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A Fossil Protein Chimera; Difficulties in Discriminating Dinosaur Peptide Sequences From Modern Cross-Contamination

ABSTRACT: Proteome analyses of ostrich bone using Orbitrap Elite mass spectrometry

INSTRUMENT(S): LTQ Orbitrap

ORGANISM(S): Struthio Camelus (ostrich)

TISSUE(S): Long Bone

SUBMITTER: Michael Buckley

LAB HEAD: Michael Buckley

PROVIDER: PXD006360 | Pride | 2020-04-20

REPOSITORIES: pride

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Dataset's files

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			Action	DRS
	20130301_SD1.raw.mgf	Mgf
	20130301_SD1.raw.pride.mgf.gz	Mgf
	20130621_MB21.raw.mgf	Mgf
	20130621_MB21.raw.pride.mgf.gz	Mgf
	20141104_NP11_1in50.raw.mgf	Mgf

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Publications

A fossil protein chimera; difficulties in discriminating dinosaur peptide sequences from modern cross-contamination.

Buckley Michael M Warwood Stacey S van Dongen Bart B Kitchener Andrew C AC Manning Phillip L PL

Proceedings. Biological sciences 20170501 1855

A decade ago, reports that organic-rich soft tissue survived from dinosaur fossils were apparently supported by proteomics-derived sequence information of exceptionally well-preserved bone. This initial claim to the sequencing of endogenous collagen peptides from an approximately 68 Myr <i>Tyrannosaurus rex</i> fossil was highly controversial, largely on the grounds of potential contamination from either bacterial biofilms or from laboratory practice. In a subsequent study, collagen peptide sequ ...[more]

PMID: 28566488

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