Skip to main content
. Author manuscript; available in PMC: 2016 Jan 15.
Published in final edited form as: Virology. 2014 Nov 25;475:46–55. doi: 10.1016/j.virol.2014.10.011

Table 4.

Proportions of secondary structurea for HCV peptidesb in deuterated phosphate buffer as estimated from Fourier self-deconvolution of the FTIR spectrac of the peptide mide I band.

Peptide % Conformation
α-Helix β-Sheet Turn Disordered
HCV1 2.10 43.11 31.05 23.74
HCV2 4.66 53.56 28.94 17.84
HCV3 11.60 54.34 21.96 12.04
HCV4 11.86 41.48 29.21 17.45
HCV5 10.55 50.90 25.72 12.83
HCV6 12.34 52.87 20.39 14.40
HCV15 11.05 39.52 31.46 17.97
HCV15R 24.77 49.12 12.97 13.14
HCV16 14.68 40.36 18.71 26.25
HCV18 5.88 47.91 29.74 16.47
HCV18RI 7.82 53.88 22.55 15.75
a

Data are the means of four separate determinations and have an SE ± 5% or better.

b

HCV Peptide [i.e., 2 mM HCV] desolvated in deuterated 10 mM phosphate buffer pH 5.6 (Figure 3).

c

FTIR spectra were deconvoluted as described in Materials and Methods.