As a real scientist, I can destroy most of this immediately. More to follow. Before I begin I would like to point out that all my responses are things I wrote. I did not copy and paste. Most of this is old stuff I composed on evolution.

1. The complexity of living systems could never evolve by chance— they had to be designed and created.
A system that is irreducibly complex has precise components working together to perform the basic function of the system. (A mousetrap is a simple example.) If any part of that system were missing, the system would cease to function. Gradual additions could not account for the origin of such a system. It would have to come together fully formed and integrated. Many living systems exhibit this (vision, blood-clotting, etc.). When you look at a watch, you assume there was a watchmaker. A watch is too complex to “happen” by chance. Yet such living systems are almost infinitely more complex than a watch. They could not be random—they simply had to be designed and created.

Ouch. First of all, you set up a false dichotomy.

If a person says this, you might as well just walk out and leave. This most basic of errors shows that they have no understanding of basic science. Evolution is a carefully guided process.

Organisms adapt to their environment through natural selection, meaning that the environmental factors both cull the herd and remove organisms with unfavorable traits, and propagate those with favorable traits. The mechanism for this is the second rule of evolution: Evolution is brought about by genetic mutation. An organism cannot adapt to its environment per se. It is the genes that must adapt, and that process takes millions of years.

The next rule is that the determinate of what constitutes an advantage is the environment. The rest of it is really simple, Evolutionary models study this axiom because it is complex. An environment includes lots of factors like other animals, temperature, gas concentration, climate etc. etc. This axiom is the driver of evolution, the guide, Adam Smith’s invisible hand. Genetic mutation is random. It is up to the environment to nurture useful genes and ensure they get passed on, and to eliminate poor genes. This is the fundamental rule of natural selection.

This incredibly ridiculous error, to state that evolution is luck, is a confusion of genetic mutation which is luck, and evolution which is the process that selects the genes and makes sense of the randomness of mutation.

Fallacy #2 Advantageous mutation is impossible

This one is ridiculous. To understand why, a short overview of genetic mechanisms and biochemistry is necessary.

DNA is made up of polymerated strings of bases, which are nucleotides bound to sugar-phosphate backbones. DNA has two functions:
Holds the code to create various proteins from amino acids
Regulating the rate of producing proteins: By definition, one gene is a string of nucleotides that codes for one protein

The language of DNA is base-pairs. DNA is entirely comprised of four molecules. Cytosine, Guanine, Adenine and Thymine. These are the nucleotides. The nucleotides are complementary. Like magnets, they will only fit to a certain opposite. G fits with C and A fits with T (A also fits with U, Uracil, but that is an RNA base). So there are only four possible base-pairs: CG, GC, TA and AT. But these four pairs will dictate every single protein imaginable.

Chemistry has absolutely everything to do with nucleic pairing. A fits with T and C with G. They are dipolar covalents. One side is slightly positively charged, the other negative. They will bind to each other much more easily if they correspond. Trying to fit A with C or T with G is sort of like trying to force two north magnets together. This kind of error can only happen in an abundance of adenosine triphosphate. It's like protons. Have you ever wondered why they don’t repel? They smash into each other with such force that they bind (gluons). (DNA doesn’t smash into each other of course, but you get the idea. So if you have a CGAT on one string, you will of course have GCTA on the other. This is called complementary encoding, and is the basis of DNA.
There are four ways that DNA can innovate.

Intragenic mutation: Errors during mitosis can swap base-pairs around, creating new strings of bases, and a new gene
Segment Shuffling: Two different genes can recombine and form two new hybrids
Duplication error: Sometimes during mitosis, a parent cell will by accident only pass part of it’s genome to the daughter cell, thus it retains a redundant copy of a gene string. This copy is completely free to mutate based on random frequency probability.
Horizontal/vertical Transfer: During sexual reproduction, organisms exchange genes. If the organism is a diploid meaning that it’s offspring has the code of two parents, then it’s offspring will have a completely new genome, combing both parents. This is the most successful method of innovation. Or an organism, particularly prokaryotes, can actually exchange genes by means of one actually encoding a packaged gene for another, which incorporates it into the genome. This is horizontal transfer, a tool that Eukaryota do not have

There are two types of genes. Introns and exons, which have these separate functions. Exons code for proteins. Introns are mostly junk or redundant, but they flank all the exons. Sometimes they are just punctuation, dictating where a gene starts and stops, but their most important function by far is to regulate the speed of protein transcription, a mechanism we will look at it more detail later. Exons dictate how a protein will be assembled. They do this because a protein is essentially a string of amino acids or a polypeptide. Therefore, exons dictate the order of amino acids in a protein. They do this by representing each amino acid with a codon. A codon is three nucleotides. Three nucleotides make up an amino acid. There are 20 possible amino acids, but 64 possible codons, therefore, exons are highly sensitive. They are also sensitive because they are ordered very precisely. For instance, let’s look at a simple string of three codons in a gene: AGG CTT GCC. Now let’s assume that an extra base is accidentally inserted (Like a G for example). The new string would be totally different, it would look like this. GAG GCT TTG CC, so every base would be shifted down one, and the entire gene would change. This would be completely devastating. This is why DNA repair mechanisms quickly target such errors.
On the other hand, Introns, which are not so sensitive or precisely executed, or are sometimes just junk or redundant, mutate based solely on random frequency. As there are 44 codons that don't correspond to an amino acid, these are used in introns. Therefore, the next axiom of evolution is that evolution is driven by the Introns. Obviously it is more complicated, Introns can become exons during shuffling/shifting, and exons can become Introns, and sometimes exons can be mutated harmlessly, so long as the mutation changes only a tiny chunk of the gene, but this rule still applies.

Now that you understand genetic mutation mechanisms, this can be applied to how advantage mutation works.
Intron mutation can change more than just transcription rate. It can change the protein fold. So, in all likelihood an organism won’t end up with one enzyme or protein morphing into another, but an identical polypeptide folding into a new enzyme. Only exon mutation will "change" an enzyme because it will change some codons, thereby changing the protein string order. From a probability standpoint, the odds of gaining a useful mutation because you can fold a protein in a new way vastly outweigh the possibility that you can get from producing a new protein. Mutations can have chain reactions on the cycle. Same string but different protein will produce a different catalytic function therefore will change another intron somewhere else down the line, or perhaps change an exon and make a new protein which, because it is bound to the cycle, not random, will be useful. If mutations operated independently, and outside the cycle, evolution would never get off the ground.

It can be understand like this:
A useless mutation occurs: Nothing happens
A bad mutation occurs: The cell dies, or the error is targeted because it is disrupting the cycle
A good mutation occurs: A new protein, rate of transcription or fold function is made. This is useful. It alters the cycle, producing a knock on effect.

For a mutation to occur which can be preserved, junk must be turned into non-junk. It is really easy to play with the introns. The prokaryotes that are the basis of life have almost no junk DNA. It is evident that such small organisms evolved to have conservative genomes. They have useful introns. It may seem extremely unreasonable in terms of probability but DNA mutates all the time. If the shift is Duplicate error, a popular method, then the gene advantage can be conserved, because it is a redundant piece. Evolution is just mathematics. As long as a gene exists, it will fight to survive...at the chemical level there exists a ruthless primal battle in which the best of the best are constantly being selected, and the weak crushed. The only phenotype affecting genes that are conserved are the ones that affect reproductive capacity. That will cause it to be conserved and cumulatively mutated upon. This is the mathematics of evolution.
Genetic drift drives evolution. Some mutations are good, some are bad, most do nothing, but through the endless cycles, organisms evolve. The analogy I like to use is the telemarketer. About 90% of people hang up on them, but the 10% who say yes make the enterprise quite profitable.

The statement advantage mutation is impossible is a confusion of possibility and probability. Advantage mutation almost never happens…the operative word being ALMOST. But if you have mutations working at quantum speed and three billion years on your hand, your odds improve dramatically.

The knock-on effect is a good demonstrator. All enzymes do only one thing, they act as a catalyst for the body's catabolic chemical reactions. Without proteins, you would have to set yourself on fire to release enough energy to perform respiration. This is obviously not practical. All proteins lower the activation energy for a chemical reaction by providing an active site which works like a lock and key model. The chemical fits into the protein receptor and is broken into smaller molecules. Therefore, one can imagine that a different fold will mean that protein will have a different catabolic function which could offer a significant advantage if it allows an organism to synthesize a new chemical. The most effective way to do this would probably be base-pair swap exon mutation, which will only change a small chunk of an exon. Normally, the amino confirmation will predispose a protein to fold in a certain way, although this process is not understood (that would be the Levinthal Paradox). Natural selection, it seems, has selected a chemical interaction set which encourages the protein to fold, because in it's primary and secondary state, it is useless.
Protein folding is also a useful demonstrator of life's autoregulatory weirdness. They fold into elegant shapes after being translated from mRNA only for a tiny piece of it to serve as an active site. The hemoglobin molecule is the bizarre case and point. It is a colossal macromolecular protein snugly wrapping a single haemite (iron). This is somewhat akin to building a nuclear powered transformer to plug in a lamp.

There are 100 nucleic acids and 300 amino acids that exist in nature, we use only 4 and 22. The sugars and phosphates snap together to form the base backbone in the exact same way that nucleic acids bond together. From a chemical standpoint, the phosphorylate-saccharide (ribose)-nucleic acid structure is sensible. There are 100 nucleic acids and 300 amino acids that exist in nature, we use only 4 and 22. There is no reason why life could not be based on other amino acids and nucleic acids. The sugars and phosphates snap together to form the base backbone in the exact same way that nucleic acids bond together. From a chemical standpoint, the phosphorylate-saccharide (ribose)-nucleic acid structure is sensible.

We can look at the knock-on effect with respect to folding like this:
1) A small mutation changes a few codons
2) A different protein is made with a new fold
3) This catalyzes a chemical in a different fashion, most likely a new product
4) This new product has a different effect on the cell membrane receptors, which keep up the autocatalytic cycle. It causes a different command to be followed, as transcription is driven when a stimuli causes a protein to bind to the introns that flank the necessary exon.
Transgenic technology has revealed that changing a gene can start making a gene down the line do bizarre things. Why? Simple. Genes can control each other. The knock-on is established by introns controlling exons which in turn produce proteins which control introns which control exons which… you understand. If evolution operated like individual genes doing individual things, it would not get on the ground.
Knock-on effects work all across the genome. After all, what do genes do, they produce proteins, or they regulate the production of proteins. What do those proteins do? Well...everything: The big functions are of course:

-Catabolism of biochemical families (nucleotides, coenzyme factors, carbohydrates)

-Anabolism (glycogen synthesis, lipid synthesis)

-RNA synthesis control

-Ion channels and membranes (cell membranes, nerve membranes, particularly oligolipoproteins for myelin) , transport mechanisms
including inorganic transport, ion flux and carrying

-Exocrine systems and secretory pathways/chemical production

-endocrine systems and hormone control Autocatalysis

-Maintenance of cell signal transduction and energy release metabolic pathways

The thing to notice about all of these is they are all dependant on biochemical triggers. You change one thing, you change a cascade. Making a new ion channel will change the electrochemical gradient or allow a different material influx, which will affect how protein receptors bind to introns. A new ion channel could trigger a hitherto unused intron. There are so many complex factors to genetic evolution, it is not a clear cut process.

The discovery of genes was probably one of the most important in the history of science. Before genomic sequencing, the human body or indeed any organism or indeed a single celled organism seemed unbearably complex. Of course, with the advent of new molecular biology techniques that was swept away. Everything can be explained in terms of metabolic pathways building macromolecules with remarkable properties. There are only thirteen families of Biochemicals (Terpenoids, Flavanoids, Carotenoids, Polyketides, Alkaloids Peptides, Polypeptides, Amino Acids, Nucleic Acids, Steroids, Enzyme Cofactors, Carbohydrates, Lipids and Tetrapyrroles). Everything can be explained in terms of these, and the manufacture, regulation, secretion and synthesis of these…can be explained by DNA. This explains everything from simple sugar metabolism all the way to the Progenitor…the stem cell with the potential to make a human body.

Then you talk about Irreducibility. I can destroy that with ease.

Irreducible Complexity is common, popular and fallacious. It was first put forth by Michael Behe and states that whereas in complex biosystems, if any single mechanism in a body function is removed, it fails to work. Thus it needs a designer. A laughable error. Every biomechanism can be broken down into simple components. We can track the evolution of an eye from simple patches of light emitting cells. Creationists like to use eyes or wings, but half a wing works fine, and might save your life if you fall out of a tree, likewise 51% of a wing will save your life from a fall from a slightly higher tree. We can see examples in nature of parachuting and gliding animals that are clearly partially and very slowly forming the systems that Behe deems Irreducible. We have fossils of birds which appear to have, half a wing or 60% of a wing. Half an eye (and there are organisms which do have half an eye) is better than no eye, and 51% of an eye might allow you to see a predator that half an eye would not. And this is how evolution works. The gradient of advantage accumulates until the “scaffolding” is no longer needed and a plethora of more advanced functions can spawn.
The organism that Behe likes to use is the bacterial flagellar motor mechanism. This device is remarkable in nature in that it is the only example outside human technology of a freely rotating axel as a means of propulsion. (Wheels on large animals really would be irreducibly complex and I suspect this is why they do not have them) It is powered by a tiny molecular motor. According to Behe, if any part were removed, the motor would stop working. Not only is this not irreducibly complex as each function works fine on its own, but we can track it back to simpler versions of it and see how it mutated. The axel bears clear resemblance to a simple mechanism used by bacteria to pump toxins into their hosts called a Type Three Secratory System (TTSS), and we can track that from simple proton pumps and ion channels.

Complex Systems do not evolve independently. You don’t see an eye in the primordial soup. A collection of simple systems accumulates more functions as these become advantageous. Darwin said in the Origin of Species: “Were it that a system could genuinely not function without the removal a mechanism, my theory would collapse completely”. So far, it holds.
There are three problems with irreducible complexity
1) Every biological function right down the level of RNA and viruses/ is self sufficient
2) Every complex system can be traced to a simple system, from photoreceptors to eyes, from ion channels to Secretion systems to flagellates and molecular motors
3) Complex systems evolve in mutual support of each other. An eye is useless without a patch of neurons to interpret it.

I can take apart one of your examples of IC immediately. I understand the Behe and the like love blood clotting:

It might be best to step back and first determine how the metabolic pathways to blood clotting work. It is a complex process indeed. At the heart of blood clotting is a substance in your blood called fibrin. Fibrin is a sticky molecule soluble in water which has the natural tendancy to form a clot. The mesh which it forms stops haemopoitic cells from escaping. Fibrin forms about 3% of the blood. However, it obviously cannot exist normally as fibrin, or it would simply block up the vessels, hence when in the blood, fibrin exists as part of a larger molecule called fibrinogen. Fibrinogen is a complex, amino-acid rich macromolecular complex, which at it’s center contains the fibrin molecule. Surrounding it are many amino acid side chains, which have a negative charge (at the pH of blood, amines and side chains always have a charge). This causes them to repel each other, thus they exist as independent molecules in the blood, without clotting.

This changes when a wound initiates the metabolic pathways known as the blood clotting cascade. A protease enzyme has to catalyze the removal of the side chains, thus exposing the fibrin. This enzyme is called thrombin. But obviously thrombin has to exist as an inactive enzyme otherwise it would simply initiate the reaction whenever. It exists as protothrombin, and has to be activated to become the catalysis enzyme. A tiny additional chain on the protothrombin fold renders it inactive. This has to be removed by another clotting serine factor, Factor X. This too, as a serine, must be activated in the same manner. And so, the blood clotting cascade has four steps more until we reach the beginning. Factor X is activated by Factor XI, which is activated by Factor IX, which is activated by Factor XII, Which is activated by the Kininogen-Kallikrein system of co-activation, which is triggered by external stimuli. This is where the process starts.

 

The activation of the serine cofactors is a similar process. For XI to become XIa (Activated Factor 11), a side chain must be cut removing the ionic charge, which allows it to cascade into the next step. It seems unnecessary complex, almost like an infinite regress of serine-cofactor activation steps. But it makes sense, because for every step that is taken, an exponential signal transduction increase occurs. If it was just a very short pathway, say a single cofactor triggered by external stimuli to start the thrombin conversion, then the clot would be far too small, and would take hours to form. Thus, the six-step amplification works best.

 

In others words, blood coagulation is a complex and beautiful process. But does that mean it is irreducible and could not have evolved? One of the key establishment requisites of Behe’s irreducible complexity is that a mechanism could not evolve by gradual evolutionary steps. But I beg to differ. The implication that he made clear in Darwin’s Black Box was that the designer would have to put all the parts together at once, otherwise it would not really be irreducible or a challenge to evolution. But unfortunately, genetic analysis of the cofactor cascade tells us otherwise. Thus we return to my previous comment about the homologous nature of the cascade.

 

So how could this function have evolved, and how can we trace it? Typically, when we start looking at a biomolecular function, we have a base from which to start. We never start from scratch. Only primordial chemists deal in that. This base function might be exteremly primitive, almost bound by basic laws of chemistry. For instance, when we look at the eye in all it’s glory, we see that all nine divergences that have taken their course come from a highly simplified patch of light-sensitive cells. Likewise, when we observe the fantastic complexity and variation of the Eukaroytic cell membranes, with all their complex ion channels and protein transport functions, we see that in common they are all bound a very simple chemical law known as ampipathism, the tendency of hydrophilic/phobic molecules to align in a bilayer. The membrane’s composition resembles a flagellum in molecular shape, with a long twin hydrophobic fatty acid tail and a stubby hydrophilic choline-phosphate-glycerol head.

 

What similar base function might we find in blood clotting? Studying the evolution of metabolic pathways is different to studying other molecular functions. The job is made significantly easier by the Autocatalytic nature of the pathways as described in my previous link. Much of the steps in coagulation work like that too. The serine proteases that form the original primitive life forms (as being detected on the long arms of chromosomes 1 and 5) were not originally designed for blood clotting, but they were there. In his book Finding Darwin’s God, Ken Miller suggests that cAMP (that’s cyclic adenosine monophosphate) would be a significant launch pad to build up the homologous set of serine cofactors that make the cascade. He’s correct here. cAMP is cellular transduction molecule that acts somewhat like a neurotransmitter, smoothing muscular tissue around vascular epithelial tissue, and inhibiting blood flow. A damaged cell, spilling all of it’s contents, would pour the cAMP out along with it. Evolution could work with that. Cellular mechanisms already possess, for unrelated reasons, white blood cells, whose adhesive nature allowed them to clump the wound

 

From the rudimentary system, where several factors are in place and a simple automatic system of clumping exists, a highly complex multilayered system of cascading can accumulate by two well-known evolutionary processes. One is called duplicate error from which the various homologies are formed, and the other is exon shuffling as done by spliceosomes. From the receptors point of view, we could see how the repeated duplication and slight mutation of the serine cofactors would work, for reasons not the least of which that we can track it’s paralogies. For the most part, coagulation is autocatalytic, it just needs the materials to initiate. If the progenitors are already in place, then well…all that is needed is time for the duplicative errors to occur. If we have primordial serine cofactors (we do), the rudimentary single layer is pre-existing (ie, primordial enzyme A is cleaved to make Aa, which actives the thrombin). This would initiate itself. And we can imagine the naturally selective benefits that would come from the repeated duplication of the serine, as this would make clotting more efficient.

It is in no way Irreducible. You can be sure that we would notice it in the genome if it was (as it turns out, they are strewn all over the genomes across the strata, XII is in Chromosome 5, VII is on 13, Factor VIII is on the sex chromosome etc)

Blood clotting is an example of a zymogen cascade pathway, and any metabolism generated by zymogenes can be generated by duplication and homology. This particular cascade is composed almost exclusively of serine proteases. Surely, serine protease zymogenous cascade is the worst example of "intelligent design", not because it is poor, but because the homology in this particular protein family is more obvious than any other family, kinase domains, homeodomains, Cro repressor dimers, you name it, this is the textbook example of a protein family in an obvious homology. This particular domain is so close in amino acid structure of the proteases that some of the serines are nearly indistinguishable without close scrutiny of the difference in signature sequences. (Sig sequences are tiny stretches of amino acids 10-30 amino acids long used to ID domain stretches that have diverged alot). Of course, the serines haven't exactly diverged alot. In fact, they are one of the most conserved families in the whole proteome. They are the nemesis of intelligent design, an obvious example of duplication and homology.

2. The high information content of DNA could only have come from intelligence.
Information science teaches that in all known cases, complex information requires an intelligent message sender. This is at the core of the Search for Extra-Terrestrial Intelligence (SETI). DNA is by far the most compact information storage/retrieval system known. A pinhead of DNA has a billion times more information capacity than a 4-gigabit hard drive. Ironically, evolutionists scan the heavens using massive radio telescopes hoping for relatively simple signal patterns that might have originated in outer space, all the while ignoring the incredibly complex evidence of superior intelligence built into every human’s DNA. While we’re waiting to hear signs of intelligence behind interstellar communication, we’re ignoring those built into us.

Do you know how the information in DNA works?

 

All life, from the humble protozoa to the strutting man, is based, without any known exception, on a linear chemical code, which holds in an ingenious fashion, all the instructions to create life in the complex forms we see around us. The composition of this chemical code is based on giant, unbranched polymers called DNA which hold the chemical instructions in a ladder-like formation. Namely, in two complementary strands which twist around each other to form an isomeric structure whose elegance is unmatched in nature. The rungs and strands of these ladder have a rigidly enforced chemical makeup which is what I shall detail now.

Each of the two strands of the ladder is made up of a string of molecules which snap together like chemical blocks. The composition of the molecule is sugar-phosphate. A phosphate is a simple, straight, branched molecule of interlinking oxygen and phosphorous. Attached to this phosphate is a radically different molecule, an aromatic sugar called deoxyribose. Traditionally, a sugar is defined as a molecule which follows the composition formula {CH2O}n. For this reason, it is also called a carbohydrate. All ring-structured sugars have a definite pattern. The inner ring is composed of a single oxygen and n Carbon atoms which are arranged in a circular, single-bonded pattern. Each carbon atom in the inner ring has attached to it one Hydrogen atom, and one Hydroxyl group (OH). All of the carbon atoms have this, that is, except one. Attached to one of the carbon atoms in every sugar is either a ketone or an aldehyde. Both of these are small, simple chemical groups which radically alter the sugar’s chemical property.

A ketone is very simple. It is a carbon with a double covalent bond to an oxygen. Because a carbon has a valency of four, there are two open spaces in this molecule for bonding, which is how it attaches to the ring of the sugar. An aldehyde is more or less the same, except it has a hydrogen attached to it, leaving only one free space. The sugar in DNA has an aldehyde.

The sugar in question in DNA, which is called deoxyribose, has all of these properties except one. Instead of it’s normal derivative sugar ribose, it is missing a hydroxyl group (specifically at the second carbon atom in the ring). This will become important later on.

The structure of the strands of DNA therefore, is a repeating polymer of a sugar ring linked to a phosphate linked to a sugar ring linked to a phosphate and so on. For purposes of keeping the integrity of the ladder, the other strand in the DNA molecule, called the complementary strand, has the sugar-phosphate aligned in the opposing direction.

And what of the rungs of the ladder? Well, that is quite special. It is the rungs of the ladder which hold the information, and it is the order of the rungs of the ladder which determine this information. Attached to each sugar-phosphate on both strands of the ladder is a molecule called a base. The language of DNA is made up of four bases. You may recognize their names. They are adenine, guanine, cytosine and thymine. Like sugars, all of the bases are ring structured. But they are a radically different class of molecule. Sugars are merely carbohydrates. But bases, in addition to hydrogen, carbon and oxygen they have one more element to their mix. Nitrogen.

There are many, many bases in nature, almost 100, but DNA uses only four. And within those four are two quite different classes of bases. The purines are heterocyclic, meaning that they are actually composed of two rings, not one. Many notable molecules are purines (like caffeine) and their importance extends beyond their part in DNA.

(Irrelevant but interesting side note. Methylation of some purine bases can produce free radical bases like hypoxanthine. These have a direct link to cancer and can damage healthy DNA)

Out of the four bases present in DNA, two of them are purines, adenine and guanine, which henceforth shall be referred to as A and G, and the other two referred to as C and T.

What of the others? They are a different class of base called pyrimidines. These are simpler than purines, and have a familiar single-ring structure. The pyrimidines are the class of molecule under which C and T fall.

What is the importance of the purine/pyrimidine relationship? DNA is based on a molecular relationship called complementation. Recall that DNA is made up of two strands. Each strand is made up of alternating sugar-phosphate, and the two strands face opposite directions (i.e one strand is sugar-phosphate-sugar-phosphate and the other strand in phosphate-sugar-phosphate-sugar).

Each sugar-phosphate has one base attached to it. This produces a special molecule which is called a nucleotide. What is the set of nucleotides above classed as? They are called Deoxyribonucleic acid, otherwise known as DNA.

Because the structure of DNA is held in complementation, each base has a pair. This is where the purine/pyrimidine relationship becomes important. You cannot force two North magnets together, and in the same way, the DNA code follows strict chemical rules. A will only fit with T, and C only with G.

In this way, we can start to see how the DNA ladder is formed. Each step is composed of not one rung, but two. Each side has half a rung attached to it, and the other half of the rung is determined by the pre-existing chemical composition. This is exactly how DNA replicates itself. The process is called templated polymerization. Imagine half a DNA molecule, which only has one strand. Swarming around this strand are many free nucleotides. They will automatically attach themselves to the bases on the pre-existing strand, and the complementary strand will start to take shape. If a single strand reads ATTCGGA then the complementary strand will read TAAGCCT. Although each strand keeps it’s chemical integrity through very strong covalent bonds, the two strands (who connect to each other via the bases or rungs) are held to each other by weak hydrogen bonds. This allows the two strands to peel apart and snap together with ease, which allows repeated polymerization and replication. In the lab, we can replicate this process through a technique called PCR or polymerase chain reaction.

This is the basic chemistry behind DNA, but leaves the more important question unanswered. How does this translate into the information needed to create life? How does the order of bases along a string translate into the information needed to build a cell?

DNA is a linear chemical code. It faithfully represents another class of information in a linear fashion. It has many uses which will be detailed, but any cellular biologist will immediately give you one answer: DNA holds the code to make protein.

Proteins are radically different to nucleotides. They are also composed of massive, unbranched polymers. The language of protein is composed of linked amino acid subunits. In all of life, there are 22 known amino acids and a protein is determined by the order of it’s amino acid string. This is how DNA represents proteins faithfully. The order in which DNA bases are aligned on a string is a direct representation of the order of amino acids on a protein. But how does a code of four chemicals represent an alphabet of 22?

The answer lies in the correct way DNA is read. One amino acid is represented by a specific order of three amino acids. This information structure, where DNA is grouped in triplets, is called a codon. As it is groups of three based on four possibilities, there are 64 codons and there are multiple codons which can correspond to a single amino acid. In fact, most amino acids can be represented by four codons. For instance, Serine can be read as TCT, TCA, TCG or TCC.

The definition of one gene is the length of DNA which represents one protein. A gene tends to be roughly 1,000 base pairs long, the size of the average protein. The process by which information from DNA is turned into protein is called transcription and translation. This process is very complex in its trigger mechanisms and enzymatic control. A simplified version will suffice. Recall that double-helixes can peel apart to expose the strands for replication. This is the foundation of protein synthesis. The DNA first needs to be translated into a slightly different language called RNA.

RNA is also based on sugar-phosphate and bases. It is nearly identical to DNA except for some critical differences. The sugar in the RNA backbone is standard Ribose, not deoxyribose (hence the acronym). This causes it to have a much weaker backbone than DNA. Also, one of the bases is replaced. RNA contains C, G, and A like DNA. But instead of thymine it contains another (very similar) base in it’s place- Uracil, denoted by the letter U. Isomerically, it is much less elegant than DNA. It is single stranded, not double, and because it’s backbone is much weaker, it tends to fold on itself. For instance, an AAAA section will associate with a UUUU section. Far from the beautiful twisting symmetry found in DNA, RNA is an odd, crooked molecule.

For DNA, nothing complex is required. A set of reactions that reads DNA is based on literally copying it. The key thing about DNA is that the nucleotides literally represent amino acids. One codon is identical to an amino acid. This is translation/transcription. I'll go through it step by step again.

1. A stimulus from the cell membrane causes proteins to bind to the introns flanking the necessary exon, this causes the string to unwind. This is initiated by transcriptase enzymes
2. Once unwound, the string splits
3. Through templated polymerization initiated by polymerase enzymes, free bases attach to the complementary string, producing the identical string (that which is precisely identical to the protein in question in terms of codon order), which is then tidied up using spliceosomes and ligases, enzymes that cut through the introns and glue the exons together to make the complete string.
4. The Free bases are RNA bases and attach to form the protein-identical RNA base. The reason for this is that a ribosome cannot read DNA, it must be converted into RNA. The only difference is that it has ribose instead of deoxyribose and uracil instead of thymine, but since nothing else can read thymine, that is an important difference. This string is called mRNA which is ejected from the nucleus.
5. tRNA strings which represent one amino acid bind to their corresponding amino acids on one end. On the other end they have an anticodon, which represents the base string identical to the amino acid.
6. The mRNA is captured by a ribosome, a giant macromolecular protein. The mRNA is lined up along it. The anticodon on the tRNA automatically binds to the codons on the mRNA. This forces all the amino acids to line up. They thread together automatically, which causes the now unnecessary tRNAs to detach and leave the ribosome. When the protein is finished, it is automatically detached.

 

The definition of one gene is the length of DNA which represents one protein. A gene tends to be roughly 1,000 base pairs long, the size of the average protein. The process by which information from DNA is turned into protein is called transcription and translation. This process is very complex in its trigger mechanisms and enzymatic control. A simplified version will suffice. Recall that double-helixes can peel apart to expose the strands for replication. This is the foundation of protein synthesis. The DNA first needs to be translated into a slightly different language called RNA.

RNA is also based on sugar-phosphate and bases. It is nearly identical to DNA except for some critical differences. The sugar in the RNA backbone is standard Ribose, not deoxyribose (hence the acronym). This causes it to have a much weaker backbone than DNA. Also, one of the bases is replaced. RNA contains C, G, and A like DNA. But instead of thymine it contains another (very similar) base in it’s place- Uracil, denoted by the letter U. Isomerically, it is much less elegant than DNA. It is single stranded, not double, and because it’s backbone is much weaker, it tends to fold on itself. For instance, an AAAA section will associate with a UUUU section. Far from the beautiful twisting symmetry found in DNA, RNA is an odd, crooked molecule.

Nonetheless, it is a critical medium to protein synthesis and a key material in macromolecular cellular structures. The cell’s protein synthesis mechanisms, which I will go into in more detail, cannot read the language of DNA. Therefore, it must be translated into a slightly different format which can be processed. This interface string of RNA, the medium between DNA and protein, is called mRNA, or messenger RNA. It is the template which serves to manufacture a protein.

When we look at a cell under a microscope, any cell that we wish to examine, it bears many different things. Strange swirling little organelles and beating cilia and loopy strands of DNA. They are very diverse, but there is one thing they all have, without any exceptions whatsoever. Under a microscope, it appears to be many tiny black granules, little spherical studdings that are strewn all over the cytoplasm.

However, using electron microscopy and X-Ray crystallography, we can see that these little black balls, are first of all, not black (false colour imaging) and second of all, they are not little balls, they are colossal macromolecular structures, extremely complex and interwoven, beautiful little machines. Under a Scanning Electron Micrograph, the power of the “little black balls” becomes humbling. These little devices are called ribosomes. They are composed 75% of twisting strands of protein, and 25% of a form of RNA called rRNA or ribosomal RNA. This RNA is not coding RNA, it holds no genetic information in it’s molecules, rather it is structural, the scaffolding for a miraculous little device.

The ribosome is a protein synthesizing complex, trundling along in the fluid medium of the cell, and capturing the raw materials and information to make the protein and then, remarkably, stitching together a fully functional protein based on these ingredients.

The raw materials are already in the cell, they are amino acids. The information to synthesize the amino acids is also in the cell, in the form of the mRNA strand (which is ejected from the nucleus). Yet the ribosome does not just scoop up amino acids wherever it finds them. They are brought into the ribosome, and arranged in the correct order on the mRNA by another class of RNA molecule called transfer RNA or tRNA.

Amino acids cannot be synthesized off the mRNA template alone. The languages are too different. There has to be a third medium to read the information. This is where the tRNA comes in. It has the capability to read both sets. tRNAs are special molecules. They are also composed of RNA, yet on one end of them they have a binding site which is unique to each amino acid. Due to the triplet nature of the reading of DNA, multiple types of tRNA molecule can correspond to a single amino acid.

The other end of the tRNA has three base pairs, which will correspond to the amino acid to which it binds. However, this relationship is special. For the triplet on the tRNA does not correspond to the amino acid with the parallel relationship the acid will share with mRNA. Rather, the triplet is the precise mirror image of the amino acid codon. For this reason, it is called an anticodon. This concept is relatively easy to grasp. If an amino acid is represented by AGG on the mRNA string, the tRNA to which it binds will have UCC tagged to it.

From here it is easy to see how the process unfolds. The ribosome is unbearably complex, a colossal protein/ RNA complex which is the subject of countless research papers. It is divided into domains based on the subunits which compose it, and the genetic control switches which produce the rRNA and protein to make and assemble it, as well as control of the anabolic processes which synthesize it from macromolecules, could not possibly be described in this very short introduction. For now, suffice it to say that the ribosome is arranged in two large domains with slots to hold the molecules in place. As it moves through the cell, it captures the free-floating information in the form of the mRNA and the tRNAs now bound to specific amino acids. In the smaller of the two domains, the mRNA strand is threaded through a slot-like mechanism similar to a conveyer belt. In the larger domain, there are accommodating slits which house the tRNAs.

This is where the factory process unfolds. The tRNA anticodon can recognize its counterpart codon on the mRNA string, and thus they will line up in order automatically (note: To prevent tRNA insertion into the wrong place, and to ensure they line up strictly in order, there is a complex cascade of enzymatic control barriers and mechanisms whose details need not be mentioned here).

Once the tRNAs are lined up in the correct order as dictated by the information held by the messenger string, the amino acids atop the tRNA are now in the correct order, which was the desired state of affairs to begin with. They are stitched together inside the ribosome. Once two amino acids have been stitched together, the tRNAs holding it are no longer needed, and they are enzymatically broken from their acid, and ejected from the ribosome. One by one, the tRNAs stream out of the ribosome until the protein is finished.

At this point, the work of the original gene which contained the information to make the product is finished. However, the processes which I shall detail next are, like every other process, controlled by genes. There is no function in the whole of biology which does not have genetic control mechanisms.

The protein is now correctly assembled, at very least in terms of having the correct order of amino acids. However, the actual product is far from complete. It is only in what we call the primary structure. In terms of chemical composition it is completely correct, but in terms of isometrics and structure, it is little more than a string of chemical compounds.

The true magic begins almost immediately after the protein is synthesized. It begins to twist…

A protein is not subdivided merely by it’s amino acid. It is grouped into large subunits called polypeptides, regional stretches of protein subunit roughly 100 amino acids long. In this way we can see that massive proteins (>1000 amino acids) are not only defined by their individual, but ultimately, the order of different units created by smaller strings of amino acids within the complex. The protein transforms into it’s secondary structure by folding at the kinks between the subunits. The shape, therefore, of a protein is directly determined by it’s chemical sequence. The folding becomes further intricate during progression to tertiary structure when the folds between individual units take shape. Finally, the protein reaches it’s quaternary structure or it’s native state, with the intricate system of folds.

 

 

3. No mutation that increases genetic information has ever been discovered.
Mutations which increase genetic information would be the raw material necessary for evolution. To get from “amoeba” to “man” would require a massive net increase in information. There are many examples of supposed evolution given by proponents. Variation within a species (finch beak, for example), bacteria which acquire antibiotic resistance, people born with an extra chromosome, etc. However, none of the examples demonstrate the development of new information. Instead, they demonstrate either preprogrammed variation, multiple copies of existing information, or even loss of information (natural selection and adaptation involve loss of information). The total lack of any such evidence refutes evolutionary theory.

That is ridiculous.

New information is gained by a mutatory mechanism that satisfies two requisites at once. The size of the genome in terms of bases grows, and the diversity of the genome grows. A special mutation known as duplicate error, where a spliceosome makes a mistake, and during mitosis a duplication ends up with the progenitor cell retaining an extra part of the genome. This new part is redundant, and thus free to mutate based on random frequency. This mechanism is critical to evolution, and produces two genetic flows without which evolution would not be possible. These are paralogs and orthologs. Across the vast diversity of life, the majority of genes share a near-identical similarity to another, with a very similiar job. These are grouped together in large gene families. All the gene families have a lineage that stretches back four billion years.

On this subject, in an article not displayed here, this is what I wrote:

DNA genomes are extremely redundant. 91% of the human genome is redundant, if you are interested. So changing one copy will add new information. Because most of the time the polymerization works out fine. Imagine it like a library. There is only one copy of each book. You remove one book and replace it with a different, new book. Are you adding information? No. You are changing information. This is the crux of the creationist argument. But imagine you have twelve copies of each book. You replace one copy of one book with a different, new book. Now you are adding new information because the pre-existing information is still there in the form of 11 other books.

Evolution is dependent on homologous sets of genes called orthologs and paralogs. Genes in multiple organisms that obviously descended from the same common ancestor (anyone who bothers should check the amino acid tracking branching tree of hemoglobin evolution as an example) are called orthologs, while genes which occurred as the result of mutation descended from a single gene (thereby producing two or more new genes) are called paralogs. Both of these are called homologs.

I also wrote some more on DNA origin here:

Protein assemblage too, is not chance. We would not assume that favorable formations of protein assemblage whereby the natural quaternery state would arise is affixed the same probability as a useless denatured amino acid string. That is ridiculous, and has been debunked by the Miller-Urey experiment. Insofar as the nucleic acids and proteins of cellular mechanisms are primary life (ie they are capable of self-assembly), they undergo their own natural selection. This was demonstrated as far back as 1936 when Alexander Oparin showed that in an anoxic atmosphere, organic molecular structures of the basic primary state would combine to construct elaborate complex macromolecular giants which themselves were capable of reassembly.

After all, what makes a protein successful? A protein is just a catalyst, whose amino acid configuration allows it to fold up in a quaternery state where it serves as multiple active sites. Only polypeptides with certain strings of amino acids acheive this state. But, as the macromolecular covalescence occurs, might protein undergo it's own natural selection? Where proteins that "work" would survive in place of the denaturing ones?

And then in 1961, Joan Oro, A spanish biochemist, cracked the adenine conjecture when he showed that the prebiotic nucleotide can assemble from hydrogen cyanide. Upon examination of comet traces, he concluded that comet fragments could have easily brought organic molecules to Earth. This in effect would merge Abiogenesis with panspermia except without the space aliens nonsense. His research paved the way for several more experiments, where the prebiotic synthesis of the other bases, thymine, guanine and cytosine, were demonstrated.

4. Evolution flies directly in the face of entropy, the second law of thermodynamics.
This law of physics states that all systems, whether open or closed, have a tendency to disorder (or “the least energetic state”). There are some special cases where local order can increase, but this is at the expense of greater disorder elsewhere. Raw energy cannot generate the complex systems in living things, or the information required to build them. Undirected energy just speeds up destruction. Yet, evolution is a building-up process, suggesting that things tend to become more complex and advanced over time. This is directly opposed to the law of entropy.

You know nothing of entropy do you?

I'm not your science teacher, but Ill explain entropy for you:

 

This is a lengthy explanation of the entropy laws, and how they relate to life. I understand that many people have been using the Second Law of Thermodynamics as if it were a challenge to evolution. You can imagine how amusing I find this.

At any rate, we need to understand some basic concepts first. These are The laws of thermodynamics, entropy, enthalpy and free energy.

Let us imagine a box, a system closed off from the universe, with a cell inside it. The cell in a box is a closed system with a fixed amount of free energy. This system will have a total amount of Energy denoted E. Let us suppose the reaction A to B occurs in the box and releases a great deal of chemical bond energy as heat. This energy will increase the rate of molecular motions (transitional, vibrational and rotational) in the system. In other words it will raise the temperature.

However, the energy for these motions will soon transfer out of the system as the molecular motions heat up the wall of the box and then the outside world, which is denoted sea. Eventually, the cell in a box system returns to it’s initial temperature, and all the chemical bond energy released has been transferred to the surroundings. According to the first law of thermodynamics, the change in energy in the box (denoted ∆Ebox or just ∆E) must be equal and opposite to the amount of heat energy transferred out, denoted as h. Therefore ∆E=-h.

E in the box can also change during a reaction due to work done in the outside world. Suppose there is a small volume increase in the box (∆V) which must decrease the energy in the box (∆E) by the same amount. In most reactions, chemical bond energy is converted to work and heat. Enthalpy(H) is a composite function of work and heat, (H=E+PV). Technically it is the Enthalpy change (∆H) is equal to the heat transferred to the outside world during a reaction.

Reactions with a -∆H are exothermic, and ones with +∆H are endothermic. Therefore –h=∆H. The volume change in reactions is so negligible that this is a good approximation.

-h≈∆H≈∆E

The Second Law of Thermodynamics allows us to predict the course of a reaction. We need a quantitative unit to measure this, and to measure the degree of disorder or probability for a given state (recall the coins in a box analogy). This function is entropy (denoted S) The change in entropy that occurs when the reaction A to B converts one mole A to one mole B is

∆S= R log PB/PA

PA and PB are probabilities of states A and B. R is the gas constant (2 cal/deg^-1/mole-¹⁾ ∆S is measured in entropy units (eu).

In the example with a box containing one thousand coins all facing heads, the initials state (all coins facing heads) probability is 1. The state probability after the box is shaken vigorously is about 10^298. Therefore, the entropy change when the box is shaken is R log 10^298 is about 1370eu per mole of each container (6.02x10^23 containers). ∆S is positive in this example. It is reactions with a large positive ∆S which are favorable and occur spontaneously. We say these reactions increase the entropy in the universe.

Heat energy causes random molecular commotion, the transfer of heat from the cell in a box to the outside increases the number of arrangements the molecules could have, therefore increasing the entropy (analogous to the 1000 coins a box).The release of X amount of heat energy has a greater disordering effect at low temp. than at high temp. therefore the value of ∆S for the surroundings of the cell in a box denoted ∆Ssea is equal to the amount of heat transferred divided by absolute temperature or

∆Ssea =h/T

We must now look at a critical concept: Gibbs Free Energy (G)

When observing enclosed bio-systems, we need to know whether or not a given reaction can occur spontaneously. The question regarding this is whether the ∆S for the universe is positive or negative for the reaction, as already discussed.

In the cell in a box system there are two separate components to the entropy change in the universe. The ∆S for the inside of the box and the ∆S for the surrounding sea. These must be added together.

For example, it is possible for an endothermic reaction to absorb heat therefore decreasing the entropy of the universe (-∆Ssea) but at the same time cause such a large disorder in the box (+∆Sbox) that the total ∆S is greater than zero. Note that ∆Suniverse=∆Ssea+∆Sbox. 13

For every reaction, ∆Suniverse must be >0. We have just encountered another way to restate the Second Law of Thermodynamics

In this case, the reaction can spontaneously occur even though the sea gives heat to the box during the reaction. An example of this is a beaker of water (the box) in which sodium chloride is dissolving. This is spontaneous even though the temp of the water drops as it is occurring.

The most useful composite function is Gibbs Free Energy (G) which allows one to deduce ∆S in the universe due to the reaction in the box. The formula is: G=H-TS.

For a box of volume V, H is the Enthalpy (E+PV), T is the absolute temperature and S is the entropy. All of these apply to the inside of the box only. The change in free energy in the box during a reaction is given as the ∆G of the products minus the ∆G of the reactants. It is a direct measure of the disorder created in the universe when a reaction occurs. At a constant temp, ∆G= ∆H+T∆S. ∆H is the same as –h, the heat absorbed from the sea. Therefore

-∆G= -∆H +T∆S or -∆G=h+T∆S Therefore -∆G/T=h/t+∆S

h/T still equals ∆Ssea but the ∆S in the above equation is for the box. Therefore.

-∆G= ∆Ssea +∆Sbox =∆Suniverse

A reaction will spontaneously proceed in the direction where ∆G<0, because it means that the ∆S will be >0. They are inverse functions of each other. For a complex set of coupled reactions involving many molecules, one can calculate ∆G by adding the ∆G of all the different types of molecules involved before the reaction, and comparing that to the ∆G of all the molecules produced by the end of the reaction. For example, comparing the ∆G of the passage of a single proton through the inner mitochondrial membrane across the electrochemical proton gradient to the ∆G for ATP hydrolysis, we can conclude that ATP synthase requires the passage of more than one proton for each molecule of ATP synthesized.

Does your brain hurt? Good! Let’s review:

2^nd Law: Basically an expression dictating that the whole universe progresses towards disorder, and any reaction must contribute to that disorder. Disorder is energetically favorable and probability-wise favorable.

Heat Energy: The energy in the random motion and hubbub of molecular jostling and movement. This is basically a measure of temperature, but all reactions give off heat energy, which is irretrievable (another way to restate the second law). Heat energy is denoted h.

Enthalpy: A composite function of heat and work, but since ∆V is always next to nothing, we can regard it as the inverse of heat. Enthalpy is a measure of heat energy lost or ∆H=-h

Gibbs Free Energ

The total ∆G for a reaction measures how far from equilibrium the reaction is. The large negative ∆G for ATP hydrolysis means that the cell keeps it very far from equilibrium. Equilibrium is reached when the forward and backward rates of each reaction are precisely equal and the ∆G is zero. For ATP hydrolysis, this occurs when the vast majority of ATP has been hydrolyzed (because ATP hydrolysis is much more favorable than ATP synthesis), like in a dead cell.

What we can conclude is that every reaction must have a negative ∆G to occur.

In a closed system, which, by definition, does not exchange energy input or output with the rest of the universe, the total amount of energy inside the system is constant, and expressed by the function E. In biology, states of high order have low probability. For instance, if we imagine a box with 1000 coins lying heads up, and we shake it twice, it is vastly more probable that we will end up with a chaotic arrangement of coins than the arrangement that we had previously. Thus, the law can be restated closed systems tend to progress from states of low probability to high probability. This movement towards high probability in a system where the energy is E, is progressive. In order for the entropy (the progression towards high probability) to be corrected, there must be periodic bursts of energy input, which would break the closed nature of the system. In this case, it would require someone to open the box and rearrange the coins.

When this happens, a great deal of energy is expended. What makes entropy problematic for a closed system is that useful forms of energy always progress to useless forms (another way to restate it), by which they are converted into random, chaotic thermal motions. Eventually, the universe will undergo this process when it expends it's useful energy. Such a process is called Heat Death. It will be a very very very long time before this happens (and we'll have long since gone to another universe anyway).

Therefore, for a living organism to maintain order and increase order, there must be a useful energy input. For that to happen, there will be a useless energy output. Thus increasing the order in the cell will increase the disorder of the entire universe. In this way, we can imagine life forms and other complexities as islands of order in a universe progressing towards disorder. For this to happen, there must be a colossal influx of free energy all the time. This is one the requisites for life. As luck would have it, we have such a system: The sun.

This explains another nonsensical hurdle set by the creationist cohorts (does anyone notice how they set absurd standards of proof for evolution, but have absolutely nothing to back themselves up?): Namely, the supposedly irreducible nature of metabolic pathways. One might be deluded into thinking, by their nonsense, that the enzymatic reactions evolved in such a manner. Not so. The enzymes can only speed up thermodynamically possible reactions. The cells must maintain order by maintaining a constant stream of biochemical catabolism and anabolism being driven by enzymes which lower the activation energy. Food is broken down from macromolecular giant biological polymers like polysaccharides, polypeptides, proteins and giant fatty acids by oxidation, electron carrying, and catalysis of favorable reactions into simple molecules like glucose, amino acids and glycerol. Some of this is in turn, catabolized to break the phosphate bonds which release heat energy to power the cell (and increase entropy in the universe). The rest of it is used to be anabolized again into giant structures in glycogen or lipid storage for later consumption or construction into cellular structures like ribosomes. All of these highly intricate metabolic pathways that do these things must be set in motion by thermodynamically favorable events.

For instance, imagine rocks falling off a cliff onto the ground. The kinetic energy is being converted into heat and sound. This is useless. But if we set up a turbine underneath the rock which powers a small hydraulic pump, we are obtaining useful work from free energy.

This is known as a coupled reaction. An energetically favorable reaction must drive the many unfavorable reactions that cannot start by themselves. Coupled reactions are useful in terms of synthesis because the free energy change is zero. Typically, the unfavorable reaction involves the synthesis of carrier molecules the NADH or ATP or FADH etc.

Free energy is denoted by Schroedinger and Gibb's constant G.

If a reaction is favorable, for instance, converting X into Y, then the universe becomes more disordered as the cell becomes more ordered. The rule is that all catabolism is favorable and all anabolism is unfavorable. Thus reactions like glycolosis and ATP Hydrolosis must maintain reactions like glycosynthesis and ribosomal assembly. If it is unfavorable, converting Y back into X, then the order in the universe will increase, and in the cell, the order will decrease.

The axiom states that anabolism of positive G must be linked to a catabolic reaction of negative G of much larger value in order to drive the reaction. Thus all metabolic pathways have a sum entropy which always ends up as a negative -dG. We call this negentropy. (The d in front of G represents delta or change of.

But how? What about anabolism, free energy creation, energy stores? Many reactions in cells are energetically unfavorable. Most polymerizations are, oxaloacete generation, ADP condensation etc as well as supramolecular operation like ribosomal assembly, mitosis, mRNA synthesis etc

 

These seemingly impossible reactions make use of a key concept covered earlier. Let us return to our cell in the sea scenario. Except the cell is not in the box, it is in the sea, receiving free energy from the sun.

 

Recall: ∆Ssea +∆Sbox =∆Suniverse

 

Except now it becomes: ∆Ssea +∆Scell =∆Suniverse

 

For an unfavorable reaction to occur, it must be coupled to a favorable reaction of higher magnitude. IN this way, even the order in the cell increases, the disorder in the sea increases by a greater amount therefore the ∆S is still positive and the ∆G is still negative, leaving the laws of thermodynamics intact.

 

There are a vast number of examples to choose from. Let us consider a typical unfavorable condensation reaction

 

A-H+ B-OH = A-B + H20

 

This reaction will not occur spontaneously. It cannot. It will create free energy of its own accord. That’s impossible. Fortunately there is a mechanism to bypass this.

 

A favorable reaction is coupled to it. ATP Hydrolysis is a favorable and readily occurring reaction where ATP splits one phosphanhydride to ADP, leaving a very reactive inorganic phosphate. This bond, because it is highly reactive, readily bonds with B-OH forming B-O-PO3.

 

This is called a high-energy intermediate. Because the bond is so high-energy, it will immediately react with B-H producing A-B + H2O + Pi + ADP

 

This concept exists in a huge number of reactions. Many reactions involve critical stepwise passing of high energy intermediate chains.

 

The cells must maintain order by maintaining a constant stream of biochemical catabolism and anabolism being driven by enzymes which lower the activation energy. Food is broken down from macromolecular giant biological polymers like polysaccharides, polypeptides, proteins and giant fatty acids by oxidation, electron carrying, and catalysis of favorable reactions into simple molecules like glucose, amino acids and glycerol. Some of this is in turn, catabolized to break the phosphate bonds which release heat energy to power the cell (and increase entropy in the universe). The rest of it is used to be anabolized again into giant structures in glycogen or lipid storage for later consumption or construction into cellular structures like ribosomes. All of these highly intricate metabolic pathways that do these things must be set in motion by thermodynamically favorable events.

For instance, imagine rocks falling off a cliff onto the ground. The kinetic energy is being converted into heat and sound. This is useless. But if we set up a turbine underneath the rock which powers a small hydraulic pump, we are obtaining useful work from free energy.

 

7. The dating methods that evolutionists rely upon to assign millions and billions of years to rocks are very inconsistent and based on unproven (and questionable) assumptions.
Dating methods that use radioactive decay to determine age assume that radioactive decay rates have always been constant. Yet, research has shown that decay rates can change according to the chemical environment of the material being tested. In fact, decay rates have been increased in the laboratory by a factor of a billion. All such dating methods also assume a closed system—that no isotopes were gained or lost by the rock since it formed. It’s common knowledge that hydrothermal waters, at temperatures of only a few hundred degrees Centigrade, can create an open system where chemicals move easily from one rock system to another. In fact, this process is one of the excuses used by evolutionists to reject dates that don’t fit their expectations. What’s not commonly known is that the majority of dates are not even consistent for the same rock. Furthermore, 20th century lava flows often register dates in the millions to billions of years. There are many different ways of dating the earth, and many of them point to an earth much too young for evolution to have had a chance. All age-dating methods rely on unprovable assumptions.

Again, not your science teacher. But do you want to know how readiometry works?

Large atoms with concentrated, crowded nuclei are highly unstable. To correct the instability, they will either
a) Release a highly ionizing but low energy particle consisting of a helium nucleus with two protons and neutrons. This is called alpha radiation.
b) If the nucleon number is isotopically unstable, the atom will change a proton into a neutron or vice versa allowing an electron to be released or a positron depending on beta minus versus positive.

Another thing they can do is released an ultra-high energy wave called gamma which is irrelevant to my question below.

For instance, a carbon-14 isotope. 99.999% of all carbon is stable carbon-12. but carbon-14 isotopes are not stable and make up 1ppt (part per trillion) of all carbon. They release beta radiation to correct the nucleon instability by firing off an electron. This causes it to decay into Nitrogen-14. The great thing about radioactive decay is that it is a random process that obeys probability laws. The other good thing about it is that you can dip a radioactive material in molten lead, in acid, shoot it, burn it, fire particles at it, try to irradiate it again, pass a current through it...and none of these things will change the isotope clocks. They are fixed.

Now let me explain how we use this to measure the age of the Earth and organic material. Radioactive half-life is the amount of time it takes for the Geiger counter count rate (CPS) to fall by half. Radioactivity is a Zeno's paradox, because it falls to 1/2 then 1/4 then 1/8, but never to 0. It takes the same amount of time to fall from full to half as from half to quarter because the probability remains the same, because radioactive decay is an elemental nuclear cycle.

Depending on their isotopic properties, different isotopes and elements decay at different rates. Uranium 238 has a half life of 4500 million years...almost exactly the age of the Earth. Certain Thorium isotopes, and Polonium 221 for example, half in hours to seconds.
All life is made out of carbon, and all life is made out of roughly the same percentage of carbon-14, which is 1ppt (part per trillion). When something is alive, the amount of carbon-14 it has remains at a constant 1ppt, but once it decays, biological processes stop so the carbon influx/outflux stops too, and the C-14 starts to decay into N-14 and is not replaced. So if we examine a dead plant by giving it a radiocarbon test, and we find the amount of carbon 14 (can be calculated using the mass of total carbon) and the amount of C-14 has reduced to 1/8, it means that the plant is 18,000 years old roughly, because C-14 has a half life of 6000 years (actually about 5300 years). The N-14 that C-14 decays into is simply released into the atmosphere.

If you don’t like Carbon 14 dating, there are over 20 types of radioisotope dating, including Pb-Ur, Ar-Ar, K-Ar etc. Some of which can date back millions and billions of years because the isotope is more stable.

To prove that the dinosaur bones are 6000 years old, you would need to find some rocks in ancient geological striation, among the dinosaurs, and test them using multiple isotope tests, which should give you a dating of between 3000 and 10,000 years if you are right.
Radiometric dating is not exact science. However, dinosaur bone dating never drops below 65 million years. They cannot provide exact answers for ancient (millions to billions of years) dating, but using a range establishes consensus. If the Earth was only 6,000 years old, the radioactivity emitted by unstable materials would be huge. We would immediately notice it because almost none would have decayed...in fact, we would not be here because life could not survive in that environment.

Creationists typically answer this with two fallacious arguments:
1. Radiometric dating is erratic, different techniques give you totally different numbers. It cannot be trusted
2. Scientists assume uniformitarianism, while radiometric dating might have been greatly speeded up in the past.

Both of these are ridiculous. The error in the spectrum of radiometric dating is normal experimental error. Radioactivity, after all, is a completely random process. However, the use of multiple isotope tests is not designed to establish a precise age. It is meant to establish the magnitude. If you have three tests, one which says 50 million years, another says 70 million and another says 92 million, then that is your age range. Radiometric errata does not help creationists, because it is used only to establish the magnitude of age. Even with such error, we would notice if the Earth was 6000 years old because the spectrum would bluntly stop between 2000 years and 12000 years. Radiometric errata is not an argument for creationism. The magnitude of age always comes up on the order of millions and billions.
Uniformitarianism. Firstly, this argument is self-defeating. To assume anti-uniformitarianism (a legitimate scientific debate) one must assume the Earth is millions or billions of years old. We can measure the conditions of the last 10 000 years so accurately now that we can be certain that the cataclysm of the conditions necessary to increase radioactivity that much could only have existed long before advanced life, as such bombardment would have inevitably shut down any evolutionary projects. Anti-uniformitarianism only calls into question the accuracy of ultra-slow isotopes like U238, which halves in over 4.5 billion. years. It does not affect fast isotopes like C-14, which we can measure only to the past 60,000 years. Going back this recently, radioactivity could not have increased at all in such a short time span unless our Neanderthal ancestors were performing atomic blast tests.

Obviously, insisting the universe is 6,000 years old is completely ridiculous. As is the idea that the world was created in six days. I could present literally thousands of arguments from every scientific field in existence. Gaseous shifts, atmospheric depletion, spectroscopy, radioactive decay…all impossible if the universe is so young. At 6,000 years of age the universe was barely a tiny baby, and stellar evolution had not yet taken place with the result that matter was simple quark soup and dark energy. On the other hand, when the Earth was 6,000 years old, the Universe was fully mature. Hydrogenous ionization that had taken place during what cosmologists and astrophysicists call the “dark ages” had formed every element imaginable, and had created the fusion process necessary for the creation of stellar bodies and galactic clusters. The sun was still a little sun, because it was created roughly the same time as Earth was pulled together by it’s gravity. When Earth hit it’s 6,000th birthday, it was a lifeless boiling radioactive rock and an immature, barely existent atmospheric layer of carbon dioxide.

 

 

 

 

 

It probably wasn't the best idea to put all of your scientific cards on the table on your first move, and even if you prove these people wrong, they won't concede the point.

(deludedgod)

Guided by whom?

(Ophios)

Do you understand the difference between information and order derrived from patterns?

 

I will make one and only one point here.

The fittest survive because they are the most fit.

First off, this is a tautology, so it (in context) is true by definition. BUT also note that the group declared to be survivors is defined by the group that does survive. We have some circular reasoning.

For this reason, even if evolution is the "correct" theory of origins, it isn't and will never be science (until science is redefined to mean no experiments and just fiddling around with premises to wind up with interesting sounding statements, that is.)

Not true. Many here (myself included) would love to see an argument presented that proves us wrong. This is why we keep asking for one.

Um, no. The survivors are not defined by the group that survives. They are defined by the environment to which they have adapted. (or something like that)

1. Theory of Evolution is not a theory for the origins of life.
   
   
2. I do not even know how you came up with the second part of the above sentence. What exactly are you basing that assumption on?
   

Don't you mean, "can I have your babies?" 

 

Hee hee, Norris zen de-creationism. I like it. One could also say

 

There is no gravity, only the force of Chuck Norris's roundhouse kicks from which all other forces are derived. 

Nice rebuttal deludedgod. 

Perhaps Impeached should change his name to 'Plagiarist' though as he looks like another copy and paste jockey.

Impeached was PWNED by Deludedgod.

His bum must be awfully sore after that. O.o

Well obviously they won't concede any point. "They", as you say, would reject the knowledge regardless of how "true" (Or what we each believe to be truth.) because it contradicts what they know. Some people are afraid to change their beliefs, no matter how wrong they are proven (Please note the proven.) because they just can't stand to be wrong. Furthermore, most people get their religion from their parents, and to go against something you learned as "true" from a parent goes against their authority. Young children often view their parents as "invincible". Hence the "My daddy can beat your daddy in anything" claim made my some kids." But, one idea has scientific observation and one does not. Go figure.

(deludedgod)

Guided by whom?