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. Author manuscript; available in PMC: 2008 Dec 1.
Published in final edited form as: Biomaterials. 2007 Aug 13;28(34):5185–5192. doi: 10.1016/j.biomaterials.2007.07.044

Figure 2.

Figure 2

Coiled-coil protein domains. (A) Cartoon depicting the interaction of two heptads. The hydrophobic core is formed by the interactions of amino acid residues in positions a and d. (B) Helical wheel representation of two-stranded, antiparallel α-helical coiled-coils formed by the dimerization of CCE and CCK. The view is shown looking down the superhelical axis from the N-terminus of CCE and from the C-terminus of the CCK. CC denotes the coiled-coil peptides. E and K denote peptides in which most of the e and g positions are occupied by either glutamic acid or lysine, respectively. (C) Schematic illustration of the parallel or antiparallel orientation of two coiled-coil strands. (D) Primary structure of CCE and CCK. The sequences are written in the one-letter amino acid code. Positions a and d of the heptad repeats are underlined and form the hydrophobic core of the coiled-coil. N and C denote the amino and carboxy ends of the α-helix, respectively. Cartoons are from ocw.mit.edu/NR/rdonlyres/Biology.