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. 2011 Oct 14;103:231–275. doi: 10.1016/B978-0-12-415906-8.00001-7

Fig. 3.

Fig. 3

Hydrophobic core interactions in coiled coils. (A) Solvent-accessible surface of an α-helix in a coiled coil illustrating how hydrophobic a and d core residues (highlighted) are aligned into a “hydrophobic stripe” on one side of the helix. The second helix of the coiled coil is shown docked along this stripe, through contact with its own hydrophobic stripe. (B) A view of a single helical repeat (seven residues) of the coiled coil from above, showing the organization of the side chains. The a and d residues point into the core, interacting with their opposite number. (C) The helical wheel diagram used to diagrammatically represent the structure of a coiled coil.