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Ancient amino acids from fossil feathers in amber.
- Source :
-
Scientific reports [Sci Rep] 2019 Apr 23; Vol. 9 (1), pp. 6420. Date of Electronic Publication: 2019 Apr 23. - Publication Year :
- 2019
-
Abstract
- Ancient protein analysis is a rapidly developing field of research. Proteins ranging in age from the Quaternary to Jurassic are being used to answer questions about phylogeny, evolution, and extinction. However, these analyses are sometimes contentious, and focus primarily on large vertebrates in sedimentary fossilisation environments; there are few studies of protein preservation in fossils in amber. Here we show exceptionally slow racemisation rates during thermal degradation experiments of resin enclosed feathers, relative to previous thermal degradation experiments of ostrich eggshell, coral skeleton, and limpet shell. We also recover amino acids from two specimens of fossil feathers in amber. The amino acid compositions are broadly similar to those of degraded feathers, but concentrations are very low, suggesting that much of the original protein has been degraded and lost. High levels of racemisation in more apolar, slowly racemising amino acids suggest that some of the amino acids were ancient and therefore original. Our findings indicate that the unique fossilisation environment inside amber shows potential for the recovery of ancient amino acids and proteins.
- Subjects :
- Amino Acids chemistry
Amino Acids history
Animals
Birds anatomy & histology
Chromatography, Reverse-Phase
Dinosaurs anatomy & histology
Extinction, Biological
Feathers anatomy & histology
Fossils anatomy & histology
History, Ancient
Preservation, Biological
Proteins chemistry
Proteins history
Proteolysis
Amber chemistry
Amino Acids isolation & purification
Egg Shell chemistry
Feathers chemistry
Fossils history
Proteins isolation & purification
Subjects
Details
- Language :
- English
- ISSN :
- 2045-2322
- Volume :
- 9
- Issue :
- 1
- Database :
- MEDLINE
- Journal :
- Scientific reports
- Publication Type :
- Academic Journal
- Accession number :
- 31015542
- Full Text :
- https://doi.org/10.1038/s41598-019-42938-9