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

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