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. Author manuscript; available in PMC: 2013 Nov 4.
Published in final edited form as: Biopolymers. 2008 Sep;89(9):10.1002/bip.21004. doi: 10.1002/bip.21004

TABLE I.

NMR Structuring Shifts and CD Measures of Helicity for Peptides with Different N- and C-Capping Motifs

Peptide Sequence 13C=O structuring shifts at 280K CD, 278K
A4 A8 A9 − [θ]222
Ac-GGG(KAAAA)3K-NH2 2.37 2.41 n. d. n.d.
YGG(KAAAA)3A-NH2 1.98 2.07 1.82 18,700
Ac-YGG(KAAAA)3A-NH2 2.29 2.28 2.01 16,700
Ac-YGG(KAAAA)3K-NH2 2.22 2.33 1.98 21,400a
Ac-YGG(KAAAA)3R-NH2 n. d. 2.51 n. d. 19,300
Ac-YGG(KAAAA)3r-NH2 n. d. 2.45 2.05 18,700b
(KAAAA)3rGY-NH2 0.87 1.01 0.90 2,900
Ac-(KAAAA)3AGY-NH2 2.30 2.34 2.01 11,900
Ac-(KAAAA)3KGY-NH2 2.54 2.51 2.18 12,200
Ac-(KAAAA)3rGY-NH2 2.47 2.43 2.16 14,300
Ac-(KAAAA)3KAAAAKGY-NH2 2.94 3.13 2.85 18,700
(KAAAA)3KAAAAKGY-NH2 1.54 2.18 2.08 n.d.
a

Prior value from a graph reported by Andersen et al.51

b

Huang et al.11 reported [θ]222․ = −18,300°.