Stabilization of collagen structure: Dependence of collagen denaturation enthalpy on the imino acid content

Abstract An analysis of the available data on the enthalpy (ΔHr) of denaturation (melting) of collagens with different imino acid content in solution and in the aggregated state has shown that ΔHr in solution increases with increasing denaturation temperature, whereas in the aggregated state there is an inverse dependence. ΔHr in solution correlates with the hydroxyproline content but not with that of proline. No correlation between the change of ΔHr and the imino acid content is observed for the aggregated state.