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. Author manuscript; available in PMC: 2013 Dec 18.
Published in final edited form as: J Mol Biol. 2012 Mar 15;419(0):10.1016/j.jmb.2012.03.004. doi: 10.1016/j.jmb.2012.03.004

Figure 3. Crossing Angles Dependency of RPCs cliques.

Figure 3

Instantaneous crossing angles between two α-helices for each RPC was computed using HELANAL121 (see Materials and Methods), and the frequency distribution of helix RPCs is shown against the crossing angle. The black is from α-helices in globular proteins and the white are from coiled-coils. It is interesting to note that the distributions would be about equal if the coiled-coils were removed. Each peak corresponds to a canonical packing pattern depicted in Figure 4. The well-known peaks of coiled coils are found for anti-parallel at −165° and 25°. The other peaks occur at −30° and 150°, which also includes the shoulder at 175°.