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Figure 4 | BMC Structural Biology

Figure 4

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

Figure 4

Conformational characterisation of peptide-1. (A). Tris-Tricine electrophoretic mobility of peptide-1 and peptide-122. (see Table 1 for theoretical molecular weights). Standard molecular weight markers are shown on the left. (B). far-UV CD spectra as a function of pH at 10°C. The concentration of peptide-1 was 50 μM. pH values are indicated in the spectra. The insert shows the dependence with the temperature of the molar ellipticity at 198 nm from spectra acquired at pH 6.8. (C). 1H NMR monodimensional spectra of peptide-1 (50 μM) in water at different pH values.

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