where R is the universal gas constant, T is absolute temperature (K), and [F] and [M] are protein concentrations in fibrillar (insoluble) and monomeric (i.e., soluble) states, respectively . The amyloid state is thought to be the global energy minimum of the protein free energy landscape. Consequently, high thermodynamic stability of fibrils translates to low concentrations of soluble protein at the end of the aggregation reaction which are often difficult to quantify accurately . In order to increase the equilibrium concentration of soluble protein to easily quantifiable levels, the equilibrium can be shifted in favour of fibril dissociation by changing external conditions, e.g., increasing (or decreasing) temperature , high pressure , or by addition of chemical denaturants . The latter is perhaps the most versatile since, similarly to protein unfolding, a linear dependence of Gibbs free energy on denaturant concentration can be reasonably assumed which allows for the application of a (relatively) straightforward analytical framework. This typically involves fitting chemical depolymerization data to an isodesmic polymerisation model, in which a single equilibrium constant is assumed between monomers and aggregates regardless of their size . Recently, a more realistic cooperative model has been applied to the analysis of depolymerization of glucagon and PI3K-SH3 domain fibrils .The model recognizes nucleation and polymerization through two distinct equilibrium constants and is able to correctly model the protein concentration dependency of the depolymerization curves .