Why collagens best survived in fossils? Clues from amino acid thermal stability
Publikation: Bidrag til tidsskrift › Review › Forskning › fagfællebedømt
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Why collagens best survived in fossils? Clues from amino acid thermal stability. / Wang, Shuang-Yin; Cappellini, Enrico; Zhang, Hong-Yu.
I: Biochemical and Biophysical Research Communications, Bind 422, Nr. 1, 25.05.2012, s. 5-7.Publikation: Bidrag til tidsskrift › Review › Forskning › fagfællebedømt
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TY - JOUR
T1 - Why collagens best survived in fossils? Clues from amino acid thermal stability
AU - Wang, Shuang-Yin
AU - Cappellini, Enrico
AU - Zhang, Hong-Yu
N1 - Copyright © 2012 Elsevier Inc. All rights reserved.
PY - 2012/5/25
Y1 - 2012/5/25
N2 - 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.
AB - 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.
KW - Amino Acids
KW - Animals
KW - Collagen Type I
KW - Fossils
KW - Hot Temperature
KW - Humans
U2 - 10.1016/j.bbrc.2012.04.122
DO - 10.1016/j.bbrc.2012.04.122
M3 - Review
C2 - 22564740
VL - 422
SP - 5
EP - 7
JO - Biochemical and Biophysical Research Communications
JF - Biochemical and Biophysical Research Communications
SN - 0006-291X
IS - 1
ER -
ID: 48853484