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. Author manuscript; available in PMC: 2020 Apr 29.
Published in final edited form as: Acc Chem Res. 2008 Jul 17;41(10):1289–1300. doi: 10.1021/ar700264k

FIGURE 5.

FIGURE 5.

(a) Medium-range NOEs expected from an idealized α-helix–amino acid side chains are represented as green spheres; (b) NOESY correlation chart for HBS α-helix 9–the alanine-3 residues in both artificial helices are alkylated; filled rectangles indicate relative intensity of the NOE cross-peaks, while empty rectangles indicate NOE that could not be unambiguously assigned because of overlapping signals; (c, d) NMR-derived structures of HBS α-helix 9, views of (c) 20 lowest energy structures and (d) lowest energy structure showing hydrogen-bonding pattern within the artificial α-helix. All carbon, nitrogen, and oxygen atoms are shown in green, blue, and red, respectively, with the exception of the trans alkene group, which is shown in magenta.