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Fig. 3 | BMC Biophysics

Fig. 3

From: α-synuclein-lanthanide metal ions interaction: binding sites, conformation and fibrillation

Fig. 3

Intensities changes of amide groups in αS at various concentration of Tb3+ or Dy3+. The I/I0 profiles of α-synuclein backbone amide groups were plotted as a function of residue number at molar ratios of (a) αS/Tb3+(4/1), (b) αS/ Tb3+(2/1), (c) αS/Tb3+(1/1), (d) αS/Dy3+(4/1), (e) αS/Dy3+(2/1), (f) αS/Dy3+ (1/1), respectively. The residues that were severely broadened were labelled in red rectangle. According to the attenuation degree of cross peaks (I/I0), the whole residues of αS were divided into three parts: residues 1 to 97, residues 98 to 109, and residues 110 to 140, which were all labelled with orange lines. αS sequence shown above the figure is the same as that in Fig. 2

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