The Next Step

Compared to the ultimate complexity of life, the naturalistic advent of amino acids would be simple child’s play. The real meat of the problem comes with the formation of proteins, genetic material, and the cell as a whole.

You see, amino acids, under certain conditions, begin linking together by peptide bonds, forming chains known as polypeptides. While some proteins are composed of single polypeptide chains, others are complex, incorporating many peptide chains within their construction. In either case, conditions must be excruciatingly accurate for the chains to assemble correctly, and any deviations from those conditions are detrimental to the nascent proteins.

Assemblage itself is not so straightforward a process as one would expect. Polypeptide chains are formed when amino acids – by eliminating water molecules from their composition – form those peptide bonds in question. Under natural conditions, this process is far less likely to occur than the opposite, whereby peptide bonds degrade by taking on additional water molecules through a process known as hydrolysis.(1) Hydrolysis of course is exasperated in the presence of an abundance of water, which, interestingly enough, is where the mainstream claims the first biopolymers formed!

What’s more is the fact that – assuming peptide bonds could magically form in spite of their aqueous environment – the nature of their bonding is not limited to a single site, thereby making the assembly of any given polypeptide chain somewhat random without critical guidance and maintenance protocols in place. In other words, proper chains can only be constructed if bonds are formed in the appropriate areas.

In observable biology, intricate enzymatic control systems are enacted to avoid the production of improper, and often dangerous, chains. If life today employs such stringent control methods to ensure the proper assembly of necessary proteins, utilizing a range of cellular functions, how then was it possible that this occurred originally in the harsh environment of the early Earth, especially outside the protection provided by the cellular body itself? Even the basic assembly of two amino acids joined by a single peptide bond is difficult under natural conditions, yet average proteins are composed of as many as four hundred amino acids,(2) with the largest known protein, connectin, being comprised of 26,926 amino acids.

The complexity of proteins themselves cannot be understated as well. Though essentially all proteins are composed of various combinations of the most common twenty amino acids, the range of those combinations is breathtaking, with as many as one hundred-thousand individual types of proteins known just from the human body,(3) and with untold numbers existing across the remainder of nature. Not only is their range diverse, but their shapes also, each being critical to their function, determined by their amino acid constituents, forming twisted, bundled molecules that fold and flex in reaction to the systems they interact with.

The inherent complexity of proteins can be seen in the common hemoglobin molecule, the protein used by each of our red blood cells to transport gases – including oxygen – throughout our bodies and to our tissues and organs. Each hemoglobin molecule is made up of as many as 100,000 atoms, but critically, it contains only four iron atoms. These iron atoms – electrically charged to form ions – are situated within the hemoglobin structure, secured by a protective non-protein molecule called heme.

Due to their position within the hemoglobin molecule, oxygen molecules can access the iron ions, yet other molecules, such as water, are held at bay. As air is drawn into our bodies by breathing, it is channeled into the alveoli of the lungs, where the oxygen it contains comes in contact with red blood cells there, quickly diffusing into them. Inside, a single oxygen molecule forces its way into a hemoglobin molecule, at which point the hemoglobin begins to alter its shape, opening just enough to allow three additional oxygen molecules access. This process occurs rapidly, with the first interaction stimulating all subsequent others immediately in a process known as cooperativity, and in seconds approximately 95% of the 250 billion hemoglobin molecules on each red blood cell within the lungs has been filled to capacity! As the blood transits through the circulatory system, it deposits oxygen, with the hemoglobin molecule changing shape yet again, preventing deposited oxygen from being reabsorbed, and acquiring carbon dioxide molecules in the process before returning to the lungs and repeating the cycle.

As one commentator put it, the process is quite a bit like a cab service (hemoglobin molecules within red blood cells) picking up travelers (oxygen molecules) from the airport (lungs). As the first passenger enters the cab, it subsequently opens the cab doors for three additional passengers. Fully loaded, each taxi departs, following a circuitous path around the body, dropping off its passengers along the way, and picking up others (carbon dioxide molecules) for their own trip back to the airport. It’s a whimsical comparison, but certainly a valid one.

3.04 Hemoglobin Molecule
Figure 3:04 – Hemoglobin Molecule

It is only due to the specific construction of particular peptides in particular places that provide the hemoglobin molecule with its ability to flex and alter shape, thereby allowing it to carry out the vital function of gas exchange. This example is but one of hundreds of thousands – each as complex as it is critical – and without it in perfect, functional form life could not exist. Are we to just accept that the incredible diversity of these molecules simply appeared by accident in a hostile world? As great a hurdle as it is to imagine the formation of delicate amino acids in that world, how much more impossible is it to envision the rise of the infinitely more complex proteins?

As one source figured, life requires, at a minimum, some 250 proteins to function. The actual statistical odds associated with the naturalistic formation and requisite interaction of those proteins was estimated to be a staggering one-in-a-trillion trillion trillion trillion trillion trillion.(4)

In fact, new evidence from the Stanford University School of Medicine actually indicates that even this frightfully unlikely figure is too small an estimate, with the new research suggesting that no less than a thousand proteins – four times as many as the original estimate – are actually required for life at its most basic form to exist.(5)

Notes & References

  1. Sarfati, J., “Origin of life: the polymerization problem,” TJ 12(3):281–284, 1998
  2. Bergman, Jerry, “Why the Miller–Urey research argues against abiogenesis,” Journal of Creation 18(2):28–36 August 2002
  3. Toledo, Chelsea  & Saltsman, Kirstie, “Inside Life Science, Genetics by the Numbers,” National Institute of General Medical Sciences, posted June 11th, 2012, http://publications.nigms.nih.gov/insidelifescience/genetics-numbers.html, retrieved May 26th, 2015
  4. “Expelled: No Intelligence Allowed,” Stein, B., 2008 DVD, Directed by Nathan Frankowski, Premise Media Corporation, L.P.
  5. Thomas, Brian, M.S., “First Cell’s Survival Odds Not in Evolution’s Favor,” Institute for Creation Science, September 8th, 2011, https://www.icr.org/article/6374, retrieved June 23rd, 2015

– This was an excerpt fromRemnants of Eden: Evolution, Deep-Time, & the Antediluvian World.” Get your copy here today. God bless! –


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