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. 2000 Jul 11;97(15):8245–8250. doi: 10.1073/pnas.150518097

Figure 1.

Figure 1

Ribbon-model representation of the backbone structure of buforin II in 50% trifluoroethanol. The N-terminal random coil, the extended helix, the hinge, and the C-terminal regular helix form an overall amphipathic structure. The amino acid residues are colored as follows: positively charged residues, red; other hydrophilic residues, blue; proline, white; other hydrophobic residues, yellow.