Is the Laminin “Cross” Evidence for a Creator?

isthelaminincrossevidence

BY FAZALE RANA – JANUARY 31, 2018

As I interact with people on social media and travel around the country to speak on the biochemical evidence for a Creator, I am frequently asked to comment on laminin.1 The people who mention this protein are usually quite excited, convinced that its structure provides powerful scientific evidence for the Christian faith. Unfortunately, I don’t agree.

Motivating this unusual question is the popularized claim of a well-known Christian pastor that laminin’s structure provides physical evidence that the God of the Bible created human beings and also sustains our lives. While I wholeheartedly believe God did create and does sustain human life, laminin’s apparent cross-shape does not make the case.

Laminin is one of the key components of the basal lamina, a thin sheet-like structure that surrounds cells in animal tissue. The basal lamina is part of the extracellular matrix (ECM). This structure consists of a meshwork of fibrous proteins and polysaccharides secreted by the cells. It forms the space between cells in animal tissue. The ECM carries out a wide range of functions that include providing anchor points and support for cells.

Laminin is a relatively large protein made of three different protein subunits that combine to form a t-shaped structure when the flexible rod-like regions of laminin are fully extended. Each of the four “arms” of laminin contains sites that allow this biomolecule to bind to other laminin molecules, other proteins (like collagen), and large polysaccharides. Laminin also provides a binding site for proteins called integrins, which are located in the cell membrane.

is-the-laminin-cross-evidence-for-a-creator

Figure: The structure of laminin. Image credit: Wikipedia

Laminin’s architecture and binding sites make this protein ideally suited to interact with other proteins and polysaccharides to form a network called the basal reticulum and to anchor cells to its biochemical scaffolding. The basal reticulum helps hold cells together to form tissues and, in turn, helps cement that tissue to connective tissues.

The cross-like shape of laminin and the role it plays in holding tissues together has prompted the claim that this biomolecule provides scientific support for passages such as Colossians 1:15–17 and shows how the God of the Bible must have made humans and continues to sustain them.

I would caution Christians against using this “argument.” I see a number of problems with it. (And so do many skeptics.)

First, the cross shape is a simple structure found throughout nature. So, it’s probably not a good idea to attach too much significance to laminin’s shape. The t configuration makes laminin ideally suited to connect proteins to each other and cells to the basal reticulum. This is undoubtedly the reason for its structure.

Secondly, the cross shape of laminin is an idealized illustration of the molecule. Portraying complex biomolecules in simplified ways is a common practice among biochemists. Depicting laminin in this extended form helps scientists visualize and catalog the binding sites along its four arms. This configuration should not be interpreted to represent its actual shape in biological systems. In the basal reticulum, laminin adopts all sorts of shapes that bear no resemblance to a cross. In fact, it’s much more common to observe laminin in a swastika configuration than in a cross-like one. Even electron micrographs of isolated laminin molecules that appear cross-shaped may be misleading. Their shape is likely an artifact of sample preparation. I have seen other electron micrographs that show laminin adopting a variety of twisted shapes that, again, bear no resemblance to a cross.

Finally, laminin is not the only molecule “holding things together.” A number of other proteins and polysaccharides are also indispensable components of the basal reticulum. None of these molecules is cross-shaped.

As I argue in my book, The Cell’s Design, the structure and operation of biochemical systems provide some of the most potent support for a Creator’s role in fabricating living systems. Instead of pointing to superficial features of biomolecules such as the “cross-shaped” architecture of laminin, there are many more substantive ways to use biochemistry to argue for the necessity of a Creator and for the value he places on human life. As a case in point, the salient characteristics of biochemical systems identically match those features we would recognize immediately as evidence for the work of a human design engineer. The close similarity between biochemical systems and the devices produced by human designers logically compels this conclusion: life’s most fundamental processes and structures stem from the work of an intelligent, intentional Agent.

When Christians invest the effort to construct a careful case for the Creator, skeptics and seekers find it difficult to deny the powerful evidence from biochemistry and other areas of science for God’s existence.

Resources:

Endnotes

  1. This article was originally published in the April 1, 2009, edition of New Reasons to Believe.
Reprinted with permission by the author
Original article at:
https://www.reasons.org/explore/blogs/the-cells-design/read/the-cells-design/2018/01/31/is-the-laminin-cross-evidence-for-a-creator

Fatty Acids Are Beautiful

fattyacidsarebeautiful

BY FAZALE RANA – NOVEMBER 22, 2017

Who says that fictions onely and false hair
Become a verse? Is there in truth no beauty?
Is all good structure in a winding stair?
May no lines passe, except they do their dutie
Not to a true, but painted chair?

George Herbert, “Jordan (I)”

I doubt the typical person would ever think fatty acids are a thing of beauty. In fact, most people try to do everything they can to avoid them—at least in their diets. But, as a biochemist who specializes in lipids (a class of biomolecules that includes fatty acids) and cell membranes, I am fascinated by these molecules—and by the biochemical and cellular structures they form.

I know, I know—I’m a science geek. But for me, the chemical structures and the physicochemical properties of lipids are as beautiful as an evening sunset. As an expert, I thought I knew most of what there is to know about fatty acids, so I was surprised to learn that researchers from Germany recently uncovered an elegant mathematical relationship that explains the structural makeup of fatty acids.From my vantage point, this newly revealed mathematical structure boggles my mind, providing new evidence for a Creator’s role in bringing life into existence.

Fatty Acids

To first approximation, fatty acids are relatively simple compounds, consisting of a carboxylic acid head group and a long-chain hydrocarbon tail.

fatty-acids-are-beautiful-1

Structure of two typical fatty acids
Image credit: Edgar181/Wikimedia Commons

Despite their structural simplicity, a bewildering number of fatty acid species exist. For example, the hydrocarbon chain of fatty acids can vary in length from 1 carbon atom to over 30. One or more double bonds can occur at varying positions along the chain, and the double bonds can be either cis or trans in geometry. The hydrocarbon tails can be branched and can be modified by carbonyl groups and by hydroxyl substituents at varying points along the chain. As the hydrocarbon chains become longer, the number of possible structural variants increases dramatically.

How Many Fatty Acids Exist in Nature?

This question takes on an urgency today because advances in analytical techniques now make it possible for researchers to identify and quantify the vast number of lipid species found in biological systems, birthing the discipline of lipidomics. Investigators are interested in understanding how lipid compositions vary spatially and temporally in biological systems and how these compositions change in response to altered physiological conditions and pathologies.

To process and make sense of the vast amount of data generated in lipidomics studies, biochemists need to have some understanding of the number of lipid species that are theoretically possible. Recently, researchers from Friedrich Schiller University in Germany took on this challenge—at least, in part—by attempting to calculate the number of chemical species that exist for fatty acids varying in size from 1 to 30 atoms.

Fatty Acids and Fibonacci Numbers

To accomplish this objective, the German researchers developed mathematical equations that relate the number of carbon atoms in fatty acids to the number of structural variants (isomers). They discovered that this relationship conforms to the Fibonacci series, with the number of possible fatty acid species increasing by a factor of 1.618—the golden mean—for each carbon atom added to the fatty acid. Though not immediately evident when first examining the wide array of fatty acids found in nature, deeper analysis reveals that a beautiful yet simple mathematical structure underlies the seemingly incomprehensible structural diversity of these biomolecules.

This discovery indicates it is unlikely that the fatty acid compositions found in nature reflect the haphazard outcome of an undirected, historically contingent evolutionary history, as many biochemists are prone to think. Instead, the fatty acids found throughout the biological realm appear to be fundamentally dictated by the tenets of nature. It is provocative to me that the fatty acid diversity produced by the laws of nature is precisely the isomers needed to for life to be possible—a fitness to purpose, if you will.

Understanding this mathematical relationship and knowing the theoretical number of fatty acid species will certainly aid biochemists working in lipidomics. But for me, the real significance of these results lies in the philosophical and theological arenas.

The Mathematical Beauty of Fatty Acids

The golden mean occurs throughout nature, describing the spiral patterns found in snail shells and the flowers and leaves of plants, as examples, highlighting the pervasiveness of mathematical structures and patterns that describe many aspects of the world in which we live.

But there is more. As it turns out, we perceive the golden mean to be a thing of beauty. In fact, architects and artists often make use of the golden mean in their work because of its deeply aesthetic qualities.

Everywhere we look in nature—whether the spiral arms of galaxies, the shell of a snail, or the petals of a flower—we see a grandeur so great that we are often moved to our very core. This grandeur is not confined to the elements of nature we perceive with our senses; it also exists in the underlying mathematical structure of nature, such the widespread occurrence of the Fibonacci sequence and the golden mean. And it is remarkable that this beautiful mathematical structure even extends to the relationship between the number of carbon atoms in a fatty acid and the number of isomers.

As a Christian, nature’s beauty—including the elegance exemplified by the mathematically dictated composition of fatty acids—prompts me to worship the Creator. But this beauty also points to the reality of God’s existence and supports the biblical view of humanity. If God created the universe, then it is reasonable to expect it to be a beautiful universe. Yet, if the universe came into existence through mechanism alone, there is no reason to think it would display beauty. In other words, the beauty in the world around us signifies the Divine.

Furthermore, if the universe originated through uncaused physical mechanisms, there is no reason to think that humans would possess an aesthetic sense. But if human beings are made in God’s image, as Scripture teaches, we should be able to discern and appreciate the universe’s beauty, made by our Creator to reveal his glory and majesty.

Resources to Dig Deeper

Endnotes

  1. Stefan Schuster, Maximilian Fichtner, and Severin Sasso, “Use of Fibonacci Numbers in Lipidomics—Enumerating Various Classes of Fatty Acids,” Scientific Reports 7 (January 2017): 39821, doi:10.1038/srep39821.
Reprinted with permission by the author
Original article at:
https://www.reasons.org/explore/blogs/the-cells-design/read/the-cells-design/2017/11/22/fatty-acids-are-beautiful

Ribosomes: Manufactured by Design, Part 1

ribosomesmanufacturedbydesign1

BY FAZALE RANA – NOVEMBER 1, 2017

Before joining Reasons to Believe in 1999, I spent seven years working in R&D at a Fortune 500 company, which meant that I spent most of my time in a chemistry laboratory alongside my colleagues trying to develop new technologies with the hope that one day our ideas would become a reality, making their way onto store shelves.

From time to time, my work would be interrupted by an urgent call from one of our manufacturing plants. Inevitably, there was some crisis requiring my expertise as a chemist to troubleshoot. Often, I could solve the plant’s problem over the phone, or by analyzing a few samples sent to my lab. But, occasionally, the crisis necessitated a trip to the plant. These trips weren’t much fun. They were high pressure, stressful situations, because the longer the plant was offline, the more money it cost the company.

But, once the crisis abated, we could breathe easier. And that usually afforded us an opportunity to tour the plant.

It was a thrill to see working assembly lines manufacturing our products. These manufacturing operations were engineering marvels to behold, efficiently producing high-quality products at unimaginable speeds.

The Cell as a Factory

Inside each cell, an ensemble of manufacturing operations exists, more remarkable than any assembly line designed by human engineers. Perhaps one of the most astounding is the biochemical process that produces proteins—the workhorse molecules of life. These large complex molecules work collaboratively to carry out every cellular operation and contribute to the formation of all the structures within the cell.

Subcellular particles called ribosomes produce proteins through an assembly-line-like operation, replete with sophisticated quality control checkpoints. (As discussed in The Cell’s Design, the similarity between the assembly-line production of proteins and human manufacturing operations bolsters the Watchmaker argument for God’s existence.)

Ribosomes

About 23 nanometers in diameter, ribosomes play a central role in protein synthesis by catalyzing (assisting) the chemical reactions that form the bonds between the amino acidsubunits of proteins. A human cell may contain up to half a million ribosomes. A typical bacterium possesses about 20,000 of these subcellular structures, comprising one-fourth the total bacterial mass.

Two subunits of different sizes (comprised of proteins and RNA molecules) combine to form a functional ribosome. In organisms like bacteria, the large subunit (LSU) contains 2 ribosomal RNA (rRNA) molecules and about 30 different protein molecules. The small subunit (SSU) consists of a single rRNA molecule and about 20 proteins. In more complex organisms, the LSU is formed by 3 rRNA molecules that combine with around 50 distinct proteins and the SSU consists of a single rRNA molecule and over 30 different proteins. The rRNAs act as scaffolding that organizes the myriad ribosomal proteins. They also catalyze the chain-forming reactions between amino acids.

Ribosomes Make Ribosomes

Before a cell can replicate, ribosomes must manufacture the proteins needed to form more ribosomes—in fact, the cell’s machinery needs to manufacture enough ribosomes to form a full complement of these subcellular complexes. This ensures that both daughter cells have the sufficient number of protein-manufacturing machines to thrive once the cell division process is completed. Because of this constraint, cell replication cannot proceed until a duplicate population of ribosomes is produced.

Is There a Rationale for Ribosome Structure?

Clearly, ribosomes are complex subcellular particles. But, is there any rhyme or reason for their structure? Or are ribosomes the product of a historically contingent evolutionary history?

New work by researchers from Harvard University and Uppsala University in Sweden provides key insight into the compositional make up of ribosomes, and, in doing so, help answer these questions.1

As part of their research efforts, the Harvard and Uppsala University investigators were specifically trying to answer several questions related to the composition of ribosomes, including:

  1. Why are ribosomes made up of so many proteins?
  2. Why are ribosomal proteins nearly the same size?
  3. Why are ribosomal proteins smaller than typical proteins?
  4. Why are ribosomes made up of so few rRNA molecules?
  5. Why are rRNA molecules are so large?
  6. Why do ribosomes employ rRNA as the catalyst to form bonds between amino acids, instead of proteins which are much more efficient as enzymes?

Ribosome Composition Is Optimal for Efficient Production of Ribosomes

Using mathematical modeling, the Harvard and Uppsala University investigators discovered that if ribosomal proteins were larger, or if these biomolecules were variable in size, ribosome production would be slow and inefficient. Building ribosomes with smaller, uniform-size proteins represents the faster way to duplicate the ribosome population, permitting the cell replication to proceed in a timely manner.

These researchers also learned that if the ribosomal proteins were any shorter, inefficient ribosome production also results. This inefficiency stems from biochemical events needed to initiate protein production. If proteins are too short, then the initiation events take longer than the elongation processes that build the protein chains.

The bottom line: The mathematical modeling work by the Harvard and Uppsala University research team indicates that the sizes of ribosomal proteins are optimal to ensure the most rapid and efficient production of ribosomes. The mathematical modeling also determined that the optimal number of ribosomal proteins is between 50 to 80—the number of ribosomal proteins found in nature.

Ribosome Composition Is Optimal to Produce a Varied Population of Ribosomes

The insights of this work have bearing on the recent discovery that within cells a heterogeneous population of ribosomes exists, not a homogeneous one as biochemists have long thought.2 Instead of every ribosome in the cell being identical, capable of producing each and every protein the cell needs, a diverse ensemble of distinct ribosomes exists in the cell. Each type of ribosome manufactures characteristically distinct types of proteins. Typically, ribosomes produce proteins that work in conjunction to carry out related cellular functions. The heterogeneous makeup of ribosomes contributes to the overall efficiency of protein production, and also provides an important means to regulate protein synthesis. It wouldn’t make sense to use an assembly line to make both consumer products, such as antiperspirant sticks, and automobiles. In the same manner, it doesn’t make sense to use the same ribosomes to make the myriad proteins, performing different functions for the cell.

Because ribosomes consist of a large number of small proteins, the cell can efficiently produce heterogeneous populations of ribosomes by assembling a ribosomal core and then including and excluding specific ribosomal proteins to generate a diverse population of ribosomes.3 In other words, the protein composition of ribosomes is optimized to efficiently replicate a diverse population of these subcellular particles.

The Case for Creation

The ingenuity of biochemical systems was one of the features of the cell’s chemistry that most impressed me as a graduate student (and moved me toward the recognition that there was a Creator). And the latest work by researchers on ribosome composition from Harvard and Uppsala Universities provides another illustration of the clever way that biochemical systems are constructed. The composition of these subcellular structures doesn’t appear to be haphazard—a frozen accident of a historically contingent evolutionary process—but instead is undergirded by an elegant molecular rationale, consistent with the work of a mind.

The case for intelligent design gains reinforcement from the optimal composition of ribosomal proteins. Quite often, designs produced by human beings have been optimized, making this property a telltale signature for intelligent design. In fact, optimality is most often associated with superior designs.

As I pointed out in The Cell’s Design, ribosomes are chicken-and-egg systems. Because ribosomes are composed of proteins, proteins are needed to make proteins. As with ingenuity and optimality, this property also evinces for the work of intelligent agency. Building a system that displays this unusual type of interdependency requires, and hence, reflects the work of a mind.

On the other hand, the chicken-and-egg nature of ribosome biosynthesis serves as a potent challenge to evolutionary explanations for the origin of life.

The Challenge to Evolution

Because ribosomes are needed to make the proteins needed to make ribosomes, it becomes difficult to envision how this type of chicken-and-egg system could emerge via evolutionary processes. Protein synthesis would have to function optimally at the onset. If it did not, it would lead to a cycle of auto-destruction for the cell.

Ribosomes couldn’t begin as crudely operating protein-manufacturing machines that gradually increased in efficiency—evolving step-by-step—toward the optimal systems, characteristic of contemporary biochemistry. If error-prone, ribosomes will produce defective proteins—including ribosomal proteins. In turn, defective ribosomal proteins will form ribosomes even more prone to error, setting up the auto-destruct cycle. And in any evolutionary scheme, the first ribosomes would have been error-prone.

The compositional requirement that ribosomal proteins be of the just-right size and uniform in length only exacerbates this chicken-and-egg problem. Even if ribosomes form functional, intact proteins, if these proteins aren’t the correct number, size, or uniformity then ribosomes couldn’t be replicated fast enough to support cellular reproduction.

In short, the latest insights in the protein composition of ribosomes provides compelling reasons to think that life must stem from a Creator’s handiwork.

So does the compositional makeup of ribosomal RNA molecules, which will be the topic of my next blog post.

Resources

Endnotes

  1. Shlomi Reuveni et al., “Ribosomes Are Optimized for Autocatalytic Production,” Nature 547 (July 20, 2017): 293–97, doi:10.1038/nature22998.
  2. Zhen Shi et al., “Heterogeneous Ribosomes Preferentially Translate Distinct Subpools of mRNAs Genome-Wide,” Molecular Cell 67 (July 6, 2017): 71–83, doi:10.1016/j.molcel.2017.05.021.
  3. Jeffrey A. Hussmann et al., “Ribosomal Architecture: Constraints Imposed by the Need for Self-Production,” Current Biology 27 (August 21, 2017): R798–R800, doi:10.1016/j.cub.2017.06.080.
Reprinted with permission by the author
Original article at:
https://www.reasons.org/explore/blogs/the-cells-design/read/the-cells-design/2017/11/01/ribosomes-manufactured-by-design-part-1

DNA Replication Winds Up the Case for Intelligent Design

dnareplicationwindsup
BY FAZALE RANA – AUGUST 8, 2017

One of my classmates and friends in high school was a kid we nicknamed “Radar.” He was a cool kid who had special needs. He was mentally challenged. He was also funny and as good-hearted as they come, never causing any real problems—other than playing hooky from school, for days on end. Radar hated going to school.

When he eventually showed up, he would be sent to the principal’s office to explain his unexcused absences to Mr. Reynolds. And each time, Radar would offer the same excuse: his grandmother died. But Mr. Reynolds didn’t buy it—for obvious reasons. It didn’t require much investigation on the principal’s part to know that Radar was lying.

Skeptics have something in common with my friend Radar. They use the same tired excuse when presented with compelling evidence for design from biochemistry. Inevitably, they dismiss the case for a Creator by pointing out all the “flawed” designs in biochemical systems. But this excuse never sticks. Upon further investigation, claimed instances of bad designs turn out to be elegant, in virtually every instance, as recent work by scientists from UC Davis illustrates.

These researchers accomplished an important scientific milestone by using single molecule techniques to observe the replication of a single molecule of DNA.1 Their unexpected insights have bearing on how we understand this key biochemical operation. The work also has important implications for the case for biochemical design.

For those familiar with DNA’s structure and replication process, you can skip the next two sections. But for those of you who are not, a little background information is necessary to appreciate the research team’s findings and their relevance to the creation-evolution debate.

DNA’s Structure

DNA consists of two molecular chains (called “polynucleotides”) aligned in an antiparallel fashion. (The two strands are arranged parallel to one another with the starting point of one strand of the polynucleotide duplex located next to the ending point of the other strand and vice versa.) The paired molecular chains twist around each other forming the well-known DNA double helix. The cell’s machinery generates the polynucleotide chains using four different nucleotides: adenosineguanosinecytidine, and thymidine, abbreviated as A, G, C, and T, respectively.

A special relationship exists between the nucleotide sequences of the two DNA strands. Biochemists say the DNA sequences of the two strands are complementary. When the DNA strands align, the adenine (A) side chains of one strand always pair with thymine (T) side chains from the other strand. Likewise, the guanine (G) side chains from one DNA strand always pair with cytosine (C) side chains from the other strand. Biochemists refer to these relationships as “base-pairing rules.” Consequently, if biochemists know the sequence of one DNA strand, they can readily determine the sequence of the other strand. Base-pairing plays a critical role in DNA replication.

 

Image 1: DNA’s Structure

DNA Replication

Biochemists refer to DNA replication as a “template-directed, semiconservative process.” By “template-directed,” biochemists mean that the nucleotide sequences of the “parent” DNA molecule function as a template, directing the assembly of the DNA strands of the two “daughter” molecules using the base-pairing rules. By “semiconservative,” biochemists mean that after replication, each daughter DNA molecule contains one newly formed DNA strand and one strand from the parent molecule.

 

Image 2: Semiconservative DNA Replication

Conceptually, template-directed, semiconservative DNA replication entails the separation of the parent DNA double helix into two single strands. By using the base-pairing rules, each strand serves as a template for the cell’s machinery to use when it forms a new DNA strand with a nucleotide sequence complementary to the parent strand. Because each strand of the parent DNA molecule directs the production of a new DNA strand, two daughter molecules result. Each one possesses an original strand from the parent molecule and a newly formed DNA strand produced by a template-directed synthetic process.

DNA replication begins at specific sites along the DNA double helix, called “replication origins.” Typically, prokaryotic cells have only a single origin of replication. More complex eukaryotic cells have multiple origins of replication.

The DNA double helix unwinds locally at the origin of replication to produce what biochemists call a “replication bubble.” During the course of replication, the bubble expands in both directions from the origin. Once the individual strands of the DNA double helix unwind and are exposed within the replication bubble, they are available to direct the production of the daughter strand. The site where the DNA double helix continuously unwinds is called the “replication fork.” Because DNA replication proceeds in both directions away from the origin, there are two replication forks within each bubble.

 

Image 3: DNA Replication Bubble

DNA replication can only proceed in a single direction, from the top of the DNA strand to the bottom. Because the strands that form the DNA double helix align in an antiparallel fashion with the top of one strand juxtaposed with the bottom of the other strand, only one strand at each replication fork has the proper orientation (bottom-to-top) to direct the assembly of a new strand, in the top-to-bottom direction. For this strand—referred to as the “leading strand”—DNA replication proceeds rapidly and continuously in the direction of the advancing replication fork.

DNA replication cannot proceed along the strand with the top-to-bottom orientation until the replication bubble has expanded enough to expose a sizable stretch of DNA. When this happens, DNA replication moves away from the advancing replication fork. DNA replication can only proceed a short distance for the top-to-bottom-oriented strand before the replication process has to stop and wait for more of the parent DNA strand to be exposed. When a sufficient length of the parent DNA template is exposed a second time, DNA replication can proceed again, but only briefly before it has to stop again and wait for more DNA to be exposed. The process of discontinuous DNA replication takes place repeatedly until the entire strand is replicated. Each time DNA replication starts and stops, a small fragment of DNA is produced.

Biochemists refer to these pieces of DNA (that will eventually compose the daughter strand) as “Okazaki fragments”—after the biochemist who discovered them. Biochemists call the strand produced discontinuously the “lagging strand” because DNA replication for this strand lags behind the more rapidly produced leading strand. One additional point: the leading strand at one replication fork is the lagging strand at the other replication fork since the replication forks at the two ends of the replication bubble advance in opposite directions.

An ensemble of proteins is needed to carry out DNA replication. Once the origin recognition complex (which consists of several different proteins) identifies the replication origin, a protein called “helicase” unwinds the DNA double helix to form the replication fork.

 

Image 4: DNA Replication Proteins

Once the replication fork is established and stabilized, DNA replication can begin. Before the newly formed daughter strands can be produced, a small RNA primer must be produced. The protein that synthesizes new DNA by reading the parent DNA template strand—DNA polymerase—can’t start production from scratch. It must be primed. A massive protein complex, called the “primosome,” which consists of over 15 different proteins, produces the RNA primer needed by DNA polymerase.

Once primed, DNA polymerase will continuously produce DNA along the leading strand. However, for the lagging strand, DNA polymerase can only generate DNA in spurts to produce Okazaki fragments. Each time DNA polymerase generates an Okazaki fragment, the primosome complex must produce a new RNA primer.

Once DNA replication is completed, the RNA primers are removed from the continuous DNA of the leading strand and from the Okazaki fragments that make up the lagging strand. A protein called a “3’-5’ exonuclease” removes the RNA primers. A different DNA polymerase fills in the gaps created by the removal of the RNA primers. Finally, a protein called a “ligase” connects all the Okazaki fragments together to form a continuous piece of DNA out of the lagging strand.

Are Leading and Lagging Strand Polymerases Coordinated?

Biochemists had long assumed that the activities of the leading and lagging strand DNA polymerase enzymes were coordinated. If not, then DNA replication of one strand would get too far ahead of the other, increasing the likelihood of mutations.

As it turns out, the research team from UC Davis discovered that the activities of the two polymerases are not coordinated. Instead, the leading and lagging strand DNA polymerase enzymes replicate DNA autonomously. To the researchers’ surprise, they learned that the leading strand DNA polymerase replicated DNA in bursts, suddenly stopping and starting. And when it did replicate DNA, the rate of production varied by a factor of ten. On the other hand, the researchers discovered that the rate of DNA replication on the lagging strand depended on the rate of RNA primer formation.

The researchers point out that if not for single molecule techniques—in which replication is characterized for individual DNA molecules—the autonomous behavior of leading and lagging strand DNA polymerases would not have been detected. Up to this point, biochemists have studied the replication process using a relatively large number of DNA molecules. These samples yield average replication rates for leading and lagging strand replication, giving the sense that replication of both strands is coordinated.

According to the researchers, this discovery is a “real paradigm shift, and undermines a great deal of what’s in the textbooks.”Because the DNA polymerase activity is not coordinated but autonomous, they conclude that the DNA replication process is a flawed design, driven by stochastic (random) events. Also, the lack of coordination between the leading and lagging strands means that leading strand replication can get ahead of the lagging strand, yielding long stretches of vulnerable single-stranded DNA.

Diminished Design or Displaced Design?

Even though this latest insight appears to undermine the elegance of the DNA replication process, other observations made by the UC Davis research team indicate that the evidence for design isn’t diminished, just displaced.

These investigators discovered that the activity of helicase—the enzyme that unwinds the double helix at the replication fork—somehow senses the activity of the DNA polymerase on the leading strand. When the DNA polymerase stalls, the activity of the helicase slows down by a factor of five until the DNA polymerase catches up. The researchers believe that another protein (called the “tau protein”) mediates the interaction between the helicase and DNA polymerase molecules. In other words, the interaction between DNA polymerase and the helicase compensates for the stochastic behavior of the leading strand polymerase, pointing to a well-designed process.

As already noted, the research team also learned that the rate of lagging strand replication depends on primer production. They determined that the rate of primer production exceeds the rate of DNA replication on the leading strand. This fortuitous coincidence ensures that as soon as enough of the bubble opens for lagging strand replication to continue, the primase can immediately lay down the RNA primer, restarting the process. It turns out that the rate of primer production is controlled by the primosome concentration in the cell, with primer production increasing as the number of primosome copies increase. The primosome concentration appears to be fine-tuned. If the concentration of this protein complex is too large, the replication process becomes “gummed up”; if too small, the disparity between leading and lagging strand replication becomes too great, exposing single-stranded DNA. Again, the fine-tuning of primosome concentration highlights the design of this cellular operation.

It is remarkable how two people can see things so differently. For scientists influenced by the evolutionary paradigm, the tendency is to dismiss evidence for design and, instead of seeing elegance, become conditioned to see flaws. Though DNA replication takes place in a haphazard manner, other features of the replication process appear to be engineered to compensate for the stochastic behavior of the DNA polymerases and, in the process, elevate the evidence for design.

And, that’s no lie.

Resources

Endnotes

  1. James E. Graham et al., “Independent and Stochastic Action of DNA Polymerases in the Replisome,” Cell 169 (June 2017): 1201–13, doi:10.1016/j.cell.2017.05.041.
  2. Bec Crew, “DNA Replication Has Been Filmed for the First Time, and It’s Not What We Expected,” ScienceAlert, June 19, 2017, https://sciencealert.com/dna-replication-has-been-filmed-for-the-first-time-and-it-s-stranger-than-we-thought.
Reprinted with permission by the author
Original article at:
https://www.reasons.org/explore/blogs/the-cells-design/read/the-cells-design/2017/08/08/dna-replication-winds-up-the-case-for-intelligent-design

DNA Wired for Design

dnawiredfordesign
BY FAZALE RANA – JUNE 20, 2017

Though this be madness, yet there is method
in’t.

Hamlet (Act II, scene II)

Was Hamlet crazy? Or was he feigning madness so he could investigate the murder of his father without raising suspicion?

In my senior year of high school, Mrs. Hodges assigned our class these questions as the topic for the first essay we wrote for honors English. I made the case that Hamlet was perfectly sane. Indeed, there was method to his madness.

I wound up with a B- on the assignment. Mrs. Hodges wasn’t impressed with my reasoning, writing on my paper in red ink, “You aren’t qualified to comment on Hamlet’s sanity. You are not a psychologist!” When she returned my paper, I muttered, “Of course, I’m not a psychologist. I’m a high school student. You were the one who asked me to speculate on his sanity. And then when I do . . .”

I was reminded of this high school memory a few days ago while contemplating the structure and function of DNA. This biomolecule’s design is “crazy.” Yet every detail of DNA’s structure is crucial for the role it plays as an information storage system in the cell. You might say there is biochemical method to DNA’s madness when it comes to its properties. One of DNA’s “insane” features is its capacity to conduct electrical current through the interior of the double helix.

DNA Wires

Caltech chemist Jacqueline Barton discovered this phenomenon in the early 1990s. Barton and her collaborators attached different chemical groups to the two ends of the DNA double helix. Both compounds possessed redox centers (metal atoms that can give off and take up electrons). When they blasted one of the redox centers with a pulse of light, it ejected an electron that was taken up by the redox center attached to the opposite end of the DNA molecule, causing the compound to emit a flash of light. The researchers concluded that the ejected electron must have travelled through the interior of the double helix from one redox center to the other.

Shortly after this discovery, Barton and her team learned that electrical charges  move through DNA only when the double helix is intact. Electrical current won’t flow through single-stranded DNA, nor will it flow if the DNA double helix is distorted, due to damage or misincorporation of DNA subunits during replication.

These (and other) observations indicate that the conductance of electrical charge through the DNA molecule stems from π-π stacking interactions of the nucleobases in the double helix interior. These interactions produce a molecular orbital that spans the length of the double helix. In effect, the molecular orbital functions like a wire running through DNA’s interior.

DNA Wires and Nanoelectronics

Charge conductance through the DNA double helix occurs more rapidly than it does through “standard” molecular wires made from inorganic materials. These “insane” transport speeds have inspired researchers to explore the possibility of using DNA as molecular scale wiring in nanoelectronic devices. In fact, some researchers think that DNA wires might become an integral feature for the next generation of medical diagnostic equipment.

Does DNA Function as a Wire in the Cell?

While the charge conductance through the DNA double helix is an interesting and potentially useful property, biochemists have long wondered if DNA functions as a nanowire in the cell.

In 2009, Barton and her team discovered the answer to this question. DNA’s capacity to transmit electrical charges along the length of the double helix plays a key role in the DNA repair process, and recently Barton’s collaborators have demonstrated that DNA’s wire property plays an important role in the initiation of DNA replication. Both processes are important for DNA to function as an information storage system. Repairing damage to DNA insures the integrity of the information it houses. And DNA replication makes it possible to pass this information on to the next generation. There is a purpose to every aspect of DNA’s properties—a method to the madness.

Detecting Damage to DNA

Damage to DNA distorts the double helix. In a process called base excision repair, the cell’s machinery recognizes and removes the damaged portion of the DNA molecule, replacing it with the correct DNA subunits.

For some time, biochemists puzzled over how the DNA repair enzymes located the damaged regions. In the bacteria E. coli, two repair enzymes, dubbed EndoIII and MutY, occur at low levels. (E. coli is a model organism often used by biochemists to study cellular processes.) Biochemists estimate that less than 500 copies of EndoIII exist in the cell and around 30 copies of MutY. These are low numbers considering the task at hand. These repair enzymes bear the responsibility of surveying the E. coli genome for damage—a genome that consists of over 4.6 million base pairs (genetic letters).

Barton and her team discovered that the two repair enzymes possess a redox center consisting of an iron-sulfur cluster (4Fe4S) that has no enzymatic activity.1 They speculated and then demonstrated that the 4Fe4S cluster functions just like the compounds they attached to the DNA double helix in their original experiment in the 1990s.

It turns out Barton and her team were right. These repair proteins bind to DNA. Once bound, they send an electron from the 4Fe4S redox center through the interior of the double helix, which establishes a current through the DNA molecule. Once the repair protein loses an electron, it cannot dissociate from the DNA double helix. Other repair proteins bound to the DNA pick up the electrons from the DNA’s interior at their iron-sulfur redox center. When they do, they dissociate from the DNA and resume their migration along the double helix. Eventually, the migrating repair protein will bind to the DNA again, sending an electron through the DNA’s interior.

This process is repeated, over and over again. However, if the DNA becomes damaged and the double helix distorted, then the DNA wire breaks, interrupting the flow of electrons. When this happens, the repair proteins remain attached to the DNA close to the location of the damage—thus, initiating the repair process.

Initiating DNA Replication

Recently, Barton and her team discovered that charge conductance through DNA also plays a critical role in the early stages of DNA replication.DNA replication—the process of generating two “daughter molecules” identical to the “parent” molecule—serves an essential life function.

DNA replication begins at specific sites along the double helix, called replication origins. Typically, prokaryotic cells, such as E. coli, have only a single origin of replication.

The replication machinery locally unwinds the DNA double helix at the origin of replication to produce a replication bubble. Once the individual strands of the DNA double helix unwind and are exposed within the replication bubble, they are available to direct the production of the daughter strand.

Before the newly formed daughter strands can be produced, a small RNA primer must be produced. DNA polymerase—the protein that synthesizes new DNA by reading the parent template strand—can’t start production from scratch. It must be primed. The primosome, a massive protein complex that consists of over 15 different proteins (including the enzyme primase), produces the RNA primer. From there, DNA polymerase takes over and begins synthesizing the daughter DNA strand.

Barton and her team discovered that the handoff between primase and DNA polymerase relies on DNA’s wire property. Both primase and DNA polymerase possess 4Fe4S redox clusters. When primase’s 4Fe4S redox center loses an electron, this protein binds to DNA to produce the RNA primer. When primase’s 4Fe4S redox center picks up an electron, the protein detaches from the DNA to end the production of the RNA primer.

When DNA polymerase binds to the DNA to begin the process of daughter strand synthesis, it sends an electron from its 4Fe4S redox center along the double helix formed by the parent DNA-RNA primer. When the electron reaches the 4Fe4S redox center of primase, it brings the production of the RNA primer to a halt.

DNA Wires and the Case for a Creator

The work by Barton and her colleagues highlights the elegant and sophisticated design of biochemical systems. DNA’s wire property is so remarkable that it serves as inspiration for the design of the next generation of electronic devices—at the nanoscale. The use of biological designs to drive technological advance is one of the most exciting areas in engineering. This area of study—called biomimetics and bioinspiration—presents us with new reasons to believe that life stems from a Creator. It paves the way for a new type of design argument I dub the converse Watchmaker argument: If biological designs are the work of a Creator, then these systems should be so well-designed that they can serve as engineering models and, otherwise, inspire the development of new technologies.

The converse Watchmaker argument complements William Paley’s classical Watchmaker argument for God’s existence. In my book The Cell’s Design, I describe how recent advances in biochemistry revitalize this classical argument. Over the last few decades, one of the most astounding insights from biochemistry is the recognition that many biochemical systems display the same properties as human designs. This similarity can be used to argue that life must come from the work of a Mind.

The Watchmaker Prediction

In conjunction with my presentation of the revitalized Watchmaker argument in The Cell’s Design, I proposed the Watchmaker prediction. I contend that many of the cell’s molecular systems currently go unrecognized as analogs to human designs because the corresponding technology has yet to be developed. That is, the Watchmaker argument may well become stronger in the future, and its conclusion more certain, as human technology advances.

The possibility that advances in human technology will ultimately mirror the molecular technology that already exists as an integral part of biochemical systems leads to the Watchmaker prediction: As human designers develop new technologies, examples of these technologies, which previously went unrecognized, will become evident in the operation of the cell’s molecular systems. In other words, if the Watchmaker analogy truly serves as evidence for the Creator’s existence, then it is reasonable to expect that life’s biochemical machinery anticipates human technological advances.

The Watchmaker Prediction, Satisfied

The discovery that DNA’s wire properties are critical for DNA repair and the initiation of DNA replication fulfills the Watchmaker prediction. Barton and her team recognized the physiological importance of DNA charge conductance a year after The Cell’s Design was published.

Nanoscientists have been working to develop molecular-scale nanowires for the last couple of decades. The discovery of DNA’s wire properties occurred in this context. In other words, as new technology emerged—in this case, nanoelectronics—we have discovered its existence inside the cell.

Considering the wire properties of DNA, it is not madness to think that a Creator exists and played a role in life’s genesis.

Resources

Endnotes

  1. Amie K. Boal et al., “Redox Signaling between DNA Repair Proteins for Efficient Lesion Detection,” Proceedings of the National Academy of Sciences, USA 106 (September 8, 2009): 15237–42, doi:10.1073/pnas.0908059106Pamel A. Sontz et al., “DNA Charge Transport as a First Step in Coordinating the Detection of Lesions by Repair Proteins,” Proceedings of the National Academy of Sciences, USA 109 (February 7, 2012): 1856–61, doi:10.1073/pnas.1120063109; Michael A. Grodick, Natalie B. Muren, and Jacqueline K. Barton, “DNA Charge Transport within the Cell,” Biochemistry 54 (February 3, 2015): 962–73, doi:10.1021/bi501520w.
  2. Elizabeth O’Brien et al., “The [4Fe4S] Cluster of Human DNA Primase Functions as a Redox Switch Using DNA Charge Transport,” Science 355 (February 24, 2017): doi:10.1126/science.aag1789.
Reprinted with permission by the author
Original article at:
https://www.reasons.org/explore/blogs/the-cells-design/read/the-cells-design/2017/06/20/dna-wired-for-design

Hagfish Slime Expands the Case for a Creator

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BY FAZALE RANA – MARCH 8, 2017

The designs found in biological systems never cease to amaze me. Even something as gross and seemingly insignificant as hagfish slime displays remarkable properties, befitting the handiwork of a Creator. In fact, the design of hagfish slime is so ingenious, it is serving as the source of inspiration for researchers from the US Navy in their quest to develop new types of military technology.

What Are Hagfish?

Hagfish are ancient creatures that first appeared on Earth around 520 million years ago, with representative specimens recovered in the Cambrian fossil assemblages. These eel-like creatures are about 20 inches in length with loose fitting skin that varies in color from pink to blue-gray, depending on the species.

The hagfish are jawless but have a mineralized encasement around their skull (cranium). With eyespots instead of true eyes, these creatures have no vision. Hagfish are bottom-dwellers. To explore their environment, they make use of whisker-like structures. As scavengers, hagfish consume dead and dying creatures by burrowing into their bodies and ingesting the remains from the inside out. Remarkably, hagfish absorb nutrients through their skin and gills, in addition to feeding with their mouths. In fact, researchers estimate that close to half their nutrient intake comes through absorption.

Hagfish Slime

When disturbed or attacked by predators, hagfish secrete a slime from about 100 glands that line the flanks of their bodies. (This behavior explains why hagfish are sometimes called slime eels.) Produced by epithelial and gland thread cells, the slime rapidly expands to 10,000 times its original volume. A single hagfish can generate around 5.5 gallons of slime each time it’s disturbed. Once secreted, the slime coats the gills of attacking fish, suffocating the predator. With the predator distracted, the hagfish performs this defensive maneuver that allows it to escape, while scrapping the slime off its body to prevent self-suffocation.

Two different types of proteins comprise hagfish slime. One of the components, mucin, is a large protein found widely throughout nature, serving as the primary component of mucus. Secreted by epithelial cells, mucin interacts with water molecules, restricting their movement, contributing to the slime’s viscosity.1

Additionally, hagfish slime consists of long, thread-like proteins. These protein threads are 12 nanometers in diameter and 15 centimeters long! (That is one big molecule.) These dimensions equate to a rope that is 1 centimeter in diameter and 1.5 kilometers in length. These protein fibers are incredibly strong, equivalent to a string that is 100 times thinner than a strand of human hair, but 10 times stronger than a piece of nylon.

Inside the gland thread cells, these protein fibers are carefully packaged like a skein of yarn, held together by other proteins that serve as a type of molecular glue.2 When the secreted hagfish slime contacts seawater, the glue proteins dissolve, leading to an explosive unraveling of the protein skeins, without any of the fibers becoming tangled. The protein threads contribute to the slime’s viscoelastic properties and provide the mechanism for the rapid swelling of the slime.

Hagfish Slime Inspires Military Technologies

The unusual and ingenious properties of the slime and the slime’s thread proteins have inspired researchers from the US Navy to explore their use in military technology. For example, the remarkable durability of the protein fibers (reminiscent of Kevlar) suggests an application for them in bulletproof vests. The properties of the hagfish slime could also be used as a flame retardant and a shark repellent for Navy divers.

Other commercial labs are exploring applications that include food packaging, bungee cords, and bandages. In fact, some have gone as far as to dub the thread proteins as the ultimate biodegradable biofiber.

Biomimetics and the Case for a Creator

In recent years, engineers have routinely and systematically benefited by insights from biology to address engineering problems and to inspire new technologies by either directly copying (or mimicking) designs from biology, or using insights from biological designs to guide the engineering enterprise.

From my perspective, the use of biological designs to guide engineering efforts fits awkwardly within the evolutionary paradigm. Why? Because evolutionary biologists view biological systems as the products of an unguided, historically contingent process that co-opts preexisting systems to cobble together new ones. Evolutionary mechanisms can optimize these systems, but they are still kludges.

Given the unguided nature of evolutionary mechanisms, does it make sense for engineers to rely on biological systems to solve problems and inspire new technologies? Conversely, biomimetics and bioinspiration find a natural home in a creation model approach to biology. Using designs in nature to inspire engineering makes sense only if these designs arose from an intelligent Mind—even if they are as disgusting as the slime secreted by a bottom-dwelling scavenger.

Resources

Endnotes

  1. Lukas Böni et al., “Hagfish Slime and Mucin Flow Properties and Their Implications for Defense,” Scientific Reports 6 (July 2016): id. 30371, doi:10.1038/srep30371.
  2. Timothy Winegard et al., “Coiling and Maturation of a High-Performance Fibre in Hagfish Slime Gland Thread Cells,” Nature Communications 5 (April 2014): id. 3534, doi:10.1038/ncomms4534; Mark A. Bernards Jr. et al., “Spontaneous Unraveling of Hagfish Slime Thread Skeins Is Mediated by a Seawater-Soluble Protein Adhesive,” Journal of Experimental Biology 217 (April 2014): 1263–68, doi:10.1242/jeb.096909.
Reprinted with permission by the author
Original article at:
https://www.reasons.org/explore/blogs/the-cells-design/read/the-cells-design/2017/03/08/hagfish-slime-expands-the-case-for-a-creator

The Remarkable Scientific Accuracy of Psalm 139

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BY FAZALE RANA – MARCH 1, 2017

For you created my inmost being; you knit me together in my mother’s womb. I praise you because I am fearfully and wonderfully made; your works are wonderful, I know that full well.

– Psalm 139:13–14

Psalm 139 has been on my mind quite a bit lately. Maybe it’s because I have recently written a couple of articles about the incredible design of human pregnancy—design that highlights just how fearfully and wonderfully human beings are made.

Posting these articles to my Facebook page prompted one of my Facebook friends, Eric, to ask a thought-provoking question:

“Psalm 139:13 says God ‘knit’ us in our mother’s womb. This sounds a lot to me like DNA replication. Is this reading science into the text?”

Given the importance of DNA replication to embryological development and the specific features of the replication process, I understand why Eric would want to make that comparison. While I think that there are passages in Scripture that anticipate (even predict) scientific discoveries, I don’t see Psalm 139 referring to DNA replication. (By the way, I appreciate Eric’s caution about reading science into the text.)

Having said that, I do think that the description of God knitting each one of us together in our mother’s womb is an apt analogy for the process of embryological development at the cellular level, because both knitting and development are predicated on forethought and rely on a special type of information—qualities that reflect the activity of an Intelligent Agent.

An Overview of Embryo Growth and Development

Embryological development begins the moment the egg cell (oocyte) becomes fertilized by a sperm cell, yielding a zygote. In turn, the zygote undergoes several rounds of cell division (referred to as cleavage) to produce a berry-like structure, called a morula. All of this happens by the third or fourth day of pregnancy.

Over the next couple of days, the morula undergoes changes that characterize the process of embryogenesis. In addition to undergoing growth and division, cells in the morula begin to migrate relative to one another to form a structure with a hollow sphere called a blastula. Within the sphere is a clump of cells called the inner cell mass.

scientific-accuracy-of-psalm-139-1The next stage in embryogenesis sees the inner cell mass transform into a stack of three cellular layers (called germ layers) through cell growth, division, and migration. At this stage, the embryo is referred to as the gastrula.

The specific cell layers of the gastrula are labeled: (1) the ectoderm, (2) the mesoderm, and (3) the endoderm. Each of these cell layers is fated to develop into different organ systems in the body. The ectoderm forms the nervous system and the epidermis of the skin. The mesoderm forms muscles, the skeletal system, blood and blood vessels, and the dermis of the skin. The endoderm forms the linings of the digestive and respiratory systems, and organs that comprise the digestive system, such as the liver and pancreas.

After gastrulation, the next stage involves organ formation. Organogenesis begins in each of the individual cell layers and involves the careful orchestration of several processes, including cell growth, cell division, cell-to-cell communication, cell migration, differentiation of cells into specialized types, secretion of extracellular materials, and even cell death (which is necessary to sculpt the tissues and organs).

These cellular processes are directed by the complex interplay between gene networks within the cells (with genes turning on and off) and chemical gradients produced from materials secreted by the cells. Some scientists think that bioelectric fields generated by the cells of the developing embryo also direct embryogenesis.1 The patterns formed by the chemical gradients and bioelectric fields direct the movements, differentiation, and behavior of the embryonic cells. Still, the scientific community is unclear what ultimately determines the chemical gradient and bioelectric field patterns. To put it another way, while scientists are beginning to understand the role that chemical gradients and bioelectric fields play in development, they have no idea where the instructions ultimately come from that direct individual cells in the developing embryo to contribute to and, in turn, respond to the chemical gradients and bioelectric fields that guide embryonic development.

Perhaps the problem has to do with the fact that the scientific community views embryogenesis from a strictly materialistic/naturalistic framework. But what if embryo development were to be examined from a creation model vantage point?

Embryological Development and the Case for Intelligent Design

Remarkably, the instructions for embryogenesis appear to be instantiated in the cells that make up the developing embryo. From a creation model perspective, these instructions must come from a Mind, because instructions are a form of information (specifically, algorithmic information) and common experience teaches that algorithms emanate from a Mind. Toward that end, origin-of-life researchers Paul Davies and Sara Walker recently acknowledged that currently there is no evolutionary explanation for algorithmic information instantiated in living matter.2

Another reason to think that embryological development stems from a Creator’s involvement relates to the foresight required to formulate the instructions so that they lead to the desired outcome for embryogenesis. Evolutionary processes do not have foresight. Foresight also reflects the work of a Mind. If these instructions are flawed for even a single cell during the early stages of development, the consequences would be disastrous, with the offspring turning into a “developmental monster,” compromised in its capacity to survive and reproduce. To put it differently, it is hard to envision how evolutionary processes could generate the algorithmic information needed for embryogenesis through trial and error, without the benefit of foresight.

To help make this point clear, consider the analogy between embryogenesis and the routine performed by cheerleaders during a competition.3 Throughout the performance, each cheerleader has a specific set of movements and actions she will perform. Before the performance, her coach instructs her in exactly what to do, when to do it, and where to do it on the mat. Her individual movements and actions are different from every other team member, but when performed in conjunction with her teammates (who have their own set of instructions), the outcome can be dazzling. All this is possible, because the coach choreographed the routine ahead of the performance, with an eye toward how the routine would unfold at different stages of the performance. That is, the routine was intelligently designed with the benefit of the coach’s foresight and that design was implemented through the instructions given to each girl. If not for the coach’s foresight and instructions, chaos would ensue during the performance as each girl did whatever seemed right to her at the time.

In like manner, during embryogenesis, each cell harbors a set of instructions that tell it: (1) what chemicals and how much of these materials to secrete to establish the gradients needed to guide development, (2) when to reproduce, (3) when and where to migrate, (4) when to differentiate, (5) when and what materials to secrete to form the extracellular matrix, and (6) when to die. In a sense, the cells are like cheerleaders. And the process of embryological development is akin to the choreography of a cheer routine. The only difference: the choreography of embryological development is much more complex, elaborate, and sophisticated.

As with cheerleading, someone must give the cells instructions ahead of time with the end goal of embryological development in view. And I see that “someone” as the Creator.

Knit Together in the Womb

I also find “knitting” an apt metaphor for embryological development. My mother is an avid knitter. And whenever I watch her knit, I can’t help but recognize the similarities to a cheer routine. Knitting consists of a choreography, of sorts. Someone who knits a sweater has a final product in mind before she even picks up needles and chooses the yarn. Making use of a set of instructions—algorithmic information—that tells her which yarn to use and which knitting strokes to employ, she performs a series of actions that will eventually lead to the final product, though what that product is may not be evident at the instant those actions are performed, at least to the uninitiated.

In this context, it is intriguing that David, the author of Psalm 139, would describe embryological development as a knitting process. David writes,

“Your eyes saw my unformed body; all the days ordained for me were written in your book before one of them came to be.”

– Psalm 139:16

In light of what we have learned about embryological development, I find the scientific prescience of Psalm 139 remarkable.

Resources

Endnotes

  1. Michael Levin, “Bioelectric Mechanisms in Regeneration: Unique Aspects and Future Perspectives,” Seminars in Cell and Developmental Biology 20 (July 2009): 543–56, doi:10.1016/j.semcdb.2009.04.013.
  2. Sara Imari Walker and Paul C. W. Davies, “The Algorithmic Origins of Life,” Journal of the Royal Society Interface 10 (February 2013): doi:10.1098/rsif.2012.0869.
  3. One of my daughters was a competitive cheerleader. Before she started, if you would have asked me, “Are cheerleaders athletes?” I would have laughed. But after spending several years around cheerleaders, I am truly impressed with their athleticism. In short, cheerleaders are amazing athletes.
Reprinted with permission by the author
Original article at:
https://www.reasons.org/explore/blogs/the-cells-design/read/the-cells-design/2017/03/01/the-remarkable-scientific-accuracy-of-psalm-139

Q&A: Why Would a Limitless Creator Face Trade-Offs in Biochemical Designs?

qawhywouldalimitlesscreator

BY FAZALE RANA – FEBRUARY 1, 2017

“Biologists must constantly keep in mind that what they see was not designed, but rather evolved.”
—Francis Crick, What Mad Pursuit
In my experience, no one denies the complexity and sophistication of biochemical systems, regardless of their philosophical or religious views. To put it another way, there is no debate. Biochemical systems have the indisputable appearance of design. The question at the center of the creation/evolution controversy relates to the source of the design. Is it the handiwork of a Creator? Or, is it the product of unguided, evolutionary processes? Is the design authentic? Or is it only apparent?

As a creationist, I regard the elegant designs of biochemical systems as evidence for a Creator’s role in bringing life into existence. Yet, many in the scientific community would disagree, maintaining that the design emerges through evolutionary processes. In support of this position, these detractors point to so-called “bad” biochemical designs and argue that if an all-powerful, all-knowing, all-good Creator produced biochemical systems, these systems should display perfection. On the other hand, less-than-optimal designs are precisely what one would expect if life resulted from an evolutionary history.

Are Bad Designs a Challenge to the Design Argument?

In my book The Cell’s Design, I offer a chapter-length rejoinder to this challenge, pointing out the following:

  • Often when life scientists interpret biochemical systems as poorly designed, their view is based on an incomplete understanding of the structure and function of these systems. Inevitably, as researchers develop new insight, these systems are revealed to be additional examples of the elegant designs, characteristic of biochemistry.

Junk DNA serves as the quintessential illustration of this point.

  • In some cases, biochemical systems labeled as flawed designs are suboptimal in reality. Their suboptimal nature is necessary for the overall system to optimally perform. Routinely, engineers intentionally suboptimize facets of the systems they design to achieve overall optimality. This practice is necessary for complex systems built to achieve multiple objectives. Inevitably, some of these objectives conflict with others. In other words, these systems face trade-offs. To manage the trade-offs, engineers must carefully suboptimize the performances of the systems’ components, again, so that the systems will result in overall optimal performances.

Some recently discovered examples of biochemical trade-offs include:

A Rejoinder

After recently posting the article I wrote on the trade-offs associated with glucose breakdown, my Facebook friend Riaz, a skeptic, offered this come back:

“There is no need for trade-offs if one has unlimited resources . . . not to mention being able to change [the] law[s] of physics and design/re-design the universe from scratch . . .”

Trade-Offs Are Inevitable

This is a reasonable question. Why would the Creator, described in the Bible, ever deal with trade-offs? But what if the God of the Bible did choose to produce a universe with fixed natural laws? If he did, trade-offs inevitably result. And, I contend, the elegance in which these trade-offs are managed in biochemical systems are nothing less than genius, befitting the God of the Bible.

A Follow-Up Question

What about Riaz’s second question? Why create a universe with unvarying natural laws, if that means suboptimal designs would necessarily result? If the Creator is infinite in power and extent, if the Creator is all-knowing and all-good, why would He confine himself so that He is forced to suboptimize even a single facet of His creation because of trade-offs?

Interesting questions, to be sure. From my perspective, there are at least three reasons why God created the universe with unvarying natural laws.

Constant Laws of Nature Reflect God’s Nature

A universe with constant natural laws reflects God’s character and nature as revealed in the Old and New Testaments. Scripture teaches that:

It is reasonable to think that the universe made by a God who does not waver would be governed by unvarying natural laws.

Along those lines, Psalm 50:6 tells us that the “heavens declare God’s righteousness.” From my vantage point, the righteousness revealed in the heavens would be most clearly manifested through the conformity of the heavenly bodies (and all of nature, for that matter) to constant laws.

An interesting interplay of these ideas is found in Jeremiah 33:25. Here, the Lord compares the certainty of the covenant He established with His people to the “established laws of heaven and earth.”1 To put it another way, if we ever wonder if God will keep his promises, all we need to do is look to the constancy of the laws of nature.

Constant Laws of Nature Are Necessary for Moral Accountability

This assertion may not seem obvious at first glance. But, careful consideration leads to the conclusion that apart from a universe with fixed laws governing nature, it is impossible to have moral laws. In his classic work Faith and Reason, the late philosopher Ron Nash writes:

“The existence of a lawlike and orderly creation is a necessary condition for a number of divine objectives. . . . it is also reasonable to believe that God placed these free moral agents in a universe exhibiting order. One can hardly act intentionally and responsibly in an unpredictable environment.”2

Ron Nash goes on to say:

“If the world were totally unpredictable, if we could never know from one moment to the next, what to expect from nature, both science and meaningful moral conduct would be impossible. While we often take the natural order for granted, this order and the predictability that accompanies it function as a necessary condition for free human action. . . . One reason people can be held accountable when they pull the trigger of a loaded gun is the predictability of what will follow such an action.”3

Constant Laws of Nature Permit Discoverability

Unchanging natural laws render the universe (and phenomena within its confines) intelligible. If the laws of nature changed from day-to-day—or at the Creator’s whim—it would be impossible to know anything about the world around us with any real confidence. In effect, science would be impossible. The orderliness of the universe leads to predictability, the most important condition for a rational investigation of the world.

Because the universe is intelligible, it is possible for human beings to take advantage of God’s provision for us, made available within the creation. As we study and develop an understanding of the laws of physics and chemistry, the composition of matter, and the nature of living systems, we can deploy that knowledge to benefit humanity—in fact, all life on Earth—through technology, agriculture, medicine, and conservation efforts. To put it in theological terms, the intelligibility of the universe allows us to unleash God’s providence for humanity as we come to understand the world around us.

Ultimately, I believe that God has designed the universe for discoverability because He wants us to see, understand, and appreciate His handiwork as a Creator, so through His creation we can know Him. Scripture teaches that we can glimpse God’s glory (Psalm 19:1), majesty (Psalm 8:1), and righteousness (Psalm 50:6) from nature. From the Old Testament, we learn that God’s eternal nature (Psalm 90:2) can be gleaned from the world around us. We can see God’s love, faithfulness, righteousness, and justice (Psalm 36:5–6) in creation. This powerful revelation of God’s character is only possible because the laws of nature are constant.

Scripture (Romans 1:20Job 12:7–9) also teaches that we can see evidence for God’s fingerprints as well—evidence for His existence. And toward that end, I maintain that we see God’s handiwork in the elegant way trade-offs are handled in biochemical systems.

Resources

Reactive Oxygen Species: Harbingers of Evolution or Signals of Design?

reactiveoxygenspeciesharbingers

BY FAZALE RANA – DECEMBER 14, 2016

“Few concepts have been embraced by popular science as enthusiastically as the idea that reactive oxygen species (ROS) are harmful and that their levels should be controlled by including antioxidants in the diet or as supplements.”1

–Ulrich Theopold

Antioxidants are the latest diet fad. Many people do whatever they can to include foods high in antioxidants in their diets. Some people even go a step further by taking antioxidant supplements. All these actions are meant to combat the harmful effects of reactive oxygen species (ROS). Produced in the mitochondria, these highly reactive chemical derivatives of molecular oxygen will destroy cellular components if left unchecked.

Yet things aren’t always what they seem. An increasing number of studies indicate that taking dietary supplements of antioxidants has questionable health benefits.2 In fact, taking certain antioxidant supplements may be harmful. For example, studies indicate that people who supplement their diets with vitamin E and beta-carotene have higher mortality rates compared to people who don’t take antioxidant supplements at all. Other studies demonstrate that instead of slowing cancer’s spread, antioxidants, in fact, accelerate the progression of certain cancers. Antioxidant consumption also impacts development, harming certain types of stem cells.

When it comes to antioxidants and ROS, the scientific community has made another surprising about-face. Biochemists no longer view ROS as harmful compounds, wreaking havoc on the cell’s components. Instead, they have learned that ROS play a key role in cell-signaling processes. As it turns out, consumption of excessive antioxidants interferes with ROS-based signaling pathways. And this interference explains why consuming inordinate levels of antioxidants aren’t part of a healthy lifestyle.

The surprising implications of this new insight regarding antioxidants and ROS extend beyond dietary considerations. This new understanding has bearing on the creation vs. evolution debate by providing a response to a common objection skeptics level against intelligent design arguments.

ROS Generation and the Case for Evolution

ROS are primarily produced in the mitochondria by the electron transport chain (ETC). The ETC harvests energy needed to carry out the various biochemical operations that take place within the cell. For the most part, the ETC is comprised of a series of protein complexes, conceptually organized into a linear array. The first complex of the ETC receives chemically energetic electrons (ultimately, derived from the breakdown of biochemical fuels) and passes them along to the next complex in the ETC. Eventually, these electrons are handed off from complex to complex, until they reach the terminal part of the ETC. When shuttled from one complex to the other, the electrons give up some of their energy. This released energy is captured, and ultimately used to produce compounds such as ATP, which serve as energy currency inside the cell.

reactive-oxygen-species-1
Image: Illustration of electron transport chain with oxidative phosphorylation.

One of the final steps carried out by the ETC is the conversion of molecular oxygen into water, with oxygen receiving the de-energized electrons. If the energy status of the cell is high, the movement of electrons through the ETC slows down, and, under some circumstances, becomes backed up. When this jam occurs, the electrons prematurely react with oxygen because they must go somewhere. (This usually happens between complex I and complex III). When this premature termination takes place, ROS (which include the superoxide ion, the hydroxyl free radical, and hydrogen peroxide) form instead of water.

At face value, it appears as if ROS form as an unintended side reaction. Traditionally, biochemists regard ROS as deadly compounds that oxidize membrane components, DNA, and proteins, causing untold damage to the cell.

For many skeptics, the apparently random, unwanted generation of ROS which terrorize the cell undermines the case for intelligent design and serves as evidence for an evolutionary origin of biochemical systems. Why? Because the seemingly unintended production of chemically destructive ROS has all the markings of a flawed system—the type of system unguided evolutionary processes would produce, not the type of design befitting a Creator.

The Cellular Roles of ROS

Yet in recent years, biochemists have come to see ROS differently. Instead of the product of an unwanted side reaction, biochemists have come to discover that these compounds serve as second messengers, communicating the cell’s energy status to key metabolic processes, including those that regulate stem cell development.3 These mechanisms allow the cell to coordinate various metabolic processes for the available bioenergetics sources.

Because hydrogen peroxide has the chemical stability and capacity to dissolve through membranes, biochemists believe that it functions as the primary second messenger. Still, the other ROS do play a role in cell signaling.

ROS can serve as second messengers because they preferentially oxidize certain amino acids in proteins, with cysteine residues often targeted. The selective oxidation of amino acid residues modifies the activity of the protein targets. Targeted proteins include transcription factors (which control gene expression), and kinases and phosphatases (which regulate different stages of the cell cycle). These protein targets explain why ROS play a critical role in stem cell renewal, stem cell proliferation, and maturation.

Oxidative Damage by ROS Is a Trade-Off

ROS are ideal second messengers for communicating and coordinating the cell’s metabolic pathways with respect to the cell’s energy status, because their production is closely linked to the ETC. When the energy status of the cell is high, ROS production increases. And when the cell’s energy status dips, ROS production tails off. In my view, there is an exquisite molecular logic that undergirds the use of ROS as second messengers for communicating the cell’s energy balance.

Of course, the drawback to using ROS as second messengers is the oxidative damage these materials cause. But instead of viewing the damaging effects of these compounds as a flawed design, I maintain that it is better to think of it as a trade-off.

Towards that end, it is important to note that the cell has an extensive and elaborate system to buffer against the harmful effects of ROS. For example, superoxide dismutase converts superoxide into hydrogen peroxide. Two other enzymes, catalase and peroxiredoxin, transform hydrogen peroxide into water. In fact, one of the targets of ROS are transcription factors that trigger the production of proteins that are part of the cell’s antioxidant defenses and proteins that take part in pathways that clear damaged proteins from the cell. This ingenious design ensures that once ROS form and play a role as second messengers, the damaged proteins are quickly destroyed and any destruction they cause is mitigated.

It is truly remarkable how dramatically the scientific community’s views on ROS (and antioxidants) have changed in recent years. Instead of being the unwanted byproducts of metabolism that plagued the cell, ROS serve as a biochemical fuel gage, triggering processes such as quiescence and even autophagy (programmed cell death) when the energy balance is too low and the cell is experiencing starvation and cell differentiation (which impacts stem cell biology) when energy stores are sufficiently full.

Often, skeptics point to so-called bad designs as evidence for an evolutionary history for life. But, the changed perspective of ROS serves as a cautionary tale. Many times, what is perceived as a bad design turns out to be anything but as we learn more about the system, and these discoveries undermine the best arguments for evolution while adding to the mounting case for intelligent design.

Resources

The Cell’s Design by Fazale Rana (book)
30% Inefficiency by Design” by Fazale Rana (article)
The Human Appendix: What Is It Good For?” by Fazale Rana (article)
New Research Highlights Elegant Design in the Inverted Retina” by Fazale Rana (article)
Wisdom Teeth Reflect the Creator’s Foresight” by Fazale Rana (article)
Is the Whale Pelvis a Vestige of Evolution?” by Fazale Rana (article)

Endnotes

  1. Ulrich Theopold, “Developmental Biology: A Bad Boy Comes Good,” Nature 461 (September 2009): 486–87, doi:10.1038/461486a.
  2. Center for the Advancement of Health, “Antioxidant Users Don’t Live Longer, Analysis of Studies Concludes,” Science News (blog), ScienceDaily, April 16, 2008, https://www.sciencedaily.com/releases/2008/04/080415194233.htm; University of Gothenburg, “Antioxidants Cause Malignant Melanoma to Metastasize Faster,” Science News (blog), ScienceDaily, October 8, 2015, https://www.sciencedaily.com/releases/2015/10/151008131112.htm; Ed Yong, “Antioxidants Speed Up Lung Cancer,” Daily News (blog), The Scientist, January 29, 2014, https://www.the-scientist.com/?articles.view/articleNo/39022/title/Antioxidants-Speed-Up-Lung-Cancer/; University of Helsinki, “Large Doses of Antioxidants May Be Harmful to Neuronal Stem Cells,” Science News (blog), ScienceDaily, June 11, 2015, https://www.sciencedaily.com/releases/2015/06/150611091340.htm.
  3. Kira Holmström and Toren Finkel, “Cellular Mechanisms and Physiological Consequences of Redox-Dependent Signalling,” Nature Reviews Molecular Cell Biology 15 (June 2014): 411–21, doi:10.1038/nrm3801; Carolina Bigarella, Raymond Liang, and Saghi Ghaffari, “Stem Cells and the Impact of ROS Signaling,” Development 141 (November 2014): 4206–18, doi:10.1242/dev.107086.
Reprinted with permission by the author
Original article at:
https://www.reasons.org/explore/blogs/the-cells-design/read/the-cells-design/2016/12/14/reactive-oxygen-species-harbingers-of-evolution-or-signals-of-design

Pseudoenzymes Illustrate Science’s Philosophical Commitments

pseudoenzzymesillustratesciences.png

BY FAZALE RANA – DECEMBER 7, 2016

A few months ago, I had a serious accident while shooting a compound bow in my backyard. The arrow jammed in the guide, and in my attempt to free the arrow, I caused the bow string to derail. When that happened, the string struck my left eye with such force that it fractured my orbit in five places and damaged my retina. I am now legally blind in my left eye. Thankfully, I still have some peripheral vision, but I lost all the central vision in my injured eye. (To mothers everywhere: Yes, I wasn’t careful and I shot my eye out. I should have listened.)

Because of my injury, there is a blacked-out area in the center part of my field of vision which prevents me from focusing with my left eye. Sometimes, if something is on my left side, I can’t see it—even if it is in plain view.

Science’s Blind Spot

Over the years I have come to appreciate that, very often, the creation/intelligent design vs. evolution controversy has less to do with the evidence on hand, and more with how each side sees the evidence. As a case in point, when examining the features of biochemical systems, most creationists and intelligent design proponents readily see evidence of a Creator’s handiwork. Yet adherents to the evolutionary paradigm don’t see evidence for design at all. Instead, they see flawed designs. Why? Because they view biochemical systems as the outworking of an unguided evolutionary history. According to this view, evolution’s mechanisms have cobbled together biochemical systems by co-opting and repurposing existing systems to generate novel biochemical functions. As such, evolution produces kludge-job designs. Not the elegant, sophisticated systems expected if life stems from a Creator’s handiwork.

In part, the differing perspectives are shaped by philosophical commitments and the expectations that flow from them. To expound upon this point: the philosophical framework for contemporary science is methodological naturalism. Accordingly, scientific explanations for the universe and phenomena within the universe (such as the characteristics of biochemical systems) must have a mechanistic accounting—an explanation exclusively rooted in natural processes. Any explanation that appeals to the work of supernatural agency violates the tenets of methodological naturalism and is not even entertained as a possibility.

The consequences of methodological naturalism are far ranging for the creation/intelligent design vs. evolution controversy. The constraints of methodological naturalism exclude a priori any model that appeals to intelligent agency to explain, say, the design of biochemical systems. So although biochemical systems bear the appearance of design, the scientific community must explain the design as a product of evolutionary mechanisms. Why? Because they have no other option. If biochemical systems didn’t evolve, then they must have been created. But, the tenets of methodological naturalism forbid this explanation. Hence, biochemical systems must have evolved—by default.

If biochemical systems arise via evolutionary mechanisms, then they must be cobbled together. They must be poorly designed. Consequently, adherents of the evolutionary paradigm are conditioned to see biochemical systems as poorly designed—even if they aren’t—because of their commitment to methodological naturalism. Many can’t see the design that is in plain view for creationists and intelligent design adherents.

The recent discovery of pseudoenzymes helps illustrate this point.

Pseudoenzymes: Evidence for Evolution or Intelligent Design?

The existence of pseudoenzymes came to light about a decade ago when the human genome sequence was made available for researchers to study. It turns out that almost every enzyme family encoded by the human genome includes seemingly nonfunctioning members. (Enzymes are proteins that catalyze—or facilitate—chemical reactions in the cell.) Biochemists have dubbed these nonfunctioning enzymes pseudoenzymes. These proteins bear structural resemblances to other members of their enzyme families, yet they are unable to catalyze chemical reactions.

Because researchers have already detected pseudoenzymes within every known enzyme family, they expect that many more pseudoenzymes await discovery. In fact, analysis of thousands of genomes has identified pseudoenzymes throughout the biological realm. To put it another way: Pseudoenzymes seem to be pervasive in biochemical systems.

Evolutionary biologists view pseudoenzymes as a byproduct of life’s evolutionary history. Presumably, these noncatalytic enzymes arose when genes encoding their functional counterpart became duplicated. After this event, the duplicated genes experienced mutations that disabled the catalytic function of their protein products, generating pseudoenzymes.

For adherents of the evolutionary paradigm, the widespread occurrence of pseudoenzymes serves as a prima facie (based on first impression) challenge to intelligent design, and a compelling reason to think that biochemical systems are the product of an evolutionary history. In this framework, pseudoenzymes are vestiges of life’s evolutionary past; nonfunctional biochemical scars that impede cellular functions.

On the other hand, as a creationist and intelligent design proponent, I resist this conclusion. Why? Because I have a different set of presuppositions than most in the scientific community. I believe that life arose through a Creator’s direct intervention and that science has the tool kit to detect evidence of intelligent agency at work. Because of my precommitments, I would posit yet-to-be-discovered functions for pseudoenzymes and a rationale for why these enzymes bear structural similarity to catalytic counterparts within their enzyme family.

And this is exactly what biochemists have discovered—pseudoenzymes are, indeed, functional, and there are good reasons why these biomolecules resemble their catalytic analogs.

The Role and Rationale for Pseudoenzymes

In a recent primer written for the open access journal BMC Biology, two biochemists surveyed recent work on pseudoenzymes, concluding that this newly recognized class of biomolecules plays a key role in cellular signaling pathways.1

The authors reflect on the role the evolutionary paradigm played in delaying this insight. They state:

“Because of the prejudice that focused attention on the catalytic functions of enzymes in signalling pathways, for a long time pseudoenzymes were considered to be dead—and therefore evolutionary remnants or bystanders in cell signalling networks. Contrary to this view, however, pseudoenzymes have now emerged as crucial players operating with an impressive diversity of mechanisms that we are only beginning to understand.”2

In other words, the biases created by viewing pseudoenzymes as the byproduct of evolutionary processes hindered biochemists from identifying and characterizing the functional importance of pseudoenzymes.

But this flawed perspective of viewing pseudoenyzmes as junk is changing. To date, biochemists have identified at least four functional roles for pseudoenzymes:

  1. They serve as protein anchors, locating cell signaling enzymes to appropriate locations within the cell.
  2. They function as scaffolds bringing enzymes of the same signaling pathway into proximity with one another, allowing the enzymes to efficiently work in conjunction with one another.
  3. They modulate the function of cell signaling proteins by binding to them, exerting an allosteric-type effect.
  4. They compete with “catalytic” cell signaling enzymes by binding the substrate without transforming it, regulating substrate transformation.

In part, the functional significance of pseudoenzymes justifies viewing these biomolecules as the work of a Creator. But, if these biomolecules are designed, why would pseudoenzymes be so structurally like their catalytic cohorts? Evolutionary biologists maintain that these similarities reflect their evolutionary history. But, if there is reason for the structural similarities, it further justifies viewing pseudoenzymes as designed systems. As it turns out, a rationale does exist for the close similarity in structure between pseudoenzymes and other members of their enzyme family. As the authors of the survey note:

“Enzyme structures are predisposed to mediating interactions with protein or metabolite ligands and thus these folds are the ideal templates for nature to repurpose for entirely new functions.”3

In other words, for pseudoenzymes to influence cellular signaling pathways, they must bind substrates and interact with other proteins in the pathways with a high degree of specificity and with the identical specificity as their catalytic counterparts. Their close resemblance to their catalytic analogs allows these biomolecules to do just that.

In short, in fulfilling their vital role as regulators of cell signaling pathways, pseudoenzymes display elegance, sophistication, and ingenuity. As a creationist, this is the reason I view these systems as a Creator’s handiwork. Because the field of pseudoenzyme biochemistry is so young, I anticipate the evidence for design to dramatically expand as we learn more about these surprising biomolecules.

Yet, despite everything we have learned about pseudoenzymes, adherents to the evolutionary paradigm simply can’t see these biomolecules as anything other than the product of an evolutionary history.

Because of the blind spot created by their philosophical commitments, the design of these systems is occluded from their view—and that causes them to miss the mark.

Resources
The Cell’s Design: How Chemistry Reveals the Creator’s Artistry by Fazale Rana (book)
Pseudoenzymes Make Real Case for Intelligent Design” by Fazale Rana (article)
Q&A: Is Christianity a Science Showstopper?” by Fazale Rana (article)
Does the Evolutionary Paradigm Stymie Scientific Advance?” by Fazale Rana (article)
Q&A: Is Evolution Falsifiable?” by Fazale Rana (article)

Endnotes

  1. Patrick Eyers and James Murphy, “The Evolving World of Pseudoenzymes: Proteins, Prejudice, and Zombies,” BMC Biology 14 (November 2016): 98, doi:10.1186/s12915-016-0322-x.
  2. Ibid.
  3. Ibid.
Reprinted with permission by the author
Original article at:
https://www.reasons.org/explore/blogs/the-cells-design/read/the-cells-design/2016/12/07/pseudoenzymes-illustrate-science’s-philosophical-commitments