Why collagens best survived in fossils? Clues from amino acid thermal stability

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Why collagens best survived in fossils? Clues from amino acid thermal stability. / Wang, Shuang-Yin; Cappellini, Enrico; Zhang, Hong-Yu.

In: Biochemical and Biophysical Research Communications, Vol. 422, No. 1, 25.05.2012, p. 5-7.

Research output: Contribution to journal › Review › Research › peer-review

Harvard

Wang, S-Y, Cappellini, E & Zhang, H-Y 2012, 'Why collagens best survived in fossils? Clues from amino acid thermal stability', Biochemical and Biophysical Research Communications, vol. 422, no. 1, pp. 5-7. https://doi.org/10.1016/j.bbrc.2012.04.122

APA

Wang, S-Y., Cappellini, E., & Zhang, H-Y. (2012). Why collagens best survived in fossils? Clues from amino acid thermal stability. Biochemical and Biophysical Research Communications, 422(1), 5-7. https://doi.org/10.1016/j.bbrc.2012.04.122

Vancouver

Wang S-Y, Cappellini E, Zhang H-Y. Why collagens best survived in fossils? Clues from amino acid thermal stability. Biochemical and Biophysical Research Communications. 2012 May 25;422(1):5-7. https://doi.org/10.1016/j.bbrc.2012.04.122

Author

Wang, Shuang-Yin ; Cappellini, Enrico ; Zhang, Hong-Yu. / Why collagens best survived in fossils? Clues from amino acid thermal stability. In: Biochemical and Biophysical Research Communications. 2012 ; Vol. 422, No. 1. pp. 5-7.

Bibtex

@article{17d616e6b2fa44fe98f5787b4d777f95,

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.",

keywords = "Amino Acids, Animals, Collagen Type I, Fossils, Hot Temperature, Humans",

author = "Shuang-Yin Wang and Enrico Cappellini and Hong-Yu Zhang",

year = "2012",

month = may,

day = "25",

doi = "10.1016/j.bbrc.2012.04.122",

language = "English",

volume = "422",

pages = "5--7",

journal = "Biochemical and Biophysical Research Communications",

issn = "0006-291X",

publisher = "Elsevier",

number = "1",

}

RIS

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

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

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