Coacervate phase, studied when

As shown in Table 3, in aqueous solution these short resilin-like peptides adopt a mixture of PPII stmcture, unordered conformations, and p-tums, while in Ttifluoroethanol (TFE) primarily type-11 p tums populate the conformational space. These findings are consistent with what Andersen has predicted and are also very similar to other elastomeric proteins studied. Interestingly, coacervation, a common phenomenon in elastin and abductin (in which a protein-rich phase is formed when the temperature is raised), has not been observed in resilin-like polypeptides (RLPs). This is almost certainly due to the inaeased hydrophilicity of resilin, which is soluble in water under all relevant experimental conditions. As mentioned above, additional spectroscopic studies on extended RLPs, as well as manipulations of RLP sequences via the introduction of different amino acid analogs and evaluation of corresponding conformational changes, would be useful to elucidate the mechanism of elasticity of resilin. 

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