Fragments of various animal proteins have been found in several different dinosaur fossils. Results of experimental decay studies clearly indicate that even small fragments of these proteins will not survive for millions of years. Critical challenges to this experimental evidence fail to adequately address known protein biochemistry. Instead, the persistence of these proteins continues to present a significant conflict with the assigned ages of dinosaur fossils.
The presence of tissue, cells, and proteins still remaining in dinosaur fossils poses a direct biochemical challenge to the standard geologic dating paradigm.1 How could bones dated at over 65 million years old still contain pliable tissue and fragments of proteins? The examples of preserved dinosaur tissue continue to grow, and the conflict with evolutionary-biased dating schemes is becoming increasingly insurmountable.
As part of ongoing research in this field, fragments of several different types of proteins have been detected in various dinosaur fossils. The most frequently detected protein is collagen,2 a common protein in all animal bone. While the structure of collagen makes it more resistant to degradation than most other proteins, it will still degrade in a predictable manner. As I described in a previous article,3 biochemical decay studies demonstrate that even under ideal conditions detectable levels of collagen do not survive much longer than about one million years.
Dr. Fazale Rana has challenged that these studies fail to accurately predict the decay rate of dinosaur collagen.4 He argues that because collagen decay experiments typically use high temperatures, the results are not applicable for the ambient subsurface temperature of a buried fossil. Instead, he suggests that these high temperatures introduce discrepancies into the experiment.
High temperatures (e.g., 80º C–90º C) are often used in laboratory studies to accelerate collagen’s degradation. Otherwise, at lower temperatures, decay will be considerably slower, likely extending experimental measurements of degradation by months or even years. In turn, the Arrhenius equation is used to convert the decay rates obtained from these high temperatures to rates at lower temperatures.5 Thus, high temperature measurements can be used to predict collagen degradation at ground temperatures.
Dr. Rana argues that the decay rates from high temperature studies may not fit within the parameters of the Arrhenius equation. He speculates that how collagen degrades at high temperatures may be chemically different than how it degrades at lower temperatures. He concludes that this difference will introduce errors into the mathematical conversion. This will result in predictions that collagen will degrade faster than it actually degrades in a buried fossil.6
Conversions using the Arrhenius equation are common practice in biochemical studies. The temperature dependence of chemical reactions is well established. So, I previously challenged Dr. Rana to provide experimental documentation of his assumption, and not just offer speculation.7
In response to my challenge, Dr. Rana claims that a 19728 study supports his position.9 He states that this study shows the denaturation temperature for collagen is well below the high temperatures used in degradation experiments. From this he surmises that collagen degrades differently at high temperatures than it does at lower temperatures. Rather, he suggests that denaturation unravels collagen’s triple helix first, thereby changing its structure. Rana speculates that once this structural change happens, collagen will degrade faster than it would degrade in its native, low-temperature structure.10 He concludes that the Arrhenius equation fails to account for this accelerated degradation after collagen has denatured. In other words, he assumes the Arrhenius equation will fail to properly convert the high temperature measurements to appropriate rates for lower temperatures.11
However, this 1972 study actually provides little experimental basis for Rana’s conclusions. The work does show that the denaturation temperature for some forms of collagen is lower than the 80º C–90º C typically used for degradation experiments. However, the study did not determine the actual rate of collagen degradation at any temperature.
Rana is suggesting that the “actual” degradation of collagen is at least 247 times slower than the mathematically predicted rate.
Dr. Rana simply makes the assumption that degradation at lower temperatures will be slower than predicted by the equation. In point of fact, he is assuming that it is considerably slower. Michael Buckley and Matthew Collins have studied collagen degradation for several decades. Based upon their analysis using high temperatures, they calculate the survival of bone collagen at about one million years, even under ideal environmental conditions.12 In contrast, collagen fragments have been found in a reptile fossil that is reportedly 247 million years old.13 According to this comparison, Rana is suggesting that the “actual” degradation of collagen is at least 247 times slower than the mathematically predicted rate.
Moreover, temperatures above collagen’s denaturation point may or may not cause degradation to differ from mathematical predictions. There is simply no current direct data to support Rana’s conclusion. Even if high temperatures do cause collagen to degrade more rapidly than the equation predicts, there is no experimental data supporting such a dramatic difference between “actual” and estimated (i.e., > 24,000% difference).
Plus, different forms of collagen denature at different temperatures.14 The 1972 study, cited by Rana, used muscle and skin collagen for its analysis. Collagen found in dinosaur fossils is bone collagen (i.e., mineralized collagen), which is more stable at high temperatures and has a far higher denaturation temperature than skin and muscle collagen.15 So, it is unlikely that results from the 1972 study are very applicable to bone collagen, thus neither are Dr. Rana’s conclusions. On the other hand, bone collagen was used as part of Buckley and Collins’s degradation studies,16 which report collagen survival as far less than 65 million years.
The arguments presented above have only addressed the persistence of collagen fragments. As I previously discussed,17 portions of other proteins are found in various dinosaur fossils as well. These other proteins, such as actin and tropomyosin, are not nearly as resistant to degradation as collagen. If collagen would likely not survive millions of years, these other proteins are even less likely to survive such a time span. Their presence is further direct biochemical evidence that dinosaur fossils are not millions of years old.18
In fact, Matthew Collins continues to struggle with the claims of dinosaur protein discoveries. He acknowledges that certain conditions may slow the rate of degradation, “but not by a lot.”19 “Since proteins decay in an orderly fashion,” he considers it very unlikely that any condition “could arrest protein degradation for tens of millions of years.”20 In other words, Dr. Collins knows proteins are far from immortal. Thus, he faces the conundrum of his evolutionist position: protein cannot last millions of years in a buried fossil, but he is unwilling to consider the possibility that the age of these fossils is not millions of years.
Not surprisingly, as with Collins, many in the evolutionist community are highly reluctant to accept the discovery of any dinosaur protein fragments. The presence of these proteins is simply not consistent with the assigned ages of the bones. In fact, their presence is completely contradictory to these ages.
If the persistence of proteins in dinosaur fossils is difficult to explain, then the retention of intact sheets of tissue should be considered even more astonishing. This tissue retains some of its original transparency, elasticity, and reactivity to specific antibodies. Such pliable tissue has been found in numerous dinosaur fossils by several different researchers.21 This tissue represents significant quantities of biological material within these fossils, not just trace amounts of protein fragments. The presumption that these sheets of tissue survived some 65+ million years of exposure to a host of potential environmental encroachments (e.g., ground radiation, microbial attack, and groundwater infiltration) stretches the bounds of biological preservation beyond any reasonable form of reality. It even stretches the bounds of imagination. It certainly stretches the limits of scientific credibility.
Tissue and individual proteins degrade at measureable rates and their use as a “clock” requires no more supposition or conjecture than other geologic dating methods.
The preservation of dinosaur tissue and protein remains strong direct biochemical evidence that these fossils are not millions of years old. Despite attempts to explain the presence of this biomaterial, there exists no viable explanation for its extensive preservation.22 What is more, other dating methods (such as radiometric measurements) do not automatically trump the relevance of this biomaterial. Tissue and individual proteins degrade at measureable rates and their use as a “clock” requires no more supposition or conjecture than other geologic dating methods.
Instead, tissue remaining in dinosaur bones is far more consistent with an age of thousands of years. While this is contrary to popular teachings, science is driven by discoveries that challenge the status quo of our understanding and open doors to new conclusions. Dismissing data that does not fit with current thinking always has the potential to be a “science stopper”—freezing the state of knowledge on a specific subject. It also can discourage critical analysis of accepted ideas, the very antithesis of the scientific process.
While evolutionists struggle to explain the persistence of dinosaur tissue in the fossil record, the presence of this tissue is evidence of a recent burial of the dinosaur bones. Degradation studies contradict claims that proteins could survive for millions of years inside a buried fossil. On the other hand, these protein decay studies are fully consistent with the conclusion that these fossils are only a few thousand years old.
Kevin Anderson, Echoes of the Jurassic, 2nd edition. Chino Valley, AZ: CRS Books, 2017.
For example, see Elena R. Schroeter et al., “Expansion for the Brachylophosaurus canadensis Collagen I Sequence and Additional Evidence of the Preservation of Cretaceous Protein,” Journal of Proteome Research 16, no. 2 (2017): 920–932, doi:10.1021/acs.jproteome.6b00873.
Kevin Anderson, “Dinosaur Tissue: A Biochemical Challenge to the Evolutionary Timescale,” Answers in Depth 11 (2016), https://answersingenesis.org/fossils/dinosaur-tissue/.
Fazale Rana, Dinosaur Blood and the Age of the Earth (Covina, CA: RTB Press, 2016), 68.
For a more detailed explanation, see Anderson, Echoes of the Jurassic.
Rana, Dinosaur Blood.
Anderson, “Dinosaur Tissue.”
Philip E. McClain and Eugene R. Wiley, “Differential Scanning Calorimeter Studies of the Thermal Transitions of Collagen. Implications on Structure and Stability,” Journal of Biological Chemistry 247, no. 3 (1972): 692–697, PMID: 5058222.
Fazale Rana, “Does Dinosaur Tissue Challenge Evolutionary Timescales? A Response to Kevin Anderson, Part 1,” http://reasons.org/explore/blogs/the-cells-design/read/the-cells-design/2017/01/11/does-dinosaur-tissue-challenge-evolutionary-timescales-a-response-to-kevin-anderson-part-1 (posted January 11, 2017). I find his title a bit odd. Dr. Rana identifies himself as a progressive creationist. Thus, he should not be overly concerned with challenges to evolution’s timescale. Yet, as biblical creationists have frequently argued, the standard geologic dating paradigm is built upon numerous evolutionary assumptions, which progressive creationists claim to reject but simultaneously accept the timescale based upon those assumptions. Dr. Rana also continues to appeal to radiometric dating as securely establishing the age for the fossils, effectively trumping any contradictory conclusions from indigenous protein and tissue. This appeal ignores the fact that, a) based upon the evolutionary assumption of great ages needed for universal common descent, relative ages for geologic periods were assigned decades before radioactivity was even discovered (e.g., see William Berry, Growth of a Prehistoric Time Scale: Based on Organic Evolution. Palo Alto, CA: Blackwell Scientific Publications, 1987), and b) the initial radiometric dates would not have been accepted had they failed to agree with, or even extend, these already assigned ages (e.g., see John Reed. Rocks Aren’t Clocks. Powder Springs, GA: Creation Book Publishers, 2013). Thus, radiometric dating is not an independent verification of the previously established evolutionary timescale, but is a direct product of that timescale. In addition, discordant radiometric dates are rarely adequately addressed in the literature (e.g., for a more detailed discussion see Andrew Snelling, Earth’s Catastrophic Past, vol. 2. Dallas, TX: Institute for Creation Research, 2009).
Denaturation disrupts the 3-dimensional structure of a protein, unwinding it into its primary amino acid peptide chain. Degradation causes further damage, breaking the bonds between the amino acids, fully destroying the integrity of the peptide chain.
Rana, “Does Dinosaur Tissue Challenge Evolutionary Timescales.”
Mike Buckley and Matthew James Collins, “Collagen Survival and Its Use for Species Identification in Holocene-lower Pleistocene Bone Fragments from British Archaeological and Paleontological Sites,” Antiqua 1, no. 1 (2011): e1, doi:10.4081/antiqua.2011.e1.
David Surmik et al., “Spectroscopic Studies on Organic Matter from Triassic Reptile Bones, Upper Silesia, Poland,” PloS ONE 11, no. 3 (2016): e0151143, doi:10.1371/journal.pone.0151143.
Matthew Collins et al., “A Basic Mathematical Simulation of the Chemical Degradation of Ancient Collagen,” Journal of Archaeological Science 22, no. 2 (1995): 175–183, doi:10.1006/jasc.1995.0019.
Collins, “Basic Mathematical Simulation.”
Buckley and Collins, “Collagen Survival and Its Use for Species Identification,” reports only 1% of bone collagen will remain after less than one million years even in “an optimal burial environment.” Caroline Wadsworth and Mike Buckley, “Proteome Degradation in Fossils: Investigating the Longevity of Protein Survival in Ancient Bone,” Rapid Communications in Mass Spectrometry 28, no. 6 (2014): 605–615, doi:10.1002/rcm.6821, reports difficulty in detecting bone collagen from archaeological samples dated over one million years of age.
Anderson, “Dinosaur Tissue”; see also Anderson, Echoes of the Jurassic.
A recent study has challenged previous descriptions of keratin and blood cells found in some fossils (Evan Saitta et al., “Experimental Taphonomy of Keratin: A Structural Analysis of Early Taphonomic Changes,” PALAIOS 32, no. 10 (2017): 647–657, doi:10.2110/palo.2017.051). Several media accounts of this study have misleadingly implied that this research draws into question all discoveries of dinosaur proteins and cells (e.g., “Dinosaur Blood? New Research Urges Caution Regarding Fossilized Soft-tissue,” https://www.eurekalert.org/pub_releases/2017-10/uob-dbn100917.php). Undoubtedly, this will lead some critics to claim that dinosaur tissue discoveries were mistaken, and that the material has now been shown to have just been an artifact.
The new study does suggest that descriptions of some dinosaur red blood cells may actually be an electron microscope (EM) artifact of degraded organic material. While it is always necessary to exercise caution when interpreting EM results (and anomalous structures can be a potential problem), the artifacts reported from this study do not have the detailed characteristics of the dinosaur red blood cells previously reported (Sergio Bertazzo et al., “Fibres and Cellular Structures Preserved in 75-Million-Year-Old Dinosaur Specimens,” Nature Communications 6, no. 7352 (2015); doi:10.1038/ncomms8352). Plus, the report assumes, but did not demonstrate, that once fossilized, this degraded organic material will still mimic the morphology of red blood cells. Moreover, bone osteocytes, which have been repeatedly found in several dinosaur bones, retain significant morphological detail not displayed by these EM artifacts.
Actually, a key focus of this recent study and that of a second study (Evan Saitta et al., “Low Fossilization Potential of Keratin Protein Revealed by Experimental Taphonomy,” Palaeontology 60, no. 4 (2017): 547–556) is the fossilization of dinosaur feathers. In particular, these studies analyzed the fate of keratin (a major protein in feathers). In their simulated burial and fossilization conditions, the researchers suggest that keratin structures degraded into nondescript masses. They conclude that keratin likely does not survive long enough to enable different feather patterns to be preserved in dinosaur fossils, calling into question some claims regarding feathered dinosaurs and feather evolution. These studies also call into question various claims that the chemical nature of keratin enables it to readily survive millions of years in geologic environments. In addition, a reanalysis of some reports of keratin survival in fossils may prove warranted. It should be noted, though, that these recent studies did not address the detection of other proteins or the persistent discovery of pliable tissue still remaining within dinosaur fossils.
Quoted in Robert Service, “Scientists Retrieve 80-Million-Year-Old Dinosaur Protein in ‘Milestone’ Paper,” Science, (2017), http://www.sciencemag.org/news/2017/01/scientists-retrieve-80-million-year-old-dinosaur-protein-milestone-paper.
See Anderson, Echoes of the Jurassic, for a detailed critique of different preservation theories.