Figure 4 | Scientific Reports

Figure 4

From: Structure based aggregation studies reveal the presence of helix-rich intermediate during α-Synuclein aggregation

Figure 4

Secondary structural changes monitored by FTIR spectroscopy.

Curve fitted FTIR spectra in the region corresponding to amide-I band showing the different secondary structural content of α-Syn species at different stages of aggregation (Upper panel). FTIR spectral data suggest predominate random coil structure at the beginning that eventually converted to β-sheet rich structure via α-helical intermediate during α-Syn aggregation. Corresponding CD spectra of the identical samples were shown in lower panel.

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