Squishosaur scepticism squashed
Tests confirm proteins found in T. rex bones
We first reported in 1997 that soft tissue in fossil Tyrannosaurus rex had been found (see Sensational dinosaur blood report! and response to critic). In 2005, in the midst of strong scepticism toward the original findings, new images showed plainly that the soft tissue was ‘fresh’ organic tissue (see Still soft and stretchy). Nevertheless, many evolutionists and long agers (See Squirming at the Squishosaur) have remained sceptical, due in part to creationists pushing the point that it provides solid evidence that these bones are not over 65 million years old but much younger (see ‘Schweitzer’s dangerous discovery’).
Now a recent paper published in Science by a research team involving Mary Schweitzer, the principal scientist involved in the previous findings, describes the presence of collagen (an important structural protein for bone tissue) in the T. rex bone.1 However, in a companion paper in the same issue,2 the researchers claim that the sequenced T. rex proteins show it is related to birds. While much media attention has been paid to the claim that the protein sequencing shows that T. rex is related to the chicken, the most exciting part for creationists is that collagen has been found in fossil T. rex bone.
Proteins or pretenders?
Despite the evolutionary speculation attached to this research that has been blown out of proportion (see below), these papers present some solid experimental science. Because many evolutionists have been sceptical of the claims of organic residues found in T. rex fossils, the researchers went to great lengths to show that the organic material found in the fossil T. rex bones was actually from the T. rex bones. They conducted a series of tests to show that the protein found, collagen, was from the bone tissue of the T. rex.1
- They imaged the bone using a number of different types of microscopy techniques after they had dissolved most of the minerals away, leaving the organic tissue (demineralized). They found, in two out of the three methods used, that the bone had a fibrous nature like modern ostrich bone. Further tests from the third method suggested that the material in the bone had changed little from the living state.
- The elasticity of the demineralized T. rex bone was compared to a modern demineralized ostrich bone. They showed that the T. rex bone performed like the ostrich bone in how it reacted to mechanical loading and unloading.
- Slices of the T. rex were tested to see if the bone would produce an immune reaction to collagen antibodies, which it did. To further show that the immune reaction of the antibodies was not an error, they also did the antibody test after the bone had been treated with enzymes that specifically degrade protein. The T. rex bone did not show any reaction to the collagen antibodies after it was treated.
- The chemical composition of the demineralized bone was tested using mass spectrometry. They found that the results were consistent with collagen fibres being in the actual bone, but didn’t show any sign of the required amino acids in the rock that encased the fossil.
- A protein sequence from T. rex was mapped and compared to other living creatures, such as a frog, a newt and a chicken. The results showed a 58% similarity with the chicken and 51% with the newt and frog.
That’s a lot of tests! Moreover, they repeated the tests numerous times. The tests have been conducted independently in three different labs, all suggesting that the proteins come from the bone and are not due to contamination.1 However, such has been the level of scepticism among evolutionists that these tests needed to be done. This scepticism was originally well-founded from an evolutionary point of view as well—how could such biological molecules and structures survive for 68 million years? The maximum possible time assumed for collagen to be preserved under the most favourable preservation conditions at 0°C was 2.7 million years, at 10°C was 180,000 years and at 20°C was 15,000 years.3 Interestingly, they have noted that results from the most recent cuttings of the bone showed less collagen than earlier ones, suggesting bone degradation since 2003. But Schweitzer et al. have shown solid evidence that these structures do in fact belong to the original T. rex bone. As we have stated many times before, this evidence is wonderfully consistent with a recent creation and worldwide Flood according to the Bible, and continues to pose more problems for evolution and millions of years.
T. rex turning into a chicken?
Not surprisingly, the researchers have tried to paint these findings with an evolutionary brush by comparing the protein sequences found in the T. rex bones to various animals. Since the T. rex protein was more similar to chicken protein than any other it was compared to, many news stories have paraded it as evidence of dino-to-bird evolution.4 However, the original paper documents a sequence similarity in the T. rex and chicken proteins of only 58% compared to 81% similarity between humans and frogs.2 If the similarity between humans and frogs, which are supposed to be distantly related, is 23% higher than the similarity between the T. rex and the chicken, which are supposed to be more closely related, there is no evolutionary significance at all in these findings. The researchers also acknowledged that the number of relevant protein sequences they had was limited. They were not able to compare it to what would be expected to be more closely related (and even creationists would expect to be more biochemically similar) animals, such as crocodilians.
Will anything change?
The presence of collagen in T. rex bones hasn’t changed the researchers’ faith in evolution and millions of years. Schweitzer et al. conclude:
‘The presence of original molecular components is not predicted for fossils older than a million years, and the discovery of collagen in this well-preserved dinosaur supports the use of actualistic conditions to formulate molecular degradation rates and models, rather than relying on theoretical or experimental extrapolations derived from conditions that do not occur in nature.’1
In other words, rather than relying on experimental data we have for how long it takes for organic molecules to degrade, we have to rely on some unknown ‘specific conditions’ that have allowed these structures to survive for millions of years.
It’s this sort of special pleading that is the hallmark of evolutionary thinking. Not only do evolutionists have to appeal to unknown ‘special conditions’ to save the proteins, but they must remain in that condition for 68 million years! Let the reader observe the desperation in these comments to save the millions of years in the light of the blindingly obvious: these soft tissues remain because these bones are not millions of years old.
- Schweitzer, M.H., Suo, Z., Avci, R., Asara, J.M., Allen, M.A., Arce, F.T., and Horner, J.R., Analyses of soft tissue from Tyrannosaurus rex suggest the presence of protein, Science 316(5822):277–280, 2007. Return to Text
- Asara, J.M., Schweitzer, M.H., Freimark, L.M., Phillips, M., and Cantley, L.C., Protein sequences from mastodon and Tyrannosaurus rex revealed by mass spectrometry, Science 316(5822):280–285, 2007. Return to Text
- Nielsen-Marsh, C., Biomolecules in fossil remains: A multidisciplinary approach to endurance, The Biochemist, pp. 12–14, June 2002, http://www.biochemist.org/bio/02403/0012/024030012.pdf Return to Text
- See e.g. Rincon, P., Protein links T. rex to chickens, BC12 April 2007; Bryner, J., T. rex related to chickens, 12 April 2007. Return to Text