomer. Aromatic packing between amino acid residues W381 and Y417 is seen. B) Effect of clockwise rotation of over 140 degrees on the aromatic packing between W381 and Y417. The aromatic packing is disrupted and torque required for continued rotation increases. C) Counterclockwise rotation at terminus B of the monomer conformation does not disrupt aromatic packing, shown here to be intact after rotation. D) More extensive aromatic packing exists at terminus A. Two sets of aromatic residues exist, each set sharing electrons within its members. Both sets are shown here with surface representation in VMD [52]. E) Clockwise rotation of terminus A. Shown here, the aromatic packing in both sets are not completely disrupted, but electron sharing between F89, F74, and Y15 is reduced. F) Counterclockwise rotation of terminus A does not seem to disrupt the aromatic packing shown here as intact with the surface representation. Direction of rotation is indicated above each panel.