Table 2.

Correspondence of C^β - C^β Distances for Peptidomimetics A, B, and 1 – 4 With Common Secondary Structures.^a

structure	sequence	D(Å)	A	B	1	2	3	4
α-helix	i-i+ 1	5.2
	i-i+ 2	7.1
	i-i+ 3	5.6
	i-i+ 4	6.5
	i-i+ 5	9.8
	i-i+ 6	10.8
	i-i+ 7	10.7
	i-i+ 8	12.9
β-turn (type-I)	i-i+ 1	5.7
	i-i+ 2	5.1
	i-i+ 3	5.4
	i+1-i+2	5.2
	i+1-i+3	7.5
	i+2-i+3	5.6
β-sheet (parallel)	i-i+ 1	5.8
	i-i+ 2	7.1
	i-i+ 3	11.1
	i-i+ 4	13.2
	i-i’	5.5
	i-i’+1	7.2
	i-i’+2	9.0
	i-i’+3	11.5
	i-i’+4	14.4
β-sheet (anti-parallel)	i-i+ 1	5.8
	i-i+ 2	6.5
	i-i+ 3	11.0
	i-i+ 4	12.8
	i-i’	4.5
	i-i’+1	7.6
	i-i’+2	8.9
	i-i’+3	12.7
	i-i’+4	14.8
γ-turn (classic)	i-i+ 1	5.2
	i-i+ 2	7.4
	i+1-i+2	5.3
γ-turn (inverse)	i-i+ 1	6.3
	i-i+ 2	5.7
	i+1-i+2	6.2

^aTemplates for ideal type I β-turns⁵⁴,⁷⁶ and for γ-turns⁷⁷ were obtained from standard torsion angles. A standard template for overlays with an α-helix was obtained from Discovery Studio 2.5⁷⁸, and a β-sheet template for overlays was obtained by β -sheet builder.⁷⁹