title: Why collagens best survived in fossils? Clues from amino acid thermal stability.
abstract: Explaining why type I collagens are preferentially preserved in the geological time scale remains a challenge. Several pieces of evidence indicate that its rich content in the bone and its unique, stable structure played key roles in its preservation. By considering the distinct thermal stability of amino acids, we reveal that the elevated abundance of thermostable amino acid residues in type I collagens also contribute to its survival.
authors.affiliation: National Key Laboratory of Crop Genetic Improvement, College of Life Science and Technology, Huazhong Agricultural University, Wuhan 430070, PR China.
authors.forename: Shuang-Yin
authors.initials: SY
authors.lastname: Wang
authors.forename: Enrico
authors.initials: E
authors.lastname: Cappellini
authors.forename: Hong-Yu
authors.initials: HY
authors.lastname: Zhang
mesh_terms: D000596:Amino Acids / Q000737:chemistry*; D000818:Animals; D024042:Collagen Type I / Q000737:chemistry*; D005580:Fossils; D006358:Hot Temperature; D006801:Humans
chemical_list: D000596:Amino Acids; D024042:Collagen Type I