The role of 4-oxyproline in the phylogenetic change of collagen thermostability]

Analysing the data on imino acid content and thermostability of collagens distinguished phylogenetically it is shown that one hydroxyproline residue (per 100 residues) which is localized in the third position of the triplet increases thermostability per 0.6 degree in the average. The magnitude obtained exceeds the value 4 times (0.16 degree). This happens at the expense of hydroxylated proline in the third position.