The interaction of ox ligamentum nuchae elastin (native, purified, and soluble) with different solvents (water, ethylene glycol, methanol, and 2,2,2‐trifluoroethanol) was investigated by means of differential scanning calorimetry. The unfreezable solvent content and the corresponding solvent to elastin residue molar ratio were determined from the melting endotherms of the freezable solvent present in these systems. The molar ratio obtained in the case of water and ethylene glycol agrees with hypothesis of a direct solvation of the main chain peptide group and is interpreted according to a model previously proposed for polyamides. Quite different molar ratios are obtained in the case of the two monofunctional solvents and no model can be proposed at present to explain their interaction with the protein.
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Ceccorulli et al. (1977) studied this question.
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