Figure 4 | Scientific Reports

Figure 4

From: Fluorescence correlation spectroscopy reveals a cooperative unfolding of monomeric amyloid-β 42 with a low Gibbs free energy

Figure 4

Unfolding curve of AF488-C(0)Aβ42 from three independent 1fFCS and one 2fFCS measurement series with their corresponding best-fit line to the two-state unfolding model (equation (4)). Each data point is the average of at least three hydrodynamic radii, which were transformed into the fraction of denatured peptide according to equation (3). The error bars were calculated as the standard deviation between these independent measurements.

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