Table 2. Fraction folded β-hairpin derived from characteristic NMR features. Values in the structure below are an average of eqn (1) and (2).

Peptide	Amidine	Eqn (1)	Eqn (2) a
			Val3	Orn8	Ile10
YKL		0.85	0.59	0.84	0.49
1-Tyr(NH)2	‘Out’	0.82	0.42	0.73	0.60
2-Val(NH)3	‘In’	0.30		0.02	0.01
3-Glu(NH)4	‘Out’	0.96	0.72	0.93	0.36
4-Gly(NH)7	‘Out’	0.61	0.61	0.81	0.48
5-Orn(NH)8	‘In’	0.03	0.03		0.08
6-Ile(NH)10	‘In’	0.16	0.03	0.19

^aBlank entries in the table correspond to peptides for which the amidine at those residues (Val₃, Orn₈, Ile₁₀) affected the chemical shift of the H^α,¹⁴ making it irrelevant for analysis. Each folded % in the structure above the table corresponds to an X = NH at that position while keeping amides (X = O) at the other positions along the backbone, and is an average of the calculated values of fraction folded (eqn (1), Val₃, Orn₈, Ile₁₀) for that peptide.