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. 2012 Mar 12;109(13):4810–4815. doi: 10.1073/pnas.1120112109

Fig. 1.

Fig. 1.

Design of α4-proteins. (A) The sequences and helical wheel diagram for the α4-proteins illustrating positions of the hydrophobic a and d residues in the antiparallel four-helix bundle topology. The hydrophobic core of these proteins comprises six layers formed by a and d residues as illustrated in the diagram. (B) End and side views of the overlay of backbone atom traces determined from the crystal structures of α4H (green), α4F3a (blue), and α4F3af3d (purple).