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. Author manuscript; available in PMC: 2015 Sep 1.
Published in final edited form as: J Pept Sci. 2014 Jun 6;20(9):704–715. doi: 10.1002/psc.2657

Figure 1.

Figure 1

The beta cap can be used on any length hairpin and maintain the same conformation. (a: the archetypal example; “n” can be any number, but must include two amino acids per strand for proper alignment. b) Key features of the beta cap, including the edge-to-face Trp/Trp interaction (upfield protons at 1) a Gly amide→Trp indole H-bond (upfield proton 2) and a bifurcated H-bond involving the N-terminal carbonyl and the Thr sidechain (Hγ1 proton visible by NMR in aqueous media, 3) c) the generic, N-acetylated form of the captide used in this study, shown with structure-validating “long”-range (i−i+>1) NOEs. These same NOEs are observed for all well-folded captides and serve as further confirmation of structure.