Figure 4 | Scientific Reports

Figure 4

From: Influence of solubilization and AD-mutations on stability and structure of human presenilins

Figure 4

Thermal unfolding of presenilin2 in FC14 monitored by far-UV CD. (a) CD spectra (260 nm to 185 nm) shown in 8 °C increments from 4 to 98 °C; (b) Fraction unfolded calculated from signal at 192, 209, 217 and 221 nm respectively. Solid lines represent the fitting of the data into equation (2). (c) Helix and strand content at different temperatures after deconvolution. Solid lines represent the fitting of the data into equation (2) (see Methods); (d) Correlation of helical structure with other secondary structures for data points at different temperatures. Solid lines represent a linear fit. For details of data deconvolution see Supplementary Figure S5. For details on the control of protein precipitation during unfolding see Supplementary Figure S4.

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