Will current technologies enable dinosaur proteomics?

Preserved Proteins from Extinct Bison latifrons Identified by Tandem Mass Spectrometry; Hydroxylysine Glycosides are a Common Feature of Ancient Collagen

“…As such, this analysis has unearthed common posttranslational modifications of collagen that may assist in its preservation over time. During the last decade, paleontology and taphonomy (the study of decaying organisms over time and the fossilization processes) have begun to overlap with the field of proteomics to shed new light on preserved organic matter in fossilized bones (1)(2)(3)(4). These bones represent a time capsule of ancient biomolecules, owing to their natural resistance to post mortem decay arising from a unique combination of mechanical, structural, and chemical properties (4 -7).…”

Proteins in Art, Archaeology, and Paleontology: From Detection to Identification

“…Mass spectrometry-based PMF and sequencing have shown evidence for the survival of protein compounds in fossil materials older than 1 million-years-old, providing thus new insights in the fields of evolutionary biology. , Collagen survival was shown during analyses of fossils of Tyrannosaurus rex , dating back 68 million years and fossils of mastodons dating back 160 000–600 000 years . The sequenced peptides were used to compute a phylogenetic tree using sequence alignments (with BLAST alignment bioinformatic tool), resulting in high similarities between the Tyrannosaurus rex collagen peptides and those of birds (Gallus gallus) and between mastodon (Mammut americanum) and other mammals, including elephant (Loxodonta africana) .…”