Here T t represents the transition temperature, where the condition pmobile/pstatic = 1 is fulfilled, D𝑆 % ! ! is the molar standard entropy difference at the transition temperature T t , and D𝐶 ' indicates the heat capacity difference between the two states. Fitted parameters for both scenarios are summarized in Table . We would like to point out that it is maybe not surprising that the condition D𝐶 ' = 0 is not perfectly fulfilled, since we still deal with a material involving many degrees of freedom, and both states are likely to be consisting of a broad variety of conformational states. Such a behaviour is not uncommon in soft condensed matter and can be found in order/disorder transitions where many degrees of freedom are involved, such the temperature induced unfolding of globular proteins. The fact that we deal with a broad temperature transition between the mobile and static states, indicates that this transition should not regarded as a phase transition, but instead as a transition between two conformational ensembles confined to rather localized domains. If the "communication" between these local domains is effectively suppressed, a phase transition is prevented and we end up with the observed "uncooperative" form of transition. A simple example for such a localized order/disorder transition, albeit from a different realm of soft condensed matter science, would be the extensively studied helix/coil transition of helical peptide chains where the "sharpness" (i.e. inverse temperature range) of the transition increases with the length of the peptide chains (i.e. the domain-size). Here the size of the molar standard transition entropy (which scales linearly with the peptide chain length) determines the "cooperativity" of the transition. In the present case a similar behaviour is observed: In both scenarios the entropy differences D𝑆 van 't Hoff analysis (D𝐶 ' =0):