Hydroxyproline content and location in relation to collagen thermal stability

Abstract

Abstract A new analysis has been made on studies of the influence of imino acid content on the changes of collagen thermal stability ( t m ). It is shown that, for the interstitial vertebrate collagens, there is a strict regularity in the changes of t m depending on hydroxyproline content. No correlation is observed between t m and proline content. Also, no correlation between t m and hydroxyproline content is observed for invertebrate and basement membrane collagens. On the basis of the reported data, the dependence of t m on hydroxyproline content is considered to be not a correlation between t m and the total content of hydroxyproline, but only as the correlation between t m and the content of hydroxyproline occurring at the third position in the sequence (Gly‐ R 2 ‐ R 3 ) n . The results agree with the idea that the influence exerted by proline and hydroxyproline on the stabilization of the triple helix of collagen is different.