Figure 3: Phosphorylation modulates the kinetic and thermodynamic stability of Aβ aggregates.
From: Phosphorylation modifies the molecular stability of β-amyloid deposits
(a) Schematic representation of two kinetic models for aggregate dissociation. Model 1 consists of a single step of reversible Aβ monomer (grey) dissociation from aggregates. Model 2 involves a reversible step in which Aβ aggregates are converted to an intermediate state under rate constants k1 and k2, followed by a second reversible step of monomer release from the intermediate state. (b) Rate constants obtained from the analysis of monomer release kinetics (Fig. 1c) according to the two kinetic models shown in a. Error bars represent s.e.s of fitting parameters.
