Introduction
Carbohydrates are one of the four classes of macromolecules needed for life. Every cell is coated with carbohydrates, specifically chains of sugar molecules called glycoconjugates or glycans. All known cells have a vast array of complex, information-bearing glycans covering the surface of their membranes, covalently bonded to either a protein or a lipid.[1] These complex saccharides (the glycans) are crucial for cell regulation and communication.[2] In fact, glycans – specifically glycoproteins and glycolipids – are involved in almost every life process as well as almost every major disease.[3] They participate in metabolism, cell communication, signaling and recognition, and cell structure. Learning about glycans has enhanced our understanding of disease, inflammation, infection, autoimmunity, cancer, real biological age, prognostic tests for health, precision medicine, and Alzheimer’s disease. For example, our knowledge of glycans has resulted in the recent invention of new anticoagulants, antibiotics, and antiviral drugs.[4] A glycan based anti-cancer vaccine is also currently in development.
The presence and construction of glycans involves much more than the genome, integrating epigenetic and environmental components. To participate in such a vast variety of processes, glycans must contain significantly more information than DNA. Humans have about 25,000 genes, which code for about 100,000 proteins. Comparatively, there are over 100,000,000 glycoproteins. Glycans have significantly more structural diversity and regulatory function than any other biological molecule.[5] Therefore, the study of any aspect of cellular activity or interaction must consider the role of glycans.
Surprisingly, two of the most popular origin of life textbooks (Smith & Morowitz, The Origin and Nature of Life on Earthand Luisi, The Emergence of Life) don’t even mention glycans. They are also rarely mentioned in introductory biology and biochemistry texts.[6] Even so, biologists are increasingly appreciating the epigenetic nature of glycans and the importance of the additional layers of cellular information glycans provide beyond the genome.[7]
In this paper, I will present four main arguments in support of the intelligent design of glycans. First, glycans present us with a chicken and egg paradox. We have found glycans on every cell nature has ever produced, but the monomeric sugars used to make the glycans are only produced by life. The paradox is explaining how early life forms obtained the materials to make the first glycans. Second, glycans contain more information than the genome and have an extraordinarily complex structure representing specified information. Third, glycan synthesis involves a complex collection of parts all working together, which is a hallmark of a designed system. Finally, glycan synthesis requires more than 500 enzymes, but the production of the glycans is not template-driven, making the evolution of glycans beyond the reach of random mutations.[8] Therefore, glycobiology doesn’t fit the evolutionary paradigm. According to biophysicist Dr. Cornelius Hunter, glycans contradict common descent.[9]
Glycan Basics
Glycans are the “dark matter” of biology.[10] The structural complexity of glycans and the fact that they are not synthesized from a DNA template makes it difficult to determine their structure and exact functions. Because of this, studies of glycans have lagged behind other major classes of biomolecules. Glycobiology investigates the structure, synthesis, function, and evolution of glycans, as well as their associated enzymes and proteins.[11] Glycans can exist covalently bonded to lipids, but most glycans exist as glycoproteins, which are oligosaccharides covalently attached to a protein. Some glycoproteins are more than 70% sugar by weight, with the sugar filling equal or more volume than the protein. Common connections between the sugar and the protein occur at the amino acids serine, threonine, and asparagine.
The human genome cannot account for our complexity. The addition of glycans changes the properties of a protein. Therefore, glycans compensate for our limited genome through posttranslational modification of the proteins to create a much larger collection of more diverse proteins.[12] The presence of glycans help to explain how such a relatively small genome can account for the variety of organisms and their tissues. For example, specific glycans added to the proteins that make up cartilage and tendons improve the flexibility of these structures. Glycans also stabilize the structure of protein, help in the prevention of degradation by proteases, control the physical maintenance of tissue structure and integrity, and direct the protein to the chaperones for proper folding. On the surface of the cell, glycans are responsible for intercellular communication, cell recognition, receptor ligand binding, and cellular addition. Glycans are also known to mediate the interaction between cells and other organisms, such as viruses.
In eukaryotes, N-linked glycoproteins are attached to the amide nitrogen atom in the amino acid asparagine. These specific glycans are highly branched and made in the endoplasmic reticulum (ER) with resident enzymes called glycotransferases (GTs). At the Golgi apparatus (GA), sugars are removed by glycosidases (GDs) while others are added using GTs. This occurs through an intricate and variable network of carbohydrates and enzymes that produce very specific glycoproteins. The added sugars help to fold the protein and also provide an address to direct the protein to a specific location. This labeling is directly analogous to an airline destination and identification tag on checked baggage. O-link glycans are attached to the oxygen in the amino acid serine or threonine. These are built up one residue at a time in the GA using resident GTs. They can be more extensive than N-linked and also help deliver proteins to specific locations, participate in immune response, assist in the recognition of foreign material, and help control cell metabolism. Glycolipids, destined to be embedded in the cell membrane, are produced in the GA and require their own set of enzymes.
The Sugar Paradox
Several sugar monomers are used as the building blocks of glycans. Before glycan construction can begin, cells must obtain the needed monosaccharrides. Vertebrates use ten simple sugars as building blocks.[13] Once inside the cell, the monosaccharide building blocks are processed by enzymes (activated) and then sent to the ER and the GA.
We have not found a life form without glycans. Paradoxically, the six-carbon sugars used in glycans are not found in nature outside of life.[14] It is likely that the only sugar used in the construction of glycans that could have been produced prior to the existence of life was xylose (a five-carbon sugar), which was found in the Murchison meteorite. As far as we know, all other sugars must be created by a life form. Vertebrate cells can build all the needed simple sugars starting from glucose. However, the sugars that are only created by existing life are also needed for life to exist. To avoid this paradox, one must postulate the existence of a life form without glycans. This early form of life must subsequently evolve not only mechanisms for building the monosaccharides but also the enzymes to process them. This impossibility is addressed in the section “Glycans Contradict Evolution.”
It is unlikely that the needed sugars could have formed on the early Earth prior to the existence of life. The only known prebiotic route to create a sugar is the formose (also called the Butlerow) reaction.[15] This reaction begins with formaldehyde, which was probably available on the early Earth but requires an inorganic catalyst such as calcium hydroxide. In addition, unless an initiator such as an aldehyde is also present, the formose reaction won’t occur. Instead, the formaldehyde most likely would undergo the Cannizzaro reaction, in which formaldehyde reacts with itself to form methanol and formic acid.[16] In addition, the formose reaction produces a random and unusable mixture of sugars. For example, D-glucose has five stereogenic centers, so it has 32 possible isomers. Even one hydroxyl group out of place represents a different monomeric sugar. Sugars are also subject to several side reactions. On the early Earth, these unwanted reactions would create useless mixtures of chemicals, appropriately termed "asphalts."[17] Nature can’t pull out the specific needed molecule from the asphalt mixture.
In addition, the first sugars could not have been made in the same location as the first proteins (to produce glycoproteins). Ammonia and amino acids react with formaldehyde and sugar and consume the products. Sugars undergo the Maillard reaction with proteins and amino acids. This reaction is responsible for the compounds that give browned food its distinctive flavor. Sugars also decompose rapidly at a non-neutral pH. For example, the half-life of sugars in deep-sea hydrothermal vent conditions is seconds.[18]
Life needs sugar, but life is required to create the sugar molecules. This provides evidence for an irreducibly complex system that needed the protein forming mechanism, the monomeric sugars, and the sugar forming mechanism to all appear simultaneously.
The Information in Glycans
The glycome contains significantly more information than the genome, the proteome, and the lipidome.[19] As sugar monomers are linked together, the glycosidic hydroxyl group of one sugar can react with one of several hydroxyls of another sugar. Thus, sugars can form numerous polysaccharides with a large number of linkage possibilities. For example, six D-hexose monomers can be linked together in more than one trillion ways.[20] Each different isomer has different structural properties. If information is defined as reducing the number of possibilities, then each specific linkage adds information to the glycan molecule. In this way, carbohydrates form the third alphabet of life.[21] As noted previously, the information content in glycans is orders of magnitude larger than DNA.
The formation of glycans is more difficult and more structurally complicated than the other biopolymers. DNA, RNA, and proteins are linked in a linear manner with the same repeating phosphodiester and amide linkages. In comparison, glycans can be branched, and each link forming a glycan can be different. Each hydroxyl group can be a site for a linkage to another sugar. This structural complexity is represented by polysaccharide nomenclature. The names of glycans must include the monosaccharide units, the specific linkage (the position) for each monosaccharide, and the specific stereochemistry (the orientation) of each linkage.
Uncertainty is inversely related to information. Each specific linkage reduces the uncertainty in the possibilities for that specific glycan. The amount of information conveyed (and the amount of uncertainty reduced) is inversely proportional to the probability of a particular event. Each new sugar that is added reduces the probability of what the glycan structure will be. This is similar to writing a letter. Once a circle is drawn, you are limiting the probability of a specific letter to an O or a Q. This type of information, called Shannon information, is a way of measuring the amount of information in a sequence of symbols or a sequence of connections between sugars. However, if a specific arrangement of symbols performs a specific function, you also have specified information, like a language or a code. Specific information in the glycan structure is just like a language: being both improbable and specifically arranged to perform a function.[22] Evidence that glycans are a form of information comes from their operation as a code. The code represented by the structure of extracellular glycans is responsible for intercellular communication.[23] This code is a complex molecular language made up of a 10-monosaccharide “alphabet” that can be arranged in a vast variety of structural “words.”[24]
Information is not material but can be coded by material and transferred between mediums. The information in glycans can be transferred to another medium to control processes in the cell. For example, glycosylated histones play a role in gene expression. Most likely, glycans represent epigenetic information that plays a part in activating or stopping the expression of specific proteins or enzymes. Glycoproteins gather information from the environment and provide information to the cell. Glycan information is also used to fold the protein or get the protein to the correct location. The complex structure of glycans acts as a crucial source of information for almost every process in a cell.
Glycan Synthesis Is Complex
The synthesis of N-linked glycoproteins occurs in factory-like, assembly-line fashion that requires multiple unconnected layers of regulation, with every step requiring an enzyme. Glycans result from coordinated assembly pathways, each with a network of enzymes, and each building on or degrading the product of prior steps.[25] First, glycan synthesis requires that the monosaccharide building blocks be activated to a high-energy donor form before they can be hooked together. This occurs through the enzymatic addition of a nucleoside triphosphate and another monosaccharide with a phosphate at the anomeric carbon. After being activated, the monosaccharides are sent to the ER and the GA. Prior to their arrival in the ER, a dolichol phosphate must be embedded in the lumen of the ER. The activated sugar is then attached, along with a second phosphate to the dolichol compound. The activated sugars are then added to part of the dolichol molecule sticking outside the of the ER into the cytoplasm. Linking together sugars is energetically unfavorable, so the reaction must be coupled to the hydrolysis of two ATP molecules.
The activation of the sugar and these first steps in glycan production must occur in the cytoplasm of the cell with specific activation enzymes and GTs that also reside in the cytoplasm. A flippase enzyme then translocates the sugar end of the dolichol-sugar complex to the inside of the ER. More activated sugars are attached using other GTs that reside inside the ER. These sugars must be attached inside the ER, and they use a different compound for activation, which requires different enzymes.
While inside the ER, the polysaccharide is then added to a translated protein, which is still attached to the ribosome. The sugars then assist in properly folding the protein, which is then severed from the dolichol structure and the ribosome with different enzymes. The ribosome is also a machine which requires its own regulation and a specific set of enzymes to build the protein. Once cleaved from the ribosome and the dolichol structure, the glycoprotein is encased in a vesicle and then moved from the ER to the GA with dynein. This transfer requires a communication system between the ER and GA, along with enzymes to build the microtubule tracks on which the dynein walks. More enzymes are needed to attach and detach the vesicle. The glycoprotein is then moved through the GA and modified by removing and/or adding more monosaccharides, again using activated sugars and requiring a different GT or GD for each different sugar linkage. Finally, the glycoprotein must be moved to the cell membrane. The synthesis of O-linked glycoproteins occurs solely in the GA, requiring different enzymes. In eukaryotes, protein glycosylation involves hundreds of molecular actors. For example, human N- and O- glycan processing involves over 500 enzymes.[26]
N-glycan structures demonstrate incredible diversity, with vast amounts of information being added without genome modification.[27] This non-templated process is controlled at multiple seemingly unconnected levels in the cytoplasm, ER, and GA.[28] Genes do not directly encode the synthesis of the glycans, but the branching structures are assembled and chemically modified by enzymes, which are template-encoded in DNA.[29] Genes code for the enzyme, which in turn performs a specific task in a specific location to build a glycan. There are at least nine separate systems (sugar uptake, sugar activation, embedding of the dolichol, the assembly outside the ER, assembly inside the ER, assembly in the GA, ATP production, transcription, and distribution) with direct analogies to supply, manufacturing, warehouse storage, and delivery, all working together for the united purpose of creating a single glycoprotein. A coordinated collection of individual systems all working together toward a single goal is the definition of engineering.
Glycans Contradict Evolution
The yeast genome consists of about 6000 genes.[30] Before this genome was sequenced, it was estimated that far more genes would be required for an organism to carry out all its functions. The nematode, C. elegans, was found to have about 15,000 genes, and a fruit fly about 20,000 genes. From these first genome sequences, evolutionary-based estimates required the human genome to be over 100,000 genes. Contrary to the predictions of evolutionists, the human genome turned out to be only around 25,000 genes, not much larger than C. elegans or a fruit fly.
Genomic size cannot account for the complexity of an organism. Non-template controlled posttranslational protein modifications are needed to explain the biological complexity. The necessity of glycans to explain the complexity of life calls into doubt the assumption that DNA and RNA can explain the makeup of cells, tissues, organs, and physiological systems. Glycans demonstrate that there is much more to the central dogma of molecular biology. The theory that genetic information only moves from DNA to RNA to protein is incorrect.
Glycans on the surface of cells can react and rapidly change when presented with a pathogen or other environmental pressures.[31] These structural variations in the glycan chains represent epigenetic regulation occurring through the sophisticated enzymatic machinery described in the previous section. These adjustments demonstrate that the flow of information is not limited to one direction.[32] The complete mechanism responsible for this adjustment is unknown but would require the production of new enzymes to create the new linkages as well as the removal of the old enzymes that made the previous linkages. Mutation and natural selection cannot account for these rapid adjustments.
This adjustment of the glycome doesn’t just occur in response to environmental pressures. It also changes from the embryonic state to a differentiated state as the organism develops. Each cell has its own distinct glycome that is different from the glycome of the embryonic state. Despite the tremendous number of possible glycan structures, only a limited subset of possible structures are found in eukaryotes. Curiously, bacteria and archaea experience more diverse O-liked glycosylation in terms of the range of monosaccharides and the types of linkages and modifications.[33] It appears odd and seemingly contradicts orthodox evolutionary theory that glycans in a more advanced organism demonstrate less complexity while earlier life forms contain many more enzymes, more complexity, and more information.
Some of the enzymes responsible for the structural variations of glycans in eukaryotes are also found in a wide range of bacteria with no evolutionary connection to eukaryotes. This doesn’t fit the standard evolutionary narrative. It is highly improbable that a significant portion of the genome evolved twice to code for enzymes that operate on a system that uses compounds (sugars) that aren’t coded for in DNA.[34] Since the glycan processing system operates without a template, it is blind to natural selection.
There is a surprising diversity of glycoproteins among mammals.[35] Common descent does not predict that glycobiology would be organism specific. Glycans occur in a discontinuous and puzzling (from an evolutionary perspective) distribution across evolutionary lineages.[36] N-glycan processing in the GA involves a large repertoire of organism-specific GDs and GTs as well as other enzymes required for specific substitution.[37] This includes humans. The presence of sialic acid on human glycans is very different from the hominids from which we supposedly descended and provides evidence for human exceptionalism.[38] We have a unique glycobiology that doesn’t fit with the predictions of standard evolutionary theory and necessitates a different explanation for the origin of life.
Theological Implications
Glycans add another level of complexity to the origin of life. But even before the discovery and illumination of the complexities of glycobiology many scientists questioned whether life could have originated on Earth. Names as notable as Francis Crick, Fred Hoyle, and Richard Dawkins have postulated that life originated elsewhere in the universe. This is an acknowledgment of the improbability of life arising through a purely natural process on Earth and that some unknown and extra-Earthly process must have created life. Romans 1:20 states that everyone will recognize God’s attributes through creation; the identification of design in life leaves us without excuse. The sugar paradox, information and engineering, and evolution-contradicting evidence makes the intelligent design of glycans reasonable and points us to a transcendent intelligence.[39] The postulation of panspermia is a tacit recognition of this needed otherworldly cause.
Glycans present us with a chicken and egg paradox. Life is the only process that creates sugar, but sugar is required for life. The simultaneous creation of the sugars and the processes that need them is a reasonable solution to this paradox. This is evidence for the necessity of a designing intelligence.
The theory of panspermia doesn’t solve the glycan chicken and egg paradox, and it also doesn’t explain the origin of specified biological information.[40] Structures exhibiting specified information like a language, integrated circuits, and computer code are the result of a mind. Intelligent design theorist Stephen Meyer states that “in all cases where we know the causal origin of ‘high information content,’ experience has shown that intelligent design played a causal role.”[41] Our repeated experience is that only a mind can generate complex specified information as well as a hierarchically arranged system of parts. Since glycoconjugates display this type of information, a reasonable conclusion is that they, and the systems that produce them, are a product of a mind.
In his book Intelligent Design, William Dembski described his explanatory filter. This filter provides a simple way to check if a system is the product of intelligent design.[42] He updated the explanatory filter in 2023.[43] Based on this updated filter and the fact that the coordination of glycan-creating systems is both improbable and specified, the systems that create glycans and glycoproteins are an example of intelligent design. Many separate processes had to be integrated, engineered, and properly arranged to allow for the one common purpose of the construction of glycoconjugates. A hierarchy of parts within parts organized to perform a higher function only occurs when created by a mind. Therefore, it is reasonable to conclude that glycobiology is also the product of a mind.
We never observe physics, chemistry, and chance organizing a hierarchical, integrated system of parts, all focused on a single purpose. However, according to naturalistic, orthodox Darwinian thinking, life emerged in exactly this way and is therefore a lucky accident. However, a reasonable conclusion from our current knowledge of glycans is that life is not an accident and instead is the creation of a super-intelligent mind.
[1] James Tour, “An Open Letter to My Colleagues,” Interference 3, no. 2 (August 2017). https://inference-review.com/article/an-open-letter-to-my-colleagues.
[2] Ibid.
[3] Dr. Hudson Freeze, “The Role of Glycans in the Medicine of Tomorrow: Insights from 11 Leading Scientists,” YouTube Interview on GlycanHub podcast, August 29, 2023. https://youtu.be/JyKBeXLV0ao?si=P9CM62qkO90vsaou.
[4] Dr. Umesh Desai, “Fundamentals of Glycan Structure 1,” YouTube lecture on Translational Glycomics Center channel, February 4 – April 22, 2019. https://www.youtube.com/watch?v=Aq7i5D3TLQs&t=4861s.
[5] Steven A. Springer and Pascal Gagneux, "Glycan evolution in response to collaboration, conflict, and constraint," Journal of Biological Chemistry 288, no. 10 (2013): 6904-6911.
[6] Cornelius Hunter, “FP9: Serological Tests Reveal Evolutionary Relationships,” YouTube video on Darwin’s God, posted on February 16, 2024. https://youtu.be/mnzvgRhwsyA?si=W_RVg67dzTmVZEUO.
[7] Change Laura Tan and Rob Stadler, The Stairway of Life: An Origin-of-Life Reality Check, (self-published, 2020), 174.
[8] Cornelius Hunter, “FP9: Serological Tests.”
[9] Ibid.
[10] Ajit Varki, “Glycans: The ‘Dark Matter’ of the Biological Universe,” Jay John Listinsky Lecture in Glycobiology on UAB Pathology YouTube channel, posted in 2022. https://www.youtube.com/watch?v=f2c1dS_KQcY&t=1818s.
[11] Ajit Varki, RD Cummings, JD Esko, et al., editors. Essentials of Glycobiology [Internet]. 4th edition. (Cold Spring Harbor, NY: Cold Spring Harbor Laboratory Press; 2022) Chapter 1. Available from: https://www.ncbi.nlm.nih.gov/books/NBK579918/doi: 10.1101/9781621824213.
[12] et al., “The Sequence of the Human Genome,” Science 291 (2001): 1304-1351. doi:10.1126/science.1058040.
[13] Carolyn Bertozzi (Berkeley), iBiology Techniques, Nov. 13, 2013, YouTube Video Lecture. https://youtu.be/Ys5kPW4u_qs?si=50X0ph7Xhsflz9nD.
[14] Y. Furukawa, Y. Chikaraishi, N. Ohkouchi, N.O. Ogawa, D.P. Glavin, J.P. Dworkin, C. Abe, & T. Nakamura, “Extraterrestrial ribose and other sugars in primitive meteorites,” Proc. Natl. Acad. Sci. U.S.A. 116, no. 49. (2019): 24440-24445. https://doi.org/10.1073/pnas.1907169116.
[15] Fazale Rana & Hugh Ross, Origins of Life: Biblical and Evolutionary Models Face Off, (Covina, CA: Reasons to Believe, 2014), 115.
[16] Fazale Rana, Creating Life in the Lab: How New Discoveries in Synthetic Biology Make a Case for a Creator, (Grand Rapids, MI: Baker Books, 2011), 159.
[17] Steven A. Benner, “Paradoxes in the Origin of Life,” Orig Life Evol Biosph 44, (2014):339-343, doi: 10.1007/s11084-014-9379-0.
[18] Fazale Rana & Hugh Ross, Origins of Life, 104.
[19] Ajit Varki, “Glycans: The ‘Dark Matter’ of the Biological Universe.”
[20] Russell W Carlson, "The Complexity of Glycan Structures, Functions, and Origins," BioCosmos 4, no. 1 (2024): 57-78.
[21] Herbert Kaltner José Abad-Rodríguez Anthony P. Corfield Jürgen Kopitz Hans-Joachim Gabius, “The sugar code: letters and vocabulary, writers, editors and readers and biosignificance of functional glycan–lectin pairing,” Biochem J 476, no. 18 (30 September 2019): 2623–2655. doi: https://doi.org/10.1042/BCJ20170853.
[22] Stephen C. Meyer, Signature in the Cell: DNA and the Evidence for Intelligent Design (New York: Harper Collins, 2009), 88-110.
[23] Wanke, Alan, Milena Malisic, Stephan Wawra, and Alga Zuccaro. "Unraveling the sugar code: the role of microbial extracellular glycans in plant–microbe interactions." Journal of Experimental Botany 72, no. 1 (2021): 15-35.
[24] Wei, Yuanyan, Anning Wei, Yirong Li, Yuerong Yang, Yu Si, Yi Li, Zhijun Fan, and Jianhai Jiang. "Deciphering the cell surface glyco-code: a promising perspective on unveiling the vulnerability of cancer stem cells." Cancer Biology & Medicine 21, no. 11 (2024): 963-969.
[25] Steven A. Springer and Pascal Gagneux, "Glycan evolution in response to collaboration, conflict, and constraint," Journal of Biological Chemistry 288, no. 10 (2013): 6904-6911.
[26] Charlotte Toustou, Marie‐Laure Walet‐Balieu, Marie‐Christine Kiefer‐Meyer, Marine Houdou, Patrice Lerouge, François Foulquier, and Muriel Bardor. "Towards understanding the extensive diversity of protein N‐glycan structures in eukaryotes." Biological Reviews 97, no. 2 (2022): 732-748.
[27] Ibid.
[28] Colin Reily, Tyler J. Stewart, Matthew B. Renfrow, and Jan Novak. "Glycosylation in health and disease." Nature Reviews Nephrology 15, no. 6 (2019): 346-366.
[29] Stevan A. Springer, and Pascal Gagneux. "Glycan evolution."
[30] Carolyn Bertozzi (Berkeley), iBiology Techniques.
[31] Steven A. Springer and Pascal Gagneux. "Glycan evolution.”
[32] Herbert Kaltner “The sugar code.”
[33] Ajit Varki, “Essentials of Glycobiology,” Chapter 20.
[34] Cornelius Hunter, “FP9: Serological Tests.”
[35] Pascal Gagneux and Ajit Varki. "Evolutionary considerations in relating oligosaccharide diversity to biological function." Glycobiology 9, no. 8 (1999): 747-755.
[36] Joseph R. Bishop and Pascal Gagneux. "Evolution of carbohydrate antigens—microbial forces shaping host glycomes?" Glycobiology 17, no. 5 (2007): 23R-34R.
[37] Charlotte Toustou, "Towards understanding the extensive diversity of protein N‐glycan structures."
[38] Ajit Varki, "Multiple changes in sialic acid biology during human evolution." Glycoconjugate journal 26 (2009): 231-245.
[39] Stephen C. Meyer, “What is the Evidence for Intelligent Design and What Are Its Theological Implications,” The Comprehensive Guide to Science and Faith: Exploring the Ultimate Questions About Life and the Cosmos, edited by William Dembski, Casey Luskin, and Joseph M. Holden (Eugene, OR: Harvest House Publishers, 2022), 149.
[40] Stephen C. Meyer, “What is the Evidence for Intelligent Design,”149.
[41] Stephen C. Meyer, “The origin of biological information and the higher taxonomic categories,” Proceedings of the Biological Society of Washington, 117 (2004): 213-239.
[42] William A. Dembski, Intelligent Design: The Bridge Between Science and Theology (Downers Grove, IL: InterVarsity Press, 1999), 134.
[43] William A. Dembski, “The Explanatory Filter,” YouTube video on Discovery Science. Posted on December 12, 2023. https://www.youtube.com/watch?v=2RvKxxTnbUU.
