I hate to ruin this for you...but just because we don't know for certain how life started that does imply a need to put God there.  I don't know how life started.  I've heard some ideas but even without them that does not produce a need for a sky daddy, it just means that we are ignorant and do not yet know the answer.

 

NOTE: MY RESPONSE IS TAKEN FROM NOTES I HAD PREVIOUSLY WRITTEN ON THESE MATTERS. Considering how often I deal with this argument, I do not want my interlocutor to think I just spent all that time typing my response below, but at the same time, that he not delude himself into thinking that I copied and pasted from somebody else.

I have a better suggestion. Your argument is a strawman.

 Many theists argue, fallaciously, for the existence of God based on the idea that existence is too complex and intricate to have formed randomly, and often attempt to make a fallacy of conflation between “not God” and “randomness.

 

The bifurcation occurs because the argument rests on the false dichotomy that “if not God, then chance”. This is fallacious because there is a third alternative (hence, we have a triconditional premise, which means that bifurcation is fallacious). That third alternative is natural process, which is not random, which is guided by the laws of physics and chemistry and such, but has no conscious will behind it. The bifurcation occurs because the theist makes the unjustified assertion that conscious will (ie a “mind” such as “the mind of God”) is necessary to create the order we see around us because it cannot be random. While it is true it cannot be random, this does not necessarily imply that it must have conscious guidance, because that fallaciously implies that we have a dichotomy between “conscious will” and “randomness”. In reality, we have unconscious, but certainly not random, processes which form the order we see. The process of biological evolution, for example, is blind-guided. But it is most certainly the absolute and precise opposite of randomness. This is true of vast numbers of natural processes which explain why things are the way they are, from star formation and cycles to geological columns . Everything down to the quantum level and up to the macrocosmic scale is governed by sets of physical and chemical laws which have no consciousness behind them, but still produce complex Order. In reality, the natural processes which do produce the order we see around us are extremely complex and anything but random. They are much, much more capable of producing natural order and complexity than we are at producing artificial complexity.

Indeed they are. Nobody here believes that it was a chance process. Chemical evolution is a well-established principle.

The process of formation of organic autocatalysis is time consuming. It begins with Piezoelectric systems on crystallien surfaces, which form the progenitors of ribozymes. The first biological molecules on Earth may have been formed by metal based catalysis on the crystalline surface of minerals.

In principle, an elaborate system of molecular synthesis and breakdown called metabolism could have existed as such long before the first cells. Life requires molecules which catalyze reactions hsih lead directly or indirectly to replication of more molecules like themselves. Catalysts with this self promoting propertycan use raw materials to reproduce themselves and therefore divert the same materials from the production of ther substances. In modern cells the most versatile catalysts are polypeptides. However, they cannot propogate self-replication, they do not replicate. There needs to be a molecule which can act as a catalyst and guide its own replication. Such a molecule does exist: RNA

Nonsense. Spontaneous generation is expressly forbidden by the laws of biogenesis. Furthermore, biological progenitors did arise numerous times individually during the RNA world and before the central organization of modern cellular organisms. Life began in the ocean, and water has left a permament stamp on our biology.

This is a strawman. The process of chemical evolution is well established. It is the opposite of chance. It is the same as biological evolution. Your argument contains a premise which is ridiculous.

The crème de la crud of your whole piece was a link to an article which openly employed the Hoyle fallacy, something that I recognized simply by the link in the first place. You do realize that the Hoyle argument is listed as a fallacy for a reason, surely?

Its easy to calculate the probabilities associated with proteins . Essentially, a protein is a string of amino acids, usually 500-2000 amino acids long. The whole of life depends on proteins. Everything else, save the genes, is a mere passive bystanders in a biological dance of life. When we observe the cell, we are in essence observing proteins. Proteins control movement (motor proteins), the control structure (structural proteins), they control concentration (transmembrane proteins), they control ion gradients (pump proteins), and most importantly, they control every single chemical reaction in the body (enzymes). Proteins don't just control the body, they are the body. All proteins fold up tightly into one highly preferred conformation. There is no limit to the number of tasks they do in the cell. Proteins can be subdivided into two large classes, the globular proteins fold up into irregular ball-like shapes and fibrous proteins. Nearly all globular proteins are allosteric, which means they can adopt two slightly different conformations, this means they have two binding sites, one of which is for a regulatory molecule, and the other is for the substrate. Allosteric control is very complex. Suffice it to say for now that it works on either negative or positive feedback (ie the regulatory molecule increases the protein's affinity for the substrate, and the other way around, or the opposite, the regulatory molecule decreases protein affinity for the substrate, which of course, would be reciprocal. In this way, regulatory molecules can turn the protein on or off, and in negative control, there is a tug of war between the regulatory ligand and substrate which are reciprocally affected by each others concentration in the cell.

A protein is a specific type of biological polymer made up a specific family of chemical subunits called amino acids. There are 20 biological amino acids, and they are distinguished by the fact that they all have a central alpha carbon, which is attached to an amine group (-NH2), a Carboxyl group (-COOH), a hydrogen, and a side chain. It is the side chain that gives each amino acid its properties, and each of the 20 has a different side chain. Proteins can be anything in length. Usually it is 50-2000 amino acids long, and the longest ones can 7000 amino acids long. The interaction between the side chains (which is determined by charge, since three are basic, four are acidic, nine are nonpolar and five are polar but uncharged) determines the shape of the protein. For instance, the nonpolar side chains are all hydrophobic (water hating) which means the protein will fold up in a manner where the nonpolar side chains are facing inwards and not exposed to water (this is the most energetically favorable conformation). This is just one of many different subtle interplays between amino acids that determine a proteins shape. However, nearly all proteins fold spontaneously in a solution, indicating that all the information necessary to fold it is stored in the amino acids.

Proteins have only one or a second highly similar conformation, that is how they work.

Now, for the number of possible combinations of amino acid, such calculations are easy to make. With just two amino acids joined in a row, we have 20^2, or 400 possibilites. With three we have 20^3 or 8000 possibilities, with ten, we have 10240000000000 possibilities, with the average protein having several hundred amino acids up to a thousand, we have vastly more conformations than there have been seconds or atoms in the universe.

However, the Hoyle Fallacy occurs here, in making our calculatiosn in the possibility of stable biological proteins arising, because the calculations, as was pointed out by the TalkOrigins archive:

· They calculate the probability of the formation of a "modern" protein, or even a complete bacterium with all "modern" proteins, by random events. This is not the abiogenesis theory at all.

· They assume that there is a fixed number of proteins, with fixed sequences for each protein, that are required for life.

· They calculate the probability of sequential trials, rather than simultaneous trials.

· They misunderstand what is meant by a probability calculation.

· They seriously underestimate the number of functional enzymes/ribozymes present in a group of random sequences.

Now, proteins do not form in this way. There is an evolutionary advantage to stable conformations forming, and stable conformations, in turn, are the ones which give rise to biological functions. There is an obvious reason for this. In my notes on the matter, I wrote:

All Proteins Bind to Other Molecules

· Properties of proteins depend on their interactions with other molecules

• Eg. Antibodies attach to viruses to mark them for destruction, the enzyme hexokinase binds glucose and ATP to catalyze the reaction between them
• Actin molecules bind to each other to produce actin filaments etc
• All proteins stick or bind to other molecules
• Sometimes tight binding, sometimes weak and short lived
• Binding is always highly specific. Each protein can usually only bind to one type of molecule out of the thousands it encounters
• The substance bound to a protein, be it an ion, a macromolecule, a small molecule etc is referred to as the ligand of that protein
• Region of the protein associating with the ligand is known as the binding site
• Usually a cavity in the protein surface caused by a particular chain of amino acids
• These can belong to different portions of the polypeptide chain brought together when the protein folds
• Separate regions of the protein surface generally provide binding sites for different ligands.

 

The Details of a Protein’s Conformation Determine It’s Chemistry

· Proteins chemical capability comes in part because neighboring chemical groups on the protein’ surface often interact in ways which enhance the reactivity of amino acid side chains

· Two categories of this: Neighboring parts of the chain may interact in a way that restricts water molecules access to the ligand binding site.

· Because water molecules tend to form hydrogen bonds, they can compete with the ligands for sites often the protein surface

· Therefore, the tightness of the protein-ligand bonding is greatly increased if water molecules are excluded

· Water molecules exist in large hydrogen bonded networks, and inside the folds of a protein a ligand can be kept dry because it is energetically unfavorable for water molecules to break from this network

· Clustering of neighboring polar amino acid side chains together can alter reactivity. If the way the protein folds forces many negative side chains together that would otherwise not associate due to their mutual repulsion, the affinity of this new pocket for a positive ion is greatly increased

· Sometimes, when normally unreactive groups like CH2OH interact with each other because the side chains on which they are on form Hydrogen bonds with each other they can become reactive, allowing them to enter reactions making/breaking covalent bonds

· Therefore the surface of each protein has a unique chemical reactivity that depends on which side chains are exposed and their exact orientation relative to each other.

 

Sequence Comparisons Between Protein Family Members Highly Crucial Ligand Binding Sights

• Many domains in proteins can be grouped into families showing clear evidence of evolution from a common ancestor
• Genome sequence reveal a large number of proteins with one or more common domains
• 3D structures of members of same domain family remarkably similar
• Even when the amino acids identity match falls to 25% the backbone atoms in two members of the same domain family have the same fold within 0.2nm
• These allow a method called “evolutionary tracing” to determine which sites in the protein domain which are most crucial to the function of said domain
• For this, the most conserved amino acids stretches are mapped onto structural model of the known structure of one family member
• The SH2 domain is a module that functions in protein-protein interactions. It binds the protein containing it to a second protein containing a phosphorylated tyrosine side chain in a specific amino acid context
• The amino acids on this binding site have been slowest to change in the evolutionary history of SH2

We must understand all of this. Biology is highly modular. It is all about the assembly of large structures from smaller ones. Polypeptides are modularly assembled from amino acids hence determining its structure hence its chemistry and binding. Proteins are modularly assembled from polypeptides, and supramolecular structures from polypeptides, therefore, the evolution of proteins will be forced in the direction of stable amino acid conformations not random possibilities associated with amino acids. This becomes evident when we consider proteomic supramolecular structures:

Protein Molecules Ofter Serve as Subunits for the Assembly of Large Structures

· Noncovalent bonding allows proteins to generate supramolecular structures like construction of giant enzyme complexes, ribosomes, proteasomes, protein filaments, and viruses

· These are not made by one giant single covalent molecule, instead by noncolvalent assembly of many giant subunits

· Advantages of this building technique: Large structure built from a few repeating subunits requires little genetic information

· Both assembly and disassembly are easily controlled and reversible

· Errors in structural synthesis are easily avoided as proofreading mechanisms can operating during the course of the assembly

· Some protein subunits assemble into flat sheets, on which the subunits are arranged in a hexagonal pattern

· Slight changes in the subunit geometry can turn the sheet into a tube, or with slightly more changes, into a hollow sphere

· Protein tubes and spheres which bind to RNA form the coats of viruses

· Formation of these closed structures provides additional stability because it increases the number of covalent bonds

· This principle is illustrate by the protein coat or capsid of may viruses

· Capsids are often made of hundreds of identical protein subunits enclosing and protecting the viral nucleic acid code

· The proteins of capsid must have particularly adaptable structure. Not only must it have multiple contact points to make a stable sphere but also must be able to change to let the nucleic acid out to initiate viral replication in a cell. This is shown here by the construction of a capsid from monomer protein subunits, which connect into dimers, then trimers, then into the intact sphere with the addition of more free dimers

 

 

Well, as you may have inferred from my response, I am a trained molecular biologist. Strobel is...well, to be charitable, Strobel is not (to be less charitable: Strobel is an idiot).

Now, allow me to continue:

 Polynucleotides Can Both Store Information and Catalyze Chemical Reactions. RNA can propagate itself by means of complementary base pairing. However, this process without catalysis is slow, error prone and inefficient. Today, such processes are catalyzed by a massive battery of complex interactions of RNA and proteins.

In the RNA world, the RNA molecules themselves would have acted as catalysts. A pre-RNA world probably Predates the RNA One. It is unlikely RNA was the first self-replicating propogater. It is difficult to imagine that they could form through nonenzymatic means. The ribonucleotides are hard to form enzymatically, also RNA polymers entail a 5 to 3 chain which must compete with other linkages that are possible including 2 to 5 and 5 to 5. It has been suggested that RNA was anteceteded by molecules with similar properties, but that were similar. Candidates for pre-RNA include p-RNA and PNA (peptide nucleic acid)

The transition from pre-RNA to RNA would have occurred through the synthesis of RNA via these simpler components as template and catalyst. Laboratory experiments demonstrate this as plausible. PNA can act as a template for RNA molecules. Once the first RNA molecules had been produced, they could have outphased their antecedents leading to the RNA world

Single-Stranded RNA molecules can fold into highly elaborate structures Comparisons between many RNA structures reveal conserved motifs, short structural elements used over and over again as part of larger structures. Common motifs include

Single strands, double strands, single nucleotide bulges, triple nucleotide bulges, hairpin loops, symmetric internal loops, asymmetric internall loops, two stem junction, three stem junctions and four stem junctions. RNA molecules can also form common conserved interactions such as psuedoknots and “kissing hairpins” and hairpin-loop bulge contacts.

-Protein catalysts require a surgace of unique countours. RNA molecules with appropriate folds can also served as enzyme. Many of the ribozymes work by positioning metal ions at the catalytic sites. Relatively few catalytic RNA exist in modern day cells, being the polypeptides work much better.

An example of In vitro selection of synthetic ribozymes:

 

-A large pool of dsDNA each with a randomly generated sequence. Transcription and folding into randomly generated RNA molecules. Addition of ATP derivative containing a sulfer in place of oxygen Only a rare RNA has the ability to phosphorylate itself. This is captured by elution of the phosphorylated material

These experiments and others like them have created RNAs that can catalyze a wide variety of reactions:

Peptide bond formation in protein synthesis, RNA cleavage and DNA ligation, DNA cleaving, RNA splicing, RNA polymerization, RNA and DNA phosphorylation, RNA aminoacylation, RAN alkylation, Amide bond formation, amide bond cleavage, glycosidic bond formation and porphyrin metalation, since, like proteins, ribozymes undero allosteric conformation change

Self-Replication Molecules Undergo Natural Selection

-he 3D structure is what gives the ribozyme chemical properties and abilities. Certain polynucleotides therefore will be especially successful at self-replication. Errors inevitably occur in such processes, and therefore variations will occur over time. Consider an RNA molecule that helps catalyze template polymerization, taking any RNA as a template

-This molecule can replicate. It can also promote the replication of other RNA. If some of the other RNA have catalytic activity that help the RNA to survive in other ways, a set of different typers of RNA may evolve into a complex system of mutual cooperation.

One of the crucial events leading to this must have been the development of compartments. A set of mutually beneficial RNA could replicate themselves only if the specialized others were to remain in proximity

Selelection of a set of RNA molecules according to the quality of replication could not occur efficiently until a compartment evolved to contain them and therefore make them available only to the RNA that had generated them. A crude form of this may have simly been simple absorption on surfaces or particles.

The need for more sophisticated containment fulfilled by chemicals with the simple physiochemical properties of ampipathism. The bilayers they form created closed vesicles to make a plasma membrane. In vitro RNA selection experiments produced RNA molecules that can tightly bind to amino acids. The nucleotide sequence of such RNA contains a disproportionate number of codons corresponding to the amino acid. This is not perfect for all amino acids, but it raises the possibility that a limited genetic code could have arised this way. Any RNA that guided the synthesis of a useful polypeptide would have a great advantage.

Is that enough detail?

To the original poster:

Deludedgod is an evolutionary biologist. He is working on one of the most cutting edge processes in the field, and has spent a great deal of his life learning, right down to the atomic level, exactly what goes on as life evolves. He has a great many letters next to his name, which correspond to thousands and thousands of hours of research, lab time, and study.

Have you ever even read an introductory book on molecular biology? Do you know anything at all about it?

This isn't a rhetorical question. I would like for you to answer the question directly. Exactly how much do you know about evolution?

 

 Oh, on an unrelated side note... I gather since you like Lee Strobel that you've never studied basic logic either...

No kidding, Strobel's logic could be used as a textbook for bad argument.  In fact, I've done exactly that when I helped a friend design a basic debate course for his university class.

 

Whoopsy!

Thanks for the clarification.

 

As others have already pointed out, science does not propose that a complex life-form came into existence from spontaneous chance collision of all the component parts in just the right place.

We don't even expect anything much more complex than a hydrogen atom to form this way.

Complex structures typically arise in a long sequence of steps.

Simple structures, say hydrogen and heiium atoms may indees form by fundamental particles coming together. Once we have large quantities of these simple atoms, the existence of gravity will tend to to cause them to clump together. Then the possibility increases for them to interact, under the right conditions, to form more complex atoms, via fusion reactions.

Once we have accumulated enough heavier atoms, we now have the possibility for them to come together into solid particles (dust). which in turn can accumulate into larger solid bodies, and so on.

It would be extremely improbable for a collection of sub-atomic particles corresponding to the atoms in an earth-sized planet to suddenly condense into a structure we would recognize as a planet, with core, mantle, oceans, continental plates and atmosphere,

All these steps rely on a large number of component parts at one level to build up by partly random processes steered by physical laws into higher level structures. Once enough of these higher-level bits accumulate, the probability of the next level of structure to arise somewhere in the 'population' of components increases.

One list of successive levels of 'complexity' could be: sub-atomic particles -> atoms -> molecules -> macro-molecules (proteins, DNA, etc) -> simple cells -> multicellular organisms. This is not necessarily the only way to organize what we observe, but it is one way to break up the complexity of what we see around us into manageable thought-patterns.

Another simple way of making the distinction between the probability of all-at-once and step-by-step change from one state to another is to think of two sorts of combination lock. If there is no feedback at all if an input sequence has some correct settings, then we are forced to explore all possible combinations, eg one million for 6 digits. However, if we had a device which allowed each consecutive digit to be set and 'locked in', we would only require a maximum of 60 tries instead of a million.

Again, science does NOT claim that life is simple to create. We just don't think it is so improbable that it is extremely unlikely to arise in a a universe containing the number of star-systems and planets which we now think are likely to exist. It does require a certain set of pre-conditions, which typically includes a minimum amount of the pre-cursor materials, eg amino acids, and the appropriate physical conditions, and quite a lot of time. The smaller the quantity of pre-cursor material, and the smaller the range of local variations and combinations of environmental conditions of temperature, pressure, exposure of certain mineral surfaces which may have catalysed certain chemistry, etc, the less likely are we to reproduce the process lab conditions and time-scales, even if we had a better understanding of the processes.

Just thought I would add my own take on what I saw as the principle errors/miscoceptions in the OP - I had contemplated more, but after seeing DG's post, decided the details had been pretty exhaustively covered .

0_0 wtf? I definitely didn't expect a reply like that. His simple acceptance of the truth was.... refreshing. Good job boys.

And Phil thanks for being reaonable, its nice for a change. 

And please... No more of 2nd law of thermodynamics.

Whatever happens, the amount of entropy will continue to rise on a cosmological scale. And the universe is the only really closed system we know of (as far as we think we know).

 

Jargon aside, this remains an argument from ignorance. In the absence of an explanation, an unsubstantiated, unprecedented agency, more complex than the problem itself, doesn't provide the default explanation for this, or any other problem. Applied uniformly, such an approach would resemble paranoid schizophrenia rather than science.

Considering that the vast majority of phenomena originally attributed to the works of God or gods have been subsequently shown to have "natrual" (i.e. non-divine) causes, including lightning, the rise and fall of the sun, the formation of the solar system, the origin of the human species, the causes of disease and illness, earthquakes, the tides, the phases of the moon, and so on, it seems odd that you would suggest that god is a viable explanation for anything at all.