Each shaving step is maintained until a constant low rate of frequency increase is reached, thereby ensuring that the accessible disordered regions are mostly degraded. The remaining release of mass at low constant rate is likely to originate from fibril shortening from the ends, where the accessibility by Proteinase K is likely to be highest. By investigating the DF plots of Proteinase K incubations, we find that the ∆D to ∆F relationship of the shaving phase converges towards a dissipation insensitive reaction, as the fibrils are grown for longer periods of time prior to shaving (Fig. ). This is consistent with the observation that Proteinase K treatment predominantly removes non-core material, but also slowly shortens the fibrils from the end. For longer fibrils, the Proteinase K treatment is increasingly dominated by the removal of non-core material as the surface-to-end ratio is increased. We find a linear relationship between the frequency response of mass added through fibril elongation and the frequency response of the shaving reaction (Fig. ) in agreement with removal of the entire available fuzzy coat and fibril depolymerization not significantly contributing to the degradation response. The shaven material corresponds to 16.2 ± 2.7 % of the frequency response of the grown fibrils. This, however, does not mean that the Proteinase K necessarily degrades 16 % of the fibril, which would only correspond to approximately 30 % of the fuzzy coat. The frequency response of fibril growth has a significant liquid con-tribution, which is demonstrated by the high ∆D to ∆F ratio and overtone dependency. However, this is not the case for the shaven material, which has a low ∆D to ∆F ratio and no significant overtone divergence (Fig. ). If the liquid contribution of the full fibril accounts for at least 50 % of the frequency response, it follows that the Proteinase K treatment removes at least 65 % of the fuzzy coat: