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. 2008 Jul 3;95(7):3400–3406. doi: 10.1529/biophysj.108.131482

TABLE 1.

% Content
Time (min) β-sheet Random coil α-Helix
5 32 ± 1 35 ± 1 33 ± 1
60 28 ± 1 38 ± 1 34 ± 1
150 23 ± 1 40 ± 1 37 ± 1
500 19 ± 1 39 ± 1 42 ± 1
2100 10 ± 1 37 ± 1 53 ± 1
Freshly dissolved 7 ± 1 39 ± 1 54 ± 1

Time dependence of the secondary structure content of BPI solutions after the quench from 60°C to 25°C. Data were obtained by calculating the areas of three Lorentzian line shapes (corresponding to β-sheet, α-helix, and random coil, respectively) that were fitted to each of the spectra shown in Fig. 3 (see text).