Precise imaging technique confirms the protection of hemoglobin in the dinosaur bone

In a new research by North Carolina State University, two dinosaurs identified the bone squeezes in the bone squeezes, and it shows that this molecule is original for these animals. The work also shows that the ham, a small molecule that gives hemoglobin the ability to carry oxygen into the blood, deteriorates over time. Studies both have increased the body of the evidence that biological remnants can and can maintain deep time in some gems and provide more insights about the process of giwim.

Soft, continuous tissues exported from two dinosaurs – Brechilofosis Canadians and Tyranosurus Rex – has been the subject of numerous studies over the past two decades, researchers have used numerous methods, including high resolution imaging, antibody testing and protein -diarrhea.

I in a new research Royal Society A action A: Math, Physical and Engineering ScienceResearchers used imaging to resonate Raman (RR) of tissues to confirm the presence of both hammers, which are bound to gluten protein and hem is bound to goatite, which is a mineral associated with oxidation of iron.

“Raman spectroscopy mainly uses light waves to identify the energy -filled ‘fingerprint’ of the ino,” says Hans Helen, a professor at NC State Physics. “

“Additionally, the type of molecule resonates to give high signal levels so that its signal is ‘overwhelmed’, the signal of other types of molecules.” “This strong signal allows us to find the needle (hemoglobin remains) in grass (Messi Fusal) to see how this molecule has changed from the active living condition, which shows that the molecules of chemical changes have passed through the molecules.”

Researchers used RR to target molecules with Ham Globin Bond. He looked at the samples of Brechlovovsor, Tea -CRACs, eliminated the modern shooter bone and human blood.

“The increase in the signal shows that hemoglobin is present, but changes in the signal also allow us to see that as hemoglobin harasses, gothite can be made on iron inside hemoglobin,” says Halin. “We can also indicate where the structure like the ham ring is damaged. And we have seen this process in both modern and ancient samples, so we know that it is quite fast after death.”

The results also reject the possibility of sample pollution.

“Raman spectroscopy will tell you which molecular bonds are not special, so the molecular bonds are not special, so those bonds can come from anywhere,” says Mary Shaitzer, a biology professor at NC State and Study co -author.

“RR identifies both bonds and structures. So we know that the ham is there, and it is still bound to hemoglobin protein. Collective people like bacteria do not have specific bonds, so we can say that molecules are from animals, or in this case.”

Researchers also explains how harassment of ham and understanding of change over time can help to explain how stomach is and why molecules can be sustained in millions of years.

“Although the biggest search is that we can use the RR to show that hemoglobin pieces can last for tens of millions of years, but we have also achieved some incredible insight into how the molecules have changed,” says Halin, “Although we can use the RR to show it, we have also achieved some incredible insight into how we have changed molecules.” “Givetite is a mineral crystal known as bio, which means it is formed by biological action. But we did not know that it could tie and strengthen the protein pieces.”

“The ham has been identified in the swords that are far more older than dinosaur, so we know it’s intact,” says Schotszer. “Understanding why hemoglobin is safe, and the role that hem plays in the process is really important if we want to know how these ancient innovatives live over time.”