Table 1.

Fraction of secondary structure of peptides

Peptide	% TFE	Helixa	β- sheet	Turns	Unordered	Total
NT	0	0.11	0.29	0.23	0.36	0.99
L1	0	0.11	0.26	0.25	0.37	0.99
	15	0.11	0.29	0.27	0.34	1.0
	30	0.10	0.27	0.26	0.36	0.99
	45	0.06	0.35	0.22	0.36	0.99
L2	0	0.07	0.27	0.21	0.44	0.99
	15	0.10	0.27	0.23	0.39	0.99
	30	0.29	0.22	0.19	0.30	1
	45	0.65	0.15	0.04	0.16	0.99
TM4b	0	0.29	0.20	0.2	0.29	0.98
	30	0.59	0.08	0.1	0.23	1.0
	45	0.47	0.12	0.13	0.25	0.99
CT	0	0.16	0.19	0.09	0.36	1

Secondary structure of peptides were determined by CD spectropolarimetry at increasing concentrations of TFE. Composition of secondary structures were obtained by deconvoluting CD spectra with CDSSTR algorithm using Dichroweb server using Basis set 4 as reference.

^aHelix is a mixture α- and 3₁₀-helices.

^bInitially, it was dissolved in 33% ACN in water.