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Hydroxyproline content and location in relation to collagen thermal stability
Author(s) -
Burjanadze Tengiz V.
Publication year - 1979
Publication title -
biopolymers
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.556
H-Index - 125
eISSN - 1097-0282
pISSN - 0006-3525
DOI - 10.1002/bip.1979.360180413
Subject(s) - hydroxyproline , proline , chemistry , imino acid , collagen helix , content (measure theory) , positive correlation , basement membrane , alanine , thermal stability , crystallography , biochemistry , triple helix , amino acid , stereochemistry , anatomy , medicine , organic chemistry , biology , mathematics , mathematical analysis
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.