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Paleoproteomics: Ancient proteins shed more light on the past

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From Catherine Offord at the at The Scientist:

In one recent project, for example, Schroeter and her advisor Mary Schweitzer extracted and analyzed collagen peptides from just 200 mg of an 80-million-year-old fossil of a Cretaceous-era herbivore, Brachylophosaurus canadensis, excavated in Montana. The amino acid sequences of those peptides, published last year, placed the dinosaur on a branch of the phylogenetic tree between crocodiles and basal birds such as ostriches.1 What’s more, the team’s collection of analyzable peptides from the ancient specimen suggests that there might be other fossils out there with similar molecular information hidden in them.

Although the findings were controversial—some researchers still doubt that proteins can resist degradation for tens of millions of years—Schroeter is one of a small but growing number of researchers specializing in the analysis of ancient proteins, or paleoproteomics, to learn about the biology of organisms past. It’s been a goal of scientists for some time now; in the 1950s, several researchers were already discussing the possibility of studying peptides preserved in fossils. But only in the last two decades have advances in techniques for protein analysis, such as mass spectrometry, made the feat practical. More.

The main problem with new sources of information is that, at one swoop, they eliminate the distinction between the tenured lectern-splinterer and some grubby individual like Schweitzer who just shuts up and digs.

The rest of us should sit back and enjoy the show.

See also: Is Mark Armitage’s soft dinosaur tissue work a replication of Mary Schweitzer’s? If so…?

and

More news from the decline: Revealing responses to creationist’s wrongful dismissal over soft dinosaur tissue discovery

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