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. Author manuscript; available in PMC: 2012 Aug 11.

Published in final edited form as: J Med Chem. 2011 Jul 14;54(15):5307–5319. doi: 10.1021/jm200004e

500MHz 2D NMR data for peptide 6. A) NH-aliphatic region of NOESY spectrum of peptide in 90% H2O/10%D2O at 298 K showing NH-CαH connectivity. Sequential as well as long-range connectivities are shown. B) NH-NH region of NOESY spectrum of peptide 6. C) Schematic diagram showing the NOESY connectivity indicating the β-strand or β-hairpin structure of the peptide in solution. Observed NOEs are shown by double-ended arrows.

500MHz 2D NMR data for peptide 6. A) NH-aliphatic region of NOESY spectrum of peptide in 90% H2O/10%D2O at 298 K showing NH-CαH connectivity. Sequential as well as long-range connectivities are shown. B) NH-NH region of NOESY spectrum of peptide 6. C) Schematic diagram showing the NOESY connectivity indicating the β-strand or β-hairpin structure of the peptide in solution. Observed NOEs are shown by double-ended arrows.