NEW MATERIAL SCIENTIFIC FACTS AGAINST
PROTEIN: THE BRAINLESS WONDER
HUMANITY'S TRUE HISTORY - 'THE BRAIN POLICE'
Wind": A Hollywood History of the
Scopes Trial -
PROTEIN: THE BRAINLESS WONDER
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
PROTEIN TRAMPLES EVOLUTION. Its existence, structure and function disproves evolutionary theory. Here is the
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
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
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
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
Eventually glycine, leucine,
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
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
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
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
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
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
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
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
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
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
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
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
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
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
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
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
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.
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
Because the protein can quickly respond to what is
happening around it, vital functions can occur which otherwise would be
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
The protein molecule is a self-adjusting miniature
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
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
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
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
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
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
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
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
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
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
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
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
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;
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
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.
CONTINUE PART 2