Infrared spectra of HEWL species recorded during the time course of the aggregation.

<p>The panels represent the ATR-FTIR spectra of HEWL solutions registered at 0 h (A), 48 h (B), 72 h (C), 96 h (D), 168 h (E) and 240 h (F). The spectra in green represent the individual secondary structure components of the protein identified by the treatment of original spectra by deconvolution and curve-fitting procedures [<a href="http://www.plosone.org/article/info:doi/10.1371/journal.pone.0142095#pone.0142095.ref050" target="_blank">50</a>,<a href="http://www.plosone.org/article/info:doi/10.1371/journal.pone.0142095#pone.0142095.ref051" target="_blank">51</a>]. Peaks in the regions 1616–1621 cm^-1, 1626–1640 cm^-1 and 1680–1694 cm^-1 are mostly from ß-sheet, those around 1645 cm^-1 from disordered structures, those centred between 1663 cm^-1 and 1673 cm^-1 from turns and loops, and from 1649 cm^-1 to 1660 cm^-1 generally from α-helix structure [<a href="http://www.plosone.org/article/info:doi/10.1371/journal.pone.0142095#pone.0142095.ref050" target="_blank">50</a>,<a href="http://www.plosone.org/article/info:doi/10.1371/journal.pone.0142095#pone.0142095.ref051" target="_blank">51</a>]. Measurements, obtained from three independent experiments, were performed for different protein concentrations.