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. Author manuscript; available in PMC: 2011 Jan 1.
Published in final edited form as: Circulation. 2010 Jan 26;121(3):351–353. doi: 10.1161/CIR.0b013e3181d0b947

Figure 1.

Figure 1

Helical relation of amino acid positions of tropomyosin's coiled coil as viewed from an axial perspective. Hydrophobic residues at position a and d stabilize interactions between α helices, where positions g and e are typically charged amino acids stabilizing tropomyosin through ionic interactions.