De novo design and characterization of an apolar helical hairpin peptide at atomic resolution: Compaction mediated by weak interactions -- Data Supplement - Supplemental Data -- Proceedings of the National Academy of Sciences

Supplementary material for Ramagopal et al. (2001) Proc. Natl. Acad. Sci. USA 98 (3), 870–874. (10.1073/pnas.031442998)

Fig. 8.
Speculated right-handed 3₁₀-helical (marked R) conformation for the model sequence -DPhe-X-X-DPhe-X-X-DPhe- and inverted structure (left-handed, marked L). The angle between the vector perpendicular to the mean plane of all the DPhe atoms and the helix axis is approximately 45°.