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Figure 5 | BMC Structural Biology

Figure 5

From: Ionic self-complementarity induces amyloid-like fibril formation in an isolated domain of a plant copper metallochaperone protein

Figure 5

Conformational characterisation of peptide-1 at 10°C in the presence of TFE and SDS (A). Far-UV CD spectra at pH 4.2 as a function of TFE concentration. TFE induces a decrease in the molar ellipticity at 215 nm (CD spectra acquired at ■, 0 %; ▲, 10 %; Δ, 20 %; , 30 %; , 40 %, and □ 60 %, v/v, TFE concentrations). (B). Far-UV CD spectra at pH 6.8 at different TFE concentrations (symbols as in panel A). The insert shows the dependence with TFE concentration (v/v) of the molar ellipticity at 215 nm. (C). Far-UV CD spectra at pH 6.8 at different SDS concentrations (■, 0 mM; , 1 mM, , 2 mM; Æ, 3 mM; + 5 mM and , 10 mM). (D). Far-UV CD spectra at pH 3.2 at different SDS concentrations (symbols as in part C). The concentration of peptide-1 in all the spectra was 50 μM.

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