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"Inherit the Wind":  A Hollywood History of the Scopes Trial - 


This is an astounding story. How can these tiny things in the cell actually do the work they do? It is totally amazing. It was written recently by the author of all the material on this website, as an example of how just one small thing in God’s creation can dumbfound all efforts to overthrow His existence and power.

PROTEIN TRAMPLES EVOLUTION. Its existence, structure and function disproves evolutionary theory. Here is the story:

Can evolution account for the existence of protein, and what it is doing right now in your body? This is a subject which every student of science should consider.

Proteins are all about the same size, with some longer than others. All are microscopic; so tiny you cannot see one with your naked eye.

Yet each little protein molecule does the most fabulous things. It carries out complicated tasks which require great intelligence. The problem is there is not a nerve cell anywhere in its body. No brains. How can it do what it does?

Each protein has a very complex structure; yet, because there are literally thousands of different protein structures, it would appear to be impossible, by random chance, to produce even one.

How could evolution fit in here?

Do you like challenges? Well, I have one for you. We are going to look at the structure and function of these little things, and see if they could be produced by the randomness of evolutionary activity.

From the latest facts unveiled by microbiology, this is the story of some of your best helpers. Along with their buddies, they keep you alive. Although brief, this is a remarkable story.

This is written for high school and college students, yet many other mature individuals will appreciate it. This will provide you with information you can use in defending your position! You are welcome to copy and use anything on this pathlights.com web site.

Historical background. In the 18th century, chemists came across certain organic substances which were rather strange. They found that heating these materials changed them from the liquid to the solid state instead of the other way around. One example was the white of the egg, another was something they found in milk (casein). Yet another was a component of the blood (globulin).

In the year 1777, Pierre Joseph Macquer, a French chemist, decided to give all these strange substances, which coagulated upon being heated, a common name: albuminous (after the word, albumen, the name that Pliny had given to egg white.)

In 1839, the Dutch chemist Gerardus Johannes Mulder found that they all contained carbon, hydrogen, oxygen, and nitrogen. Proud of the discovery, he named his four-element formula, protein, from a Greek word meaning "of first importance." That is how much he thought of his formula! But it stuck as the name for the strange substances. Over a century later, it would be discovered that it was the substances themselves—proteins (not Mulder’s inaccurate formula)—which were extremely important. They were a key ingredient in all life on earth.

But providing a name for this strange collection of substances did not explain their remarkable structures and some of the amazing things they could do. That would gradually come with time.

Let us now consider several of the many astounding facts about these tiny things:

Proteins are extremely complicated. And so are the amino acids they are constructed from.

By their own definition, evolutionists declare that evolutionary processes are always random, always purposeless, totally lacking in any planned intelligent design, yet the cause of everything in earth and sky.

However, these shuffling, bungling methods of random chance could never produce the intricate formula for even one amino acid, much less a protein that many amino acids are constructed from.

Later in this article, we will provide you with conclusive mathematical evidence that evolutionary theory could never account for a single amino acid or protein.

But, back to our story: By the beginning of the 20th century, biochemists were certain that proteins were giant molecules constructed from amino acids, just as cellulose is built up from glucose and rubber from isoprene units. Yet there is an important difference: Cellulose and rubber are made with just one kind of building block while a protein is carefully constructed from a variety of different amino acids.

What are proteins? They consist of many smaller units, called amino acids, linked together in long chains. Amino acids are organic acids which contain nitrogen. They also contain carbon, hydrogen, and oxygen. Some also have sulfur or phosphorus.

Eventually glycine, leucine, tyrosine, cystine, and other amino acids were isolated by chemists. By 1935, 19 had been identified. (One comes in two forms, producing a total of 20 essential amino acids.) Gradually, scientists were discovering that they were beginning to delve into one of the most astounding mysteries known to mankind.

Each completed chain of amino acids is called a peptide. This is actually a synonym for a complete protein. The amino acids are linked together, to form a complete peptide chain, which is a protein.

Oh, you say, it should not be too difficult for evolution to produce something like that! But, as an example, consider hemoglobin. This is a protein in the blood stream. Hemoglobin contains iron, which is only 0.34 percent of the weight of the molecule. What else is in there? —574 amino acids! All in just one protein! Here is how we know:

Chemical evidence indicates that the hemoglobin molecule has four atoms of iron, so the total molecular weight must be about 67,000. Four atoms of iron, with a total weight of 4 x 55.85, comes to 0.34 percent of such a molecular weight. Therefore, hemoglobin must contain about 574 amino acids. This is because the average weight of an amino acid is about 120.

It was through the development of new methods of analyzing amino acids and proteins that scientists gradually learned still more about them. These new methods included the centrifuge, diffusion, paper chromatography, and spectrophotometry.

Using these analytic techniques, here is a sample of what they discovered. This is what is in the blood protein called serum albumin:

It contains 15 glycines, 45 valines, 58 leucines, 9 isoleucines, 31 prolines, 33 phenylalanines, 18 tyrosines, 1 tryptophan, 22 serines, 27 threonines, 16 cystines, 4 cysteines, 6 methionines, 25 arginines, 16 histidines, 58 lysines, 46 aspartic acids, and 80 glutamic acids. That is a total of 526 amino acids of 18 different types of amino acids, all built into a single protein with a molecular weight of about 69,000. The only other common amino acid not in serum albumin is alanine.

Seriously, now, how could mindless random actions produce that protein? Yet that is only one of thousands of very different proteins in each living creature.

Are you beginning to see the picture? We must politely but firmly tell our evolutionary friends that, if their theory cannot produce protein, it is a fraud.

The German-American biochemist Erwin Brand suggested a system of symbols for the amino acids. He designated each amino acid generally by the first three letters of its name. Using that shorthand, here is the written formula for serum albumin: Gly15 Val45 Leu58 Ileu9 Pro31 Phe33 Tyr18 Try1 Ser22 Thr27 CyS32 CySH4 Met6 Arg25 His16 Lys58 Asp46 Glu80.

That is what is in one (just one) protein of serum albumin! There are trillions upon trillions of proteins in each animal, and thousands of different kinds. Keep in mind that serum albumin is only an average-size protein; many are much larger.

Do not think that, having laboriously determined the contents of a single protein, the scientists know much about it. Not so. Learning the formula was only a beginning. Next, they had to figure out the structure and arrangement of a protein molecule! "Structure" means the chemical arrangement of each amino acid; "Arrangement" is the way they are hooked together, in sequence, to form a protein.

Oh, you might say, that should not be too much of a problem. If evolution’s random actions can make them in the first place, then biochemists ought to easily figure them out. That is true! However, it was only with great difficulty that scientists were able to determine the structural sequence of even one protein. They were discovering that the randomness of their favorite theory could never have produced protein.

The only way biochemists can make a useable protein is by carefully copying the patterns found in living creatures.

Just as scientists cannot do it, so evolutionary development could never invent a workable protein with a new, different formula. Yet the theory says that proteins, like everything else, are supposed to have originated by mindless chance.

The first problem was to ascertain how the amino acids were joined together in the protein-chain molecule. In 1901, the German chemist Emil Fischer managed to link some amino acids in a chain. Mind you, all he did was take existing amino acids and hook them together. He did this by connecting the carboxyl group of one amino acid to the amine group of the next. Sounds simple enough, but it took years for science just to reach that point.

After struggling for six years in a well-equipped laboratory, by 1907 Fischer finally managed to hook together ("synthesize") a chain made up of 18 of the same amino acids. He did not have a complete protein, nor one in the proper sequence of different amino acids. One of the best brains in Germany took six years to do a little part of that which occurs in a split second in the cell.

Fischer well-knew he did not have a protein molecule, yet he simplistically imagined that this was only because his chain was not long enough. Because he correctly suspected that proteins broke down in the stomach to amino acids, Fischer called his synthetic chains peptides, from a Greek word meaning "digest."

Researchers would try to link together amino acids. The resulting chains were given the name, "peptides," but they were not real proteins. Any group of amino acids, linked together naturally or artificially, is called a peptide chain. But, of course, only the ones produced in nature are genuine, useable proteins.

After years of labor, by 1916 the Swiss chemist Emil Abderhalden had laboriously made a synthetic peptide with 19 amino acids. No one was able to do better until 1946. It was just too difficult, even in million-dollar laboratories, to make the real thing: a genuine protein!

Yet, by this time, chemists were discovering that those little peptide chains were merely tiny fragments, compared with the size of an actual protein molecule. They knew this was true because the molecular weights of proteins were immense.

Compare Abderhalden’s 19 amino acids with the 574 amino acids, we mentioned earlier, in a hemoglobin molecule. And hemoglobin is only an average-sized protein.

There could only be one correct arrangement of each protein,—yet there are millions of wrong ways it could be arranged!

The best brains of highly trained men, working in elaborate laboratories, cannot effectively do it. They cannot even produce one new protein by merely changing a single amino acid in it.

The utter randomness of evolution could never come up with the one right combination for each protein.

But consider this: Even if, just one time, evolution could produce one correct protein,—it could never repeat that success again, which it would have to do in order to replicate that correct protein in making millions more of it.

After that, evolution would have to set to work to invent the thousands of other protein formulas used in plants and animals.

But now, let us return to those 19 amino acids of serum albumin: The number of possible arrangements, in which 19 amino acids can be placed in a chain (even assuming that only one of each is used—and this is never, never true!), comes to nearly 120 million billion. If you find this hard to believe, try multiplying 19 times 18 times 18 times 16, and so on, down to 1. These are all the possible arrangements.

Yet, in just one average-sized protein, such as serum albumin, we have more than 500 amino acids. The number of possible arrangements of those 500 amino acids comes to 10600. That is a totally impossible amount! It is a quantity so vast that you might as well forget about the possibility of so-called "random selection" producing it even once. The entire universe, packed with subatomic particles, could not hold 10600.

In 1945, the British biochemist Frederick Sanger set to work trying to figure out the sequence of one of the smallest proteins: insulin. By slow, painstaking chemical treatments, he and his associates were able to split the insulin protein into individual amino acids. Then they broke separate amino acids at their weaker bonds. Ultimately, they had a lot of pieces. Chemical treatment plus paper chromatography helped them. After years of hard work, by 1952 they had put all the fragments together and arranged them in their proper sequence. They announced their achievement in 1953. For the first time, the complete structure of a protein had been identified. Six years later, in 1959, a second protein, ribonuclease, was identified. Since then, improved technology has enabled biochemists to determine additional ones.

Such analyses have shown that, in varying amounts, most proteins contain all 20 amino acids. It is only a few of the simpler fibrous proteins (such as those found in silk and tendons) which are heavily weighted with only two or three types of amino acids.

One important discovery was this: The individual amino acids are lined up in no obvious order. There are no periodic repetitions! Everything is an apparent jumble of amino acids in each sequence;—yet these proteins work, and no other man-made combinations do!

Random chance is not able to produce one useable protein; neither can trained laboratory technicians when they try to invent new proteins. Evolution flunks the test.

Where did these useable proteins come from, if evolution did not produce them? They surely did not make themselves. And man cannot make them either. Yes, a scientist can try to take apart a true amino acid and try to put it back together again in the same order, but he cannot make a new combination which works.

The best that man can do is to imitate what is already there. In 1953, the American biochemist Vincent du Vigneaud succeeded in synthesizing a peptide chain exactly like that thought to represent the natural hormone, oxytocin. Oxytocin is extremely small and has only eight amino acids.

(The word, "synthesis," is used to describe both the natural hooking together of amino acids into proteins, by constructor proteins, and also man-made productions which are done by carefully copying the chemical sequence found in nature.)

In 1965, insulin was synthesized, and later several other proteins.

Each protein is carefully assembled by another protein, from materials lying around. And it never makes a mistake.

That tiny thing, a single protein, moves around, picking up amino acids here and there and sticking them together. Higher and higher goes the assembly, until that little protein has made another complete protein! But how can this be, since there are no brains in non-neuron cells? There surely are none in that little protein which always carries out this construction project alone. And the little fellow does it in a few seconds!

We are confronted here with something beyond our ken. This is not something which the randomness of evolution could ever provide us with. A far higher Intelligence is involved.

When protein is eaten, it is broken down in the stomach into amino acids. These are absorbed by the lacteals in the small intestine and pass into the blood stream. They are then carried to the liver, for processing, and to cells throughout the body. Passing into the cells, they are assembled ("synthesized," the biochemists call it) into proteins.

What assembles them? Other microscopic proteins which were themselves assembled only a short time before. Who taught a protein how to assemble another protein? Think about that awhile. And you say you are still an atheist?

If the constructor protein finds he does not have the right amount and combination of amino acids lying around, he tells another protein to bring him some more! The messenger goes to the edge of the cell and tells the gatekeeper (another protein) to bring them in, which he does. More about the gatekeeper later.

Keep in mind that each protein consists of hundreds of amino acids, all arranged in a totally complicated order; and each, different protein has a completely different structural sequence than all the others!

Without several days of intense concentration, neither you nor I would be able to memorize the sequence of even one average-sized protein.

Where is the brain in the cell to be able to do this? We are here viewing something that cannot be done; yet it is being done, millions of times a minute, in every cell in your body. If it were to stop for even a minute, you would die.

Then, incredibly, as soon as each protein is assembled in its correct linear sequence, it automatically folds itself into a very definite, but exquisitely complex, shape!

Nearly all types of proteins bend and curve back and forth over, under, and around themselves;—and each protein has a certain pattern it follows. Scientists call these the "fold patterns." As we will learn below, if the folds do not occur in the proper way, the protein cannot perform its functions properly.

How could evolutionary theory produce those proper fold patterns? It takes brains to do all this; and so-called evolutionary methods are brainless, aimless, and useless as a means of doing anything worthwhile.

Using X-ray diffusion, by 1959 the Austrian-English chemist Max Perutz and his English associate John Kendrew managed to figure out the folded placement of hemoglobin and myoglobin.

The chemical bonds which link successive carbon atoms in the backbone of the protein are known as covalent bonds. (Covalent bonds are formed when two adjoining atoms share their electrons with one another, to complete electron shells.) Nearly all the atoms in the organic compounds, used in living organisms (sugars, fats, amino acids, the nucleotide bases in DNA, etc.), are linked together by covalent bonds.

But there is also another type of chemical bonding of atoms which does not share electrons. This is based on weaker electrostatic forces between neighboring atoms. These are known as noncovalent bonds. They are also called weak chemical bonds.

The chains of amino acids in a protein are able to bend at the points where these weak bonds are located. They are called crease points.

The protein molecules automatically bend by themselves, and always in the proper fold direction. While the protein is being synthesized (put together) by another protein, it is positioned in a linear (line-length) fashion. But as soon as it is completed, the entire protein folds itself into a special pattern!

This folding takes a fraction of a second; and, when it is completed, the protein molecule has taken the shape of an extremely complicated three-dimensional collection of atoms.

How could evolutionary theory accomplish results like this? And do it repeatedly, trillions of times?

The unfolded protein chain is capable of folding into its native form, without the assistance of any other component of the cell. It folds at those crease points. But how can it know which way to fold at those points? And who planned where those points would be located, so the folding could produce the important results it does? The protein did not figure that out. And why does the new protein wait until it is completely assembled, by another protein, before it folds up? It should be expected to start folding as soon as it was partially made; this, of course, would confuse and stop the rest of the construction.

This would be like origami papers waiting awhile and then automatically folding themselves, and always in the proper fold directions.

The ability of proteins to assemble themselves automatically is a key capability which is essential to their biological role. Without this ability, the proteins could not manipulate or construct. No sort of self-replicating machine could function unless its component machinery was self-assembling.

Can you imagine a machine which can assemble itself? Man is not able to make a robot which is able to assemble itself. As far as we know, proteins are the only self-assembling devices. Yet, having assembled themselves, they are able to carry out a wide variety of functions. More on this below.

Each type of protein always folds itself into the best pattern for accomplishing the work it is supposed to do! Every new fact about protein seems more fantastic than the preceding one, yet there is more to come.

As soon as the split-second folding is finished, negatively charged groups associate with positively charged groups, to keep everything in place; and the resulting structure is exactly that which is needed for the task it is supposed to do.

Every amino acid in the chain has something sticking out one side. These are important, and are called side chains or fingers. Some of these side chains are hydrophobic and some are hydrophilic. The hydrophobic ones do not have an affinity for attachment to water molecules while the hydrophilic ones do.

Now, it is very important that certain cell processes be completed in a water medium while others can only be done where water cannot penetrate. When the protein folds down, it always does it so in exactly the right way, so the water-resisting amino acids are at the center of the folded protein structure and the water-attaching ones are on the outside. In this way, the hydrocarbon (water-loving) side chains, on the outside, can carry out chemical, and other, reactions with the watery environment in the cell while the amino acids, in the center, can perform functions in a location where there must be little or no oxygen or hydrogen.

Sounds complicated? It surely is; yet, without it life could not continue. There are hydrophobic amino acids and lipids (fats) which must be synthesized, and that can only happen where the water is shut out.

The end result is a protein which has folded itself into a tight water-avoiding ball, yet one in which the outside is in water and able to interact efficiently with it, so it can take in needed substances.

Water itself is another marvel which we do not have the space to discuss here. It was designed to be unable to dissolve lipids (fats and oils) and compounds containing hydrocarbon chains. In addition, it is not a good medium in which to synthesize organic substances. So those functions must be done in the center of the protein molecule, where water has been excluded.

(You might wonder why water has this apparent flaw. It was intentionally designed in this manner and is not a flaw. The organs in your body could not accomplish their work if the lipids in them could be dissolved by water. Modern planographic printing presses use this same formula: They can only print on paper because water and oil do not mix.)

Think about this for a minute. The "waterproofed" amino acids are carefully placed in just the right portions of that long protein chain. The strong and weak bonds are placed at just the right points so that, when the protein automatically folds itself, the outer portions will wrap themselves in exactly the proper manner so that, on all sides, the water-excluding portions will be completely enclosed.

In view of the complicated manner in which the proteins fold in upon themselves, it would take months for a scientist to figure out how to fold one so that the watertight portions would be in the middle and the right arrangement of strong and weak bonds would be on the outside. Yet the little proteins are quickly made in a brainless cell which just as quickly, and correctly, folds in upon themselves.

This reads like fantastic science fiction. But it is true, and without it you would not be alive. There is more:

It is vital that some of the little fingers which protrude from the folded protein have both strong and weak bonds. The strong bonds are needed exactly at those points where the protein needs to solidly bind with other like proteins. The weak bonds must be located at just those places where the protein must temporarily hook up with various substances.

For example, a muscle protein must be able to solidly bond with neighboring ones, yet be able to absorb needed nutrients. The little fingers have to be located in just the right places.

How could this be planned out in advance?

It is the proteins which carry out all the atomic manipulations on which life depends. Yet in order to do it, each protein must be able to permanently or temporarily make contact with other molecules. Whether they be proteins, amino acids, or miscellaneous chemical supplies, the substances with which the protein makes contact are called ligands.

Nearly all these associations between a protein and its ligand are done by means of the weak chemical bonds. Since each weak bond is rather frail, the contact must be made using several weak-bond points on the protein.

If those bonds were either weaker or stronger, the proteins could not carry out their work. If the contact was a little weaker, contact could not be properly made; if a little stronger, the two would lock together so solidly, they could never separate.

In the structure of every part of the physical organism, you will find that every detail has been perfectly worked out! We observe highly intelligent planning, not aimless chance.

Just as the strong and weak atomic forces must be exactly as they are, in order for all atomic structures to function properly, so the difference in strength between the strong and weak bonds on the protein must be just right.

It turns out that the strong bonds are about 20 times stronger than the weak bonds; this is just the amount needed, so portions of the protein can bind while other portions can make fast contacts with other substances.

How fast?

The interactions of a single protein with other substances can occur several times a second. The case of enzymatic action produces results as often as 106 times per second! That is a million actions a second!

But since nearly every function in the body depends on the activity of these proteins, one can understand why they have a lot of work to do and need to be able to do it quickly. Tissue is constantly being worn out and must be replaced. Food must be processed. Waste must be eliminated. Manifold processes are repeated constantly, just to keep you alive and well.

Who thinks evolution should get the credit for this?

The protein molecules have, what scientists call, metastability. This is the ability to rapidly change shape, in order to adapt to changing circumstances around them.

It is the weak bonds which hold the protein in its characteristic shape. Under the stress of very minor physical or chemical challenges, these bonds give way. This makes each protein fragile. Yet it is a necessary quality.

If the temperature is increased only a few degrees, the proteins unfold. If the chemical environment is changed a little, they unravel. If another molecule is attached to them, they change shape. In the midst of stability, there is a necessary instability. If this were not so, the protein structures would not be aroused to go into action in time of injury or crisis in the cell.

Yet there are other reasons why metastability is so important.

Because the protein can quickly respond to what is happening around it, vital functions can occur which otherwise would be impossible.

The arrangement of a protein is subtly affected as soon as it binds to another molecule. Any such interaction will cause molecular distortions which will be transmitted throughout the entire molecule and affect, not only its shape, but its functioning.

Each time a protein temporarily connects with a ligand, the protein reacts to chemical data from the ligand. This causes the protein to do something which often affects the ligand.

When the protein is making contact with several different ligands at the same time, it is receiving, integrating, and outputting data or chemicals simultaneously, yet separately, to this one or that one!

And some people suppose all this is supposed to have come from evolution?

The protein is able to integrate information from several different chemical inputs, each being determined by the concentration in the cell of a particular chemical.

This astounding function of the protein molecule is called allostery. It enables the protein to do three things at once: (1) produce chemical reactions upon another substance, (2) receive and integrate within itself special information, and (3) increase or lessen its own chemical reactivity in relation to that information. Jacques Monod called this remarkable ability, "the second secret of life" (J. Monod, Chance and Necessity).

Because of this, proteins are not only capable of carrying out a specific chemical reaction, but are also able to integrate and intelligently respond to changes in their chemical environment.

The protein molecule is a self-adjusting miniature machine!

Allostery is the ability to self-regulate, and this is what the proteins can do. They must be ever aware of constant changes, in the cell, and able to react to them.

Because of this ability, proteins are far in advance of any artificial device which man could make—and certainly far in advance of anything that the mindlessness of evolution could produce. In even the most advanced man-made machines, the regulating functions of a machine are always separate from the working parts. In an oven, the regulator (thermostat) and heater (functional unit) are separate; in a protein, they are united. This allosteric function is vital to enzymatic action.

The amazing protein molecule is able to carry out the most complicated enzymatic activity automatically, yet all the while being able to adjust that activity to meet the needs of the situation.

Catalysis was a function which scientists began discovering toward the end of the 18th century. When they started studying chemical reactions, they discovered that the reaction rate (time it took for a chemical to respond to an effect) could be greatly speeded up if there were small changes in the environment. For example, the Russian chemist Kirchoff found that starch could be converted to sugar in the presence of acid; yet, while the acid speeded up the process, it was not itself consumed. The same amount of acid was still there. The acid was a catalyst. The substance which it acted upon was the substrate.

Then it was discovered that there were catalysts in the organic world. Bread dough, left to itself and kept from contamination, will not rise. But add a little yeast (leaven comes from the Latin word, "rise") and bubbles appear, lifting and lightening the dough.

In 1777, the Scottish physician Edward Stevens took fluid from the stomach and found it would dissolve protein. In 1834, the German naturalist Theodore Schwann isolated a substance he called pepsin (Greek for "digest") from the stomach acid.

In 1930, John Northrop, working at the Rockefeller Institute, established that all the enzymatic functions in living tissue were carried out by proteins.

It is now known that there are over 2,000 different protein enzymes, and they are all unmatched by any other substance for efficiency and specificity. Each protein, which works as an enzyme, works with just one type of substance.

Catalase is the protein enzyme which catalyzes the breakdown of hydrogen peroxide to water and oxygen. Yet this can also be done by iron filings or manganese dioxide. But, weight for weight, catalase accelerates the rate of breakdown faster than an inorganic catalyst can. Fast? Yes, fast! Each molecule of catalase can bring about the breakdown of 44,000 molecules of hydrogen peroxide per second while operating at a temperature of 00 C.

How is that for business efficiency? Something the random actions of evolutionary theory could never accomplish. Tell me where I can hire a worker who can do forty-four thousand things a second, and I will hire him.

(The protein enzymes can do this because an extremely small dilution of them is needed to effect such changes. How that can be is not known, since the enzymes do not give off, or lose, any substances in the process.)

Do not underestimate the need for continual enzymatic activity in your body! Cyanide, one of the most deadly of all poisons, kills people by stopping their enzymatic proteins from working. Without multiplied trillions of them every moment, you would die within 10 seconds. Nearly every other major poison also kills by stopping the enzymatic action of proteins. (An exception is carbon monoxide which locks with hemoglobin, keeping it from carrying oxygen to the cells.)

As noted earlier, it is a remarkable fact that each type of protein enzyme only acts on one type of substance. That makes them ideal catalysts. Catalase only breaks down hydrogen peroxide and nothing else; yet inorganic catalysts, such as iron filings and manganese dioxide, will break down hydrogen peroxide and also a variety of other substances. If catalase did that, it would be harmful in the body.

In living tissue, everything is perfectly designed. In contrast, the utter randomness of evolutionary processes accomplishes nothing worthwhile. Randomness never does.

There is far more that we could say about protein enzymes and their substrates, but let us now turn our attention to other wonders of protein.

Keep in mind that it is because of the allosteric quality of proteins that they can accomplish so much as enzymes. The actual activity of individual enzymes are self-regulated, so the protein can increase or decrease its catalytic activity as it is needed

Another amazing function of proteins is that those tiny things regulate the metabolism of the entire body.

A living body is a chemical plant and must be able to take in oxygen, water, carbohydrates, fats, proteins, minerals, and other raw materials. It must be able to process them and also destroy bacteria and eliminate wastes, such as carbon dioxide and urea. Each of these functions requires extremely complicated actions, yet they are vital to existence. All this is done by those fabulous little protein molecules.

Thousands of protein-induced actions and reactions must take place for each accomplishment, regardless of how small. Every major conversion in the body involves a multitude of steps and many enzymes.

Someone will say that life began with bacteria and evolved over long aeons; so there was lots of time for proteins and enzymes to be invented. Not so. The simplest organisms have lots of protein, and carry out many enzymatic functions. Even an apparently simple organism, such as the tiny bacterium, must make use of many thousands of separate enzymes and reactions. All this complexity is vital to existence. Without it, the creature would quickly die.

Evolution says a little improvement happened here, and another advance there, and gradually a living creature came into existence. That is another fiction. In reality, everything had to be in place all at once in each plant and animal. All its organs, proteins, and structures had to be there in the beginning, in order for it to exist. Nothing could be left out or added later.

A small army of proteins carry out complicated organic cycles. It has taken years of laborious labor, by a small army of researchers, to figure out the various metabolic cycles. In each one, proteins change one substance to others, and then to yet others, and then still others. Every step is complex, yet the finished result is always perfect.

How can this be done, when different proteins which never meet each other take part in the different steps? And, as you know, none of the proteins live very long; and none of them teach the new proteins they construct how to do the work they are going to do! There are no classroom teachers in the cell, for all the students have no brains; yet they all know exactly what to do!

Are you going to keep believing those who tell you that evolution is responsible for this!

The Krebs cycle is used to reduce lactic acid to carbon dioxide and water. There is the urea cycle, the fatty-acid oxidation cycle, and many others. All are vital to existence and each is so complicated, that it took years for researchers to figure them out.

How efficient are these cycles? They produce outstanding performance! For example, in 1941, the German-American chemist Fritz Lipmann discovered that carbohydrate breakdown yields certain phosphate compounds which are stored. We now know that this cycle stores unusual amounts of energy in, what came to be known as, the high-energy phosphate bond. This is transferred to energy carriers present in all cells. The best known of these carriers is adenosine triphosphate (ATP). They store the energy in small, readily used packets. When needed, the phosphate bond is hydrolyzed off and the energy is available for quick chemical energy required in the building of proteins from amino acids, the electrical energy needed for nerve impulse transmission or muscle contraction, etc.

Everywhere you turn in biology, you find new wonders which the doddering effects of evolutionary theory could never produce.

Men in their high-tech laboratories cannot as efficiently duplicate these protein functions. Seriously now, if a trained scientist, working in a million-dollar fully equipped facility, cannot improve on what the little proteins easily and rapidly do, then how could random motions of molecules produce those proteins in the first place? It could not be done.

Multiplied trillions of individual proteins are not only in each animal, but also in each plant. There is no way that evolutionary theory could have put them there.

Yes, plants as well as animals! Every living creature has proteins in it; there are no exceptions.

The proteins in plants build carbohydrates, fats, and proteins from simple molecules, such as carbon dioxide and water. This synthesis calls for an input of energy, and the plants get it from the most copious possible source: sunlight.

Certain proteins in green plants convert the energy of sunlight into the chemical energy of complex compounds—and that chemical energy supports all life forms (except for certain bacteria).

This process is called photosynthesis (Greek for "put together by light").

These plant proteins take carbon dioxide from the air, mix it with sunlight from the sky and water taken up from the root;—and, presto! carbohydrates, the basic food of life, are produced. (The plant itself also needs nitrates, phosphates, and certain other substances from the soil for normal growth.)

In 1817, two French biochemists (Pierre Pelletier and Joseph Caventou) isolated the substance that gives the green color to plants. They named it chlorophyll (Greek for "green leaf"). In 1865, the German botanist Julius von Sachs showed that chlorophyll is not found all through plant cells (even though leaves appear uniformly green), but only in extremely small bodies called chloroplasts. Here are more protein friends; in them photosynthesis takes place. It is only here that the plant uses chlorophyll.

Inside the amazing chloroplast, you will find, what some scientists describe as, little stacks of coins. These are the lamellae. In most types of chloroplasts, these lamellae thicken and darken in places to produce grana—which contain the chlorophyll. This is only mentioned to reveal a hint of the utter complexity of these protein structures!

How could the purposeless meanderings of evolution produce something like this? Yet the chlorophyll and the chloroplasts had to be there on the first day each plant came into existence—or it would have immediately died. This is because the process of photosynthesis provides food not only for animals, but for plants as well.

It was not until 1954 that the Polish-American biochemist Daniel Arnon, working with spinach leaves, managed to isolate chloroplasts intact. He discovered that inside each tiny one is not only chlorophyll, but a large collection of specialized protein enzymes, related protein, and other substances. All of them are carefully and intricately arranged. If you think that everything is arranged well under the hood of a modern automobile, you ought to take a look inside a sub-microscopic chloroplast.

How did all that perfect order and well-functioning organization come into existence? Not through the slow, dawdling inattention of evolution!

Research by scientists, stretching from 1906 to 1960, was conducted in order to figure out what was in chlorophyll. This strange protein substance was found to have a porphyrin ring structure basically like that of heme (the oxygen-carrying substance in blood hemoglobin). The difference was that chlorophyll had a magnesium atom at the center of the ring instead of an iron atom.

Meanwhile, other researchers were trying to learn how chlorophyll carried on its catalytic work. By the 1930s, all that was known was that carbon dioxide and water go in and oxygen comes out. Only intact chloroplasts performed the functions, so researchers were stumped as to what was happening inside.

If the best brains in the scientific world can hardly figure out the matter, how could the fooleries of evolution produce it?

The use of radioactive tracers (especially carbon 14) and the development of gas and paper chromatography greatly helped. Using these new tools, one of the scientists’ first discoveries was the lightning speed with which the tiny protein substances within the chloroplast carried on their work! An incredible amount of complicated work is done within seconds.

Well, by now you probably want to know the answer to the riddle. Here is how proteins in the chloroplast produce carbohydrates,—and you cannot thank evolutionary processes for giving the process to us:

Carbon dioxide is added to the normal five-carbon ribulose diphosphate, making a six-carbon compound. This quickly splits in two, creating three-carbon glyceryl phosphate. A series of reactions involving sedoheptulose phosphate and other compounds then puts two glyceryl phosphates together, to form the six-carbon glucose phosphate. Meanwhile, ribulose diphosphate is regenerated and is ready to take on another carbon-dioxide molecule. This cycle is repeated six more times. Each one supplies one carbon atom (from the carbon dioxide) and produces a molecule of glucose phosphate. Then the six cycles are repeated over and over again.

Now you can go home and try to do it yourself. If a brainless protein learned it by random chance, surely you ought to be able to improve on the process. I guarantee that, if you succeed in doing it more efficiently, you will make half a billion dollars for yourself.

The catalytic action of the chlorophyll uses the energy of sunlight to split a molecule of water into hydrogen and oxygen, a process called photolysis (Greek for "loosening by light"). In this way radiant energy of sunlight is converted into chemical energy. The resultant hydrogen and oxygen molecules contain more chemical energy than did the water molecule from which they came.

Sounds complicated? It is. Surely there must be some other way to do it. No one has found that way, or any way, to produce carbohydrates. But there is a way to break up water molecules into hydrogen. However, it takes a lot of energy: The water must be heated to 2,0000 C. or a strong electric current must be sent through it. Yet chlorophyll does it at ordinary temperatures and with energy from relatively weak light.

Neither mindless evolution nor intelligent men can do what millions of little proteins regularly do. Yet those tiny proteins have no brains. They cannot talk, they cannot see, they cannot think. Each protein is just a collection of amino acids, without one nerve cell being present anywhere in their tiny structure.

We are here confronted with an Intelligence beyond that of man or nature. A great Designer is at work.

Under ideal conditions, plants have a near 100 percent efficiency in producing energy. Astounding! Pooling all our vast human intelligence and technology, if we could somehow match that with machines which could produce high-efficiency energy from sunlight, we could solve all our fuel problems! Every one of them. The only waste would be lots of extra oxygen! And we could sure use that.

But the greatest brains among us are unable to do what the diminutive protein molecule in the leaf does with ease, and all without the help of evolution.

The action of plant proteins also provides us with our oxygen. The scale on which the earth’s green plants manufacture organic matter and release oxygen is enormous. It is estimated that, each year, they combine a total of 150 billion tons of carbon (from carbon dioxide) with 25 billion tons of hydrogen (from water) and liberate 400 billion tons of oxygen. Plants of forest and field produce about 10 percent of this oxygen, and one-celled plants and seaweed in the oceans provide us with the other 90 percent.

Amino acids in animals are only composed of L-amino acids. This is an extremely important point in the ongoing creation-evolution debate.

It is impossible for man to synthesize amino acids, without producing an equal number of left-handed (L) and right-handed (D) amino acids. Yet animals can only use the left-handed form. The chemical composition of both is identical; the difference is which side the important side chain, or finger, protrudes from.

Evolutionists, desperate to prove the validity of Darwin’s theory, have repeatedly tried to produce only L-amino acids. But they cannot do it.

It has been scientifically proven that an animal will be crippled or die if it has any D-amino acids in it. Yet, even though both types of amino acids are formulated in equal amounts in the laboratory, both chemical and X-ray analysis reveals that only the left-handed form is produced in animals. Is not that a remarkable fact!

If the random processes of evolution really did produce amino acids, then we would have even amounts of both kinds; always.

There is a little mystery here: Why are only L-amino acids found in animals?

The answer is that they are the only kind which are biologically useful: In the left-handed form, the side chains stick out alternately on one side of the central line and then the other. A chain composed of a mixture of both isomers would not be stable. This is due to the fact that, whenever an L-amino acid and a D-amino acid are next to each other, two side chains would be sticking out on the same side, crowding them and straining the bonds.

You will recall that we earlier learned that those side chains are vital in holding neighboring peptide chains together. Wherever a negatively charged side chain on one chain is near a positively charged side chain on its neighbor, an electrostatic link is formed. The side chains also provide hydrogen bonds that can serve as links. The binding together of the polypeptide chains accounts for the strength of protein fibers. It explains the remarkable toughness of spider webs and the fact that keratin can form structures as hard as fingernails, tiger claws, alligator scales, and rhinoceros horns. (A polypeptide is the scientific word for a group of proteins which have linked themselves together.)

The questions keep piling up in our mind: How can the cell know what kind of protein to assemble from the amino acids? How can its component proteins know what types are needed and how much of each? How can they know the correct sequence? How can they know how to put everything together properly?

That which they do is far more complicated than assembling Tinker Toys or Legos. Indeed, it would be equivalent to one man, without any previous instruction, ordering all the needed supplies and, then, without any help, building houses, one right after the other. Yes, some men have done that; but they had large cerebrums to think with and large cerebellums, so they could coordinate their movements. The little protein lacks all this.

We really do not know how the little fellow manages; yet, given a steady flow of raw materials from the blood stream, he always selects the type and amount of amino acids needed to construct whatever kind of material is needed.





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