New analysis of the phylogenetic change of collagen thermostability
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Updated: Jul 23, 2026

Imaging Denatured Collagen Strands In vivo and Ex vivo via Photo-triggered Hybridization of Caged Collagen Mimetic Peptides
Published on: January 31, 2014
1A. Natishvili Institute of Experimental Morphology, Georgian Academy of Science, Tbilisi, Republic of Georgia. burj@kheta.ge
Abstract:
Recent data concerning the thermostability and the primary structure of type IV collagens, some invertebrate collagens, and for the stability of synthetic collagen-like polypeptides, show that our earlier analysis of the phylogenetic change of thermostability has some shortcomings. The results of the analysis were corrected and it has been shown that the dependence of denaturation temperature Td on 4-hydroxyproline content is hyperbolic and the total Gly-Pro-Hyp sequence content is a main, but not exclusive, factor influencing the change of collagen thermostability. It appears possible that the same mechanism underlies the thermostability of fibril-forming collagens of all animal life, ranging from Antarctic ice fish to at least one annelid (Alvinella pompejana) living at very high temperatures at the bottom of the ocean near thermal vents.
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