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Kirk Durston: A common either-or mistake both Darwinists and ID theorists make

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Biophysicist Kirk Durston of the New Scholars Society offers an explanation below:

Note: Kirk Durston is back and this post has been stuck to the front page until late this evening EST, so that further comments and his responses may be noted. – News

There is a common either-or mistake made by most Darwinists and, quite frequently, by ID theorists as well. The mistake, which is an example of the fallacy known as the false dichotomy, can be described as occurring when one assumes that either no functional information encoded in the genomes of life can be produced by natural processes, or all of it was produced by natural processes. A closely related mistake made by Darwinists is the assumption that if natural processes can produce a trivial level of functional information, then we can safely conclude that natural processes can produce all biological information.

There are still challenges in mathematically defining functional information or functional complexity. For my purpose here, however, I will simply use the mathematical descriptions published by Hazen et al., and Durston et al. Both approaches cited are very closely related to an earlier equation published in 1951 by Leon Brillouin, which can be simply represented as

FI = -log nf/nt

Where nf = number of sequences that are functional and nt = the total number of possible sequences. It should be clear from the above equation that if nf is large enough for examples to be generated by random recombinations, then functional information (FI) can be generated by random natural processes, albeit a trivial level. For example, it is clear from work done at the Georgia Institute of Technology, that nf for simple binding pockets is pretty high, which entails that the FI required to code for binding pockets is relatively trivial.

Reflection on the above equation reveals that the FI required for a given function can range anywhere from zero to some very high number. It is, therefore, a mistake to assume that FI can only be generated by intelligence; a trivial level of FI can be produced by completely mindless processes, as should be obvious from the above equation, and as the Georgia Tech results illustrate.

It is also a mistake to assume, as many Darwinists do, that because mindless processes can generate a trivial level of FI, therefore mindless processes can generate high levels of FI. Again, reflection upon the above equation (or the more detailed equations published by Hazen or Durston) reveal that the higher the FI required, the less probable it becomes (i.e., the nf/nt ratio approaches zero).

The fatal mistake made by Darwinists at this point is to invoke what has become the Darwinist god-of-the-gaps, namely selection. As we can illustrate from evolutionary algorithms, selection requires a fitness function which, itself requires FI to encode. Of course, it follows from what I am arguing here that trivial levels of selection can be produced with trivial levels of FI. The question is whether natural selection has sufficient information to locate stable, functional, biological proteins. All our work to date seems to falsify that option and verify the need and actual role for intelligent design (in this case human) when producing artificial proteins of any significant structure. To clarify, recent building of artificial proteins is an example of intelligent design in action.

The Georgia Tech work has led some Darwinists to believe that because binding pockets are relatively trivial to encode in a sequence that, therefore, we have somehow explained how natural processes could have encoded biological proteins. In real life, however, proteins are about a lot more than simple binding. Binding to the right molecule is important, at the right time, at the right location and with the right binding strength so that the bond can be broken at the right time and place, etc. This can often require a larger 3D structure for proper functionality, that has a nf/nt ratio approaching zero. For example, if we take the results published for 35 protein families by Durston et al., and solve for nf/nt, we observe that it is extremely small for many protein families.

My contention is that the ability to generate statistically significant levels of functional information is unique to intelligence. It follows from this that if a function can be achieved with a statistically insignificant level of FI, then intelligence is not required. Statistical significance, therefore, is the safeguard against false positives and can be measured in a variety of ways, such as measuring the adjusted residual of the outcome and choosing a cutoff that represents a very high confidence level, such as 99.9% or greater. With this in mind, an executive summary of my own case for intelligent design in biological life is available here.

Comments
jerry: Are ORFans really genes? Yes, they are actually genes. Of course, ORFan is a play on words. ORF - Open Reading Frame, Orphan - without parents or of unknown parentage. I posted a number of relevant posts (including reference links) which Salvador Cardoza then proceeded to delete in the interests of "Serving the Intelligent Design Community." Or maybe it was out of pure pettiness. I'm going with the latter.Mung
September 2, 2013
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Dr. Durston, This thread has disappeared down the list of posts on UD but I have a question/request for you based on some recent comments on other threads. It has to do with ORFan genes. Supposedly, they are quite common in each species' genome. However, from the conversation that takes place when they are discussed it is not clear just what they are of how much is known. Assume my knowledge is limited for the questions that follow. Some questions, Are ORFans really genes? I assume a gene is something that actually codes for a protein. Can something be called a gene if it is just transcribed but never translated into a protein? Are ORFans just genomic entities that have mutated over time and may not actually do anything functional in the genome? I assume that the term "junk DNA" is becoming less appropriate but that there are some parts of the genome that are not functional in any way. Are there ORFans that are in some ethnic groups that are not in others. Let me give some examples. I recently had my genome analyzed by 23andme and it indicated that about 3% of it was due to a Neanderthal background. From what I understand this is common as the average for non-Africans is 2.7% Because of this I would expect that these differences are just different variations of alleles but are they more than that. Would there be different ORFans in Australian aborigines than in African? The Australian aborigines supposedly migrated there 40,000 years ago and so would be one of the most isolated groups on the planet. Or do all humans have essentially the same genes and what we see in both ORFans and other genes is just different alleles? Finally, could these ORFans be analyzed for the protein generating capability. I probably poorly understand proteins but is it possible to analyze an ORFan to see what kind of protein it would be and whether it would be functional or not. If you should ever read this and have time, your answers would be quite interesting to many of us here.jerry
September 2, 2013
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Anyone want to help craft a really interesting question for Kirk to ponder upon his (hopeful) return?Mung
August 20, 2013
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I, for one, hope to see more of Dr. Durston here. This post (and its comments) was awesome.MrMosis
August 18, 2013
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Oops Enjoy!Alan Fox
August 17, 2013
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Enjou your break, Dr. Durston.Alan Fox
August 17, 2013
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KD: Well noted. I think it is an inadvertent testimony to the force of the needle in the haystack point that objectors are being reduced to imagining that folding AA sequences yielding key-lock fitting patterns in life forms are common in sequence space. This seems to be one of those, this must have happened for what I "know" to be true so it is also true. What is missing of course as you point out is proper empirical warrant. KFkairosfocus
August 17, 2013
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#149 Alan Fox: Again, you are confusing 'functional' with 'structural'. In your post, re-read the opening quote you used from me. You will see that it says 'structural' not 'functional'. Biological life seems to require STRUCTURE for its functional proteins. (not sure of your background, but if the importance of structure in biological protein function is something you are unfamiliar with, you may want to read a couple of quick articles on the web on this subject.) So in this discussion, we not merely interested in some random 'function' that a scientist in the lab defines, such as 'will it bond to something'? In this discussion, we are interested in proteins that will fold into a stable, repeatable 3D structure as our first step. Then, we can sift through those to see which ones might be functional. Second, your Rosetta quote makes my point. The Rosetta results were for an existing sequence that we already knew produced a stable 3D structure, we just had to solve the structure. We gave it the sequence (T0283) and then we tried to figure out its 3D structure. An entirely different problem ..... extremely difficult, but vastly easier than feeding in random sequences to see if they have any 3D structure. Third, Dembski's P(T/H) is not what we are discussing here. We are not discussing the probability of observing some particular pattern/structure/sequence. The probability that Hazen et al use in the paper cited eaerlier on in this discussion is the ratio of ALL the functional sequences for a given biological protein, observed and not-yet-discovered (please notice the 'not-yet-discovered' bit), over the total number of possible sequences for the given number of sites in the sequence. Finally, nobody in the field thinks that stable, 3D structures are common in sequence space. Please note I am talking about 3D structural proteins, which biological life seems to need, not some random sequence that has a lab-defined 'function' of merely binding to something. I repeat, nobody in the field thinks that sequences forming stable, 3D structures are common in sequence space. If you believe they are, show us the paper. In science, we need to operate on the basis of what is testable and verifiable. The hypothesis that 3D structures are common in sequence space is consistently falsified in experiments done in the field. To clarify, we have tested it numerous times and consistently failed to verify it. Everything we are learning about protein sequence space is falsifying the hypothesis that stable, repeatable 3D structures are common. This, in turn, is falsifying the neo-darwinian hypothesis. All: I am taking two weeks vacation starting today, so I will not be able to respond to any further posts until early September. With this in mind, I think I will leave the last word to Alan Fox and others who wish to respond.KD
August 17, 2013
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These structural proteins are extremely rare in sequence space. period. fact. and all our science verifies that.
This is wrong. The rarity of functional proteins in the totality of possible protein sequences is unknown. From a Wikipedia article De novo protein structure prediction;
A major limitation of de novo protein prediction methods is the extraordinary amount of computer time required to successfully solve for the native confirmation of a protein. Distributed methods, such as Rosetta@home, have attempted to ameliorate this by recruiting individuals who then volunteer idle home computer time in order to process data. Even these methods face challenges, however. For example, a distributed method was utilized by a team of researchers at the University of Washington and the Howard Hughes Medical Institute to predict the tertiary structure of the protein T0283 from its amino acid sequence. In a blind test comparing the accuracy of this distributed technique with the experimentally confirmed structure deposited within the Protein Databank (PDB), the predictor produced excellent agreement with the deposited structure. However, the time and number of computers required for this feat was enormous – almost two years and approximately 70,000 home computers, respectively.
And that was just for one protein sequence. As I keep saying, the claim that functional proteins are rare is, at best, premature. This, of course has major impact on Dembski's CSI concept and P(T|H). As Dr. Liddle points out "P(T|H) is the Probability that we would observe the Target (i.e. a member of the Specified subset of patterns) given the null Hypothesis". I'll grant you, demonstrate that functional proteins are needles in haystacks and that will be a real problem for evolutionary theory.Alan Fox
August 17, 2013
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AVS, What he means is, that for new structures to emerge in evolutionary history new structural proteins are required. That should be fairly non-controversial. These structural proteins are extremely rare in sequence space. period. fact. and all our science verifies that. New structural proteins require new structural folds. So imagine all the "functionality" you want to conjure up, it's all irrelevant. What's relevant is protein folds. But it'll take you longer than your life span to stumble on one through random trials. IOW, Darwinism is falsified by the facts. cheersMung
August 16, 2013
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"Structure" is extremely rare in proteins? What on Earth do you mean by that?AVS
August 15, 2013
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#144 Alan Fox:It appears to me that you are confusing function with stable 3D structure ... 'function' is common if any sort of binding qualifies; 'structure' is extremely rare and all our science verifies that. If you will review my posts, I have consistently argued that functional sequence space for proteins is probably extremely common, provided we are willing take a loose definition of 'function' to include binding to various molecules and not worry about stable 3D structures. An amyloid of misfolded proteins sticking to the side of my coffee cup would qualify as 'functional' under this looser definition, but that is irrelevant to how stable, functional 3D folds were 'found'. What I have also argued for is that proteins with a stable 3D structure are extremely rare in sequence space, and that is what 70% of biological proteins seem to be. The Cherny et al. paper does nothing (e.g., absolutely nothing) to support the idea that stable 3D folds may be common in untested sequence space. In fact, it does quite the opposite; they relied on designed 4-helix barrel structure. This is explicitly stated in their paper. There are other papers that expand on how we designed this structure using knowledge we have reverse engineered from biological proteins.KD
August 15, 2013
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Alan, Dr Saurer did the experiments and demonstrated sequence space is rare. Again your ignorance, while amusing, means nothing here.Joe
August 15, 2013
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Dr Durston at 143 My point is simply that you can't infer that unknown sequence space is rare in functional proteins. One just doesn' t know. Maybe evidence will emerge but, for now, we just don't know.Alan Fox
August 14, 2013
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#141 Alan Fox: You will need to support your assertion with some details. Which of my claims does the Cherny et al. not support and what, specifically, in the paper are you referring to? I trust you are not referring to the designed (i.e., ID in action) alpha-helix proteins they used in their experiment. The 4-helix bundles were designed using information we have reverse engineered (design derivation, another way ID is firmly entrenched in science). They were not, however, designed to bind to anything in particular. There is nothing in this paper that supports your claim. If you believe there is something I have missed, please do point it out. Did you not notice the word 'designed' they use to describe how they achieved the 4-helix structures? Please note that I have never contested the ability of random sequences to bind to something.KD
August 14, 2013
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does not seem to support your claims. Quite the contrary.
Why is it quite the contrary? Or does not support Dr. Durston's claims?jerry
August 13, 2013
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@ Dr Durston Thanks for bringing the work of Michael Hecht and his team to my attention. His paper does not seem to support your claims. Quite the contrary.Alan Fox
August 13, 2013
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@ Upright Biped Dr. Durston has been awarded his Ph D in Biophysics at Gueph, now, I believe.Alan Fox
August 13, 2013
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I second that, please Mr Durston, please post as often as you can. Thanks.Upright BiPed
August 11, 2013
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KD, Yes, indeed, thanks for posting. Most interesting. Please come back often.CentralScrutinizer
August 11, 2013
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#136 Optimus: It is an honour and a pleasure.KD
August 11, 2013
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@ KD Thanks for the excellent guest post!Optimus
August 9, 2013
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AF:
But we are back to the same point. You will have to clarify how one can make a claim about unsearched sequence space when it remains, well, unsearched.
IANAS, but isn't there something like a principle of uniformitarianism where, absent evidence to the contrary, one can infer that what is true about what has been sampled or searched will be more likely to hold true for what has not yet been sampled or searched than the opposite? I would think it would be quite routine to make claims about what is unsearched based on what has previously been discovered. But again, IANAS.Phinehas
August 8, 2013
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#130 Mung: The first paper I referred to that presents a method to measure the Functional Sequence Complexity (FSC) of protein families is here . I’ve not read Life’s Ratchet but just reading the brief summary, he seems to be starting with some simple molecular machines which ‘custom-build’ other molecular machines, etc. When I read stuff like this, it is discouraging as to how low science has stooped in confusing creative story telling with doing actual work. I have read tons of stuff over the past 25 years that boils down to blissful, naive optimism which refuses to face the cold hard reality of how difficult it is to build nano-machines by molecules ‘crashing into each other’. The gigantic Achilles heel in all this just-so story telling is a failure to actually crunch the numbers. The very first step one ought to take before waxing eloquent with the latest evolutionary scenario is to test the hypothesis that the particular protein structure being extolled can actually be stumbled upon in a blind evolutionary search. More on this below by way of example. Alan Fox: I agree with you that the process of evolution is not a search for anything. The term ‘search’ is a term we use in Genetic Algoritms (GE’s), which is our best computational tool to attempt to model real-world evolution. But you are right in that the real world evolutionary process is a blind, mindless process. I also agree with your statement that ‘evolutionary processes don’t take huge leaps in the dark’, but I think you have essentially falsified the neo-darwinian theory of macro evolution when you apply that premise to the gigantic leaps it would need to take across non-folding sequence space to ‘locate’ (by blind, mindless random walks) biological protein structural domains (if one wishes to take a modular approach). Blanco (Blanco FJ, Angrand I, Serrano L (1999) Exploring the conformational properties of the sequence space between two proteins with different folds: an experimental study. J Mol Biol 285:741-753) showed this in his attempt to evolve one protein into another. Lenski’s work in the LTEE is highly commendable. Finally, after 150 years of granting the conclusion before the experiment has been carried out, we are actually witnessing the capabilities, or lack thereof, of blind, mindless evolution at work. Two successive mutations are almost certain going to occur. That is trivial. For the average structural domain, we are going to need approximately 100 successive mutations before mindless evolution ‘lucks’ into a stable, repeatable structural domain. No structural protein biologist thinks that stable 3D structures are common in protein sequence space. The consensus is that they are extremely rare. My objective was to figure out how rare they are. The first step is to measure the amount of FI or FSC required to code for any member at all of a protein family. The real story in the LTEE is that it is falsifying the neo-darwinian hypothesis that novel protein families were produced at a rate of several per 50,000 generations. The LTEE has serious negative implications for the evolution of larger organisms that have a much slower replication rate. This, however, is a major discussion in itself, worthy of a future post on this forum. An example of a single structural domain target size (and the kind of evolutionary leap it would require) is given by Ribsomal S12. I published the FSC required for Ribosomal S12, a single domain protein that is absolutely essential for life here . It is a universal protein found in all life forms, and is conjectured, therefore, to be a component of LUCA. The FSC is 359 functional bits. By plugging that into the FI variable of Hazen’s equation, you can solve for nf/nt. It turns out to be about one chance in 10^-108. Evolution does not have an ‘unimaginably’ large number of chances. A published upper limit is 10^-43. So evolution was fortunate enough to mindlessly find a target absolutely essential in its shape/structure to enable the greater function of the Ribosome, and it mindlessly performed that fantastic leap on a ‘target’ with frequency of occurrence in sequence space of about 10^-108 in less than an absurdly small 10^43 trials. Darwkins’ climing Mount Improbable is a myth when it comes to stable folding domains. Folding is such that it is all or nothing. My more recent work here shows just how integrated those structures are. If you are aware of any paper at all that shows that stable folding proteins are relatively common in sequence space (by ‘relatively common’ let us use 10^43 searches, which is an upper limit), then let me know about it and we will discuss it. The consensus is that they are so rare, it is useless to search for them. Thus, we have turned to reverse engineering biological proteins, figuring out their design principles, and intelligently designing them using these principles …. Intelligent design in action in the lab. See, for example Fisher MA, McKinley KL, Bradley LH, Viola SR, Hecht MH (2011) De novo designed proteins from a library of artificial sequences function in Escherichia coli and enable cell growth. PLoS ONE 6:e15364 and count the number of times ‘designed’ is used (29 times), ‘design’ is used (11 times) and ‘strategy’ is used (3 times). With regard to ‘transitional’ protein families that may have occurred in the past, all our science is showing is that there are no such thing as ‘transitional’ structural domains. Structural domains occupy what we can refer to as clearly bounded islands in sequence space. Each domain can be regarded as a ‘fold-set’ which can actually be capable of 2 or 3 unique, distinct folds depending upon meta-stable states in folding, (itself a design masterpiece), but each island is surrounded by unstable folding space, shown in many papers as early as Fisher MA, McKinley KL, Bradley LH, Viola SR, Hecht MH (2011) De novo designed proteins from a library of artificial sequences function in Escherichia coli and enable cell growth. PLoS ONE 6:e15364 and more recently in Yang JR, Zhuang SM, Zhang J (2010) Impact of translational error-induced and error-free misfolding on the rate of protein evolution. Mol Syst Biol 6:421 Summary Point: At the end of the day, real science has to go with what is testable, verifiable and falsifiable. Appealing to what we might discover, or what we don’t know to justify belief in neo-darwinian macroevolutionary theory, especially in the face of real science which is making such beliefs increasingly untenable, is not science. Real science indicates that the average stable structural domain families are extremely rare in sequence space requiring gigantic leaps in any supposed mindless evolutionary process, essentially falsifying the theory. A hyper-intelligence, on the other hand, is capable of understanding physico-chemical properties, solving millions of equations simultaneously, containing hundreds of thousands of variables (including the torsion angles), and with the results, creating the right-shaped structures to fit together into molecular machines such as the ribosome or F1ATPase and building an entire organism. We do similar all the time with much simpler structure such as laptop computers, and spacecraft. It is all ID in action. I have looked at Thornton’s work, but her group is focused on the evolution of functions of existing protein families and super families. My work focuses on the structure of protein families. Each structure or each protein family may have a variety of functions and two or three fold-sets. Indeed, a good design will choose those structures that are multi-functional, or within a short evolutionary step of novel functions. From what I gather, her work explores the evolutionary capabilities of existing structures/families. Those are relatively easy for an evolutionary process to stumble upon. Stable structural domains are not.KD
August 8, 2013
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I don't believe Gregory and his like-minded believers in thaumaturgy by inanimate matter realise that empirical science is no more and no less than a natural (no pun intended), indeed, inevitable, development from the utterly unique corpus of knowledge and understanding of the Christian Church accrued over more than 1000 years (now 2000). Indeed, add to that, its epistemological matrix, Judaism, equally unique in OT times, and it is clear that what we have been witnessing - despite the farce of the so-called, Enlightenment - is theism first, atheism nowhere; which is why those students interviewed by Ray Comfort were flummoxed to think of a single famous atheist. The systematic study of the world, as has been pointed out many times, is one of the benefits granted to mankind by Christ's Incarnation, through his church' So, no, the rise of science did not have to await the arrival of atheists. On the contrary, it was in Elizabethan times that the Protestant Christian, Francis Bacon proposed a new science of observation and experiment to replace the traditional Aristotelian science, as Descartes, a Huguenot, was to do later. The atheists have always lived off the back of the real scientists, theists and, of course, believers in Intelligent Design. Capitalizing those two words is deeply offensive to me, since it is no more than the most elementary common sense that the worked was designed - and that, by a super intelligence, beyond our imagination.Axel
August 8, 2013
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Mr Fox, I'm fairly certain that you have already been corrected before on Szostak and Lenski's empirical research and that you now simply refuse to accept falsification from the experimental evidence, but just to make 100% certain that you, and others, know for a fact that you are making completely bogus claims in regards to the evidence at hand, I will remind you:
Richard Lenski's Long-Term Evolution Experiments with E. coli and the Origin of New Biological Information - September 2011 Excerpt: The results of future work aside, so far, during the course of the longest, most open-ended, and most extensive laboratory investigation of bacterial evolution, a number of adaptive mutations have been identified that endow the bacterial strain with greater fitness compared to that of the ancestral strain in the particular growth medium. The goal of Lenski's research was not to analyze adaptive mutations in terms of gain or loss of function, as is the focus here, but rather to address other longstanding evolutionary questions. Nonetheless, all of the mutations identified to date can readily be classified as either modification-of-function or loss-of-FCT. (Michael J. Behe, "Experimental Evolution, Loss-of-Function Mutations and 'The First Rule of Adaptive Evolution'," Quarterly Review of Biology, Vol. 85(4) (December, 2010).) http://www.evolutionnews.org/2011/09/richard_lenskis_long_term_evol051051.html Mutations : when benefits level off - June 2011 - (Lenski's e-coli after 50,000 generations) Excerpt: After having identified the first five beneficial mutations combined successively and spontaneously in the bacterial population, the scientists generated, from the ancestral bacterial strain, 32 mutant strains exhibiting all of the possible combinations of each of these five mutations. They then noted that the benefit linked to the simultaneous presence of five mutations was less than the sum of the individual benefits conferred by each mutation individually. http://www2.cnrs.fr/en/1867.htm?theme1=7 New Research on Epistatic Interactions Shows "Overwhelmingly Negative" Fitness Costs and Limits to Evolution - Casey Luskin June 8, 2011 Excerpt: In essence, these studies found that there is a fitness cost to becoming more fit. As mutations increase, bacteria faced barriers to the amount they could continue to evolve. If this kind of evidence doesn't run counter to claims that neo-Darwinian evolution can evolve fundamentally new types of organisms and produce the astonishing diversity we observe in life, what does? http://www.evolutionnews.org/2011/06/new_research_on_epistatic_inte047151.html More from Lenski's Lab, Still Spinning Furiously - Michael Behe - January, 2012 Excerpt: So at the end of the day there was left the mutated bacteriophage lambda, still incompetent to invade most E. coli cells, plus mutated E. coli, now with broken genes which remove its ability to metabolize maltose and mannose. It seems Darwinian evolution took a little step sideways and two big steps backwards. http://www.evolutionnews.org/2012/01/more_from_lensk055751.html
This following paper was the paper that put the final nail in the coffin for Szostak's work for ATP binding:
A Man-Made ATP-Binding Protein Evolved Independent of Nature Causes Abnormal Growth in Bacterial Cells - 2009 Excerpt: "Recent advances in de novo protein evolution have made it possible to create synthetic proteins from unbiased libraries that fold into stable tertiary structures with predefined functions. However, it is not known whether such proteins will be functional when expressed inside living cells or how a host organism would respond to an encounter with a non-biological protein. Here, we examine the physiology and morphology of Escherichia coli cells engineered to express a synthetic ATP-binding protein evolved entirely from non-biological origins. We show that this man-made protein disrupts the normal energetic balance of the cell by altering the levels of intracellular ATP. This disruption cascades into a series of events that ultimately limit reproductive competency by inhibiting cell division." http://www.plosone.org/article/info:doi%2F10.1371%2Fjournal.pone.0007385 Strange Behavior: New Study Exposes Living Cells to Synthetic Protein - Dec. 27, 2012 Excerpt: ,,,"ATP is the energy currency of life," Chaput says. The phosphodiester bonds of ATP contain the energy necessary to drive reactions in living systems, giving up their stored energy when these bonds are chemically cleaved. The depletion of available intracellular ATP by DX binding disrupts normal metabolic activity in the cells, preventing them from dividing, (though they continue to grow).,,, In the current study, E. coli cells exposed to DX transitioned into a filamentous form, which can occur naturally when such cells are subject to conditions of stress. The cells display low metabolic activity and limited cell division, presumably owing to their ATP-starved condition. The study also examined the ability of E. coli to recover following DX exposure. The cells were found to enter a quiescent state known as viable but non-culturable (VBNC), meaning that they survived ATP sequestration and returned to their non-filamentous state after 48 hours, but lost their reproductive capacity. Further, this condition was difficult to reverse and seems to involve a fundamental reprogramming of the cell. http://www.sciencedaily.com/releases/2012/12/121227143001.htm How Proteins Evolved - Cornelius Hunter - December 2010 Excerpt: Comparing ATP binding with the incredible feats of hemoglobin, for example, is like comparing a tricycle with a jet airplane. And even the one in 10^12 shot, though it pales in comparison to the odds of constructing a more useful protein machine, is no small barrier. If that is what is required to even achieve simple ATP binding, then evolution would need to be incessantly running unsuccessful trials. The machinery to construct, use and benefit from a potential protein product would have to be in place, while failure after failure results. Evolution would make Thomas Edison appear lazy, running millions of trials after millions of trials before finding even the tiniest of function. http://darwins-god.blogspot.com/2010/12/how-proteins-evolved.html
Here is a very interesting comment by Nobel prize winner Jack Szostak himself:
The Origin of Life on Earth Excerpt: Every living cell, even the simplest bacterium, teems with molecular contraptions that would be the envy of any nanotechnologist. As they incessantly shake or spin or crawl around the cell, these machines cut, paste and copy genetic molecules, shuttle nutrients around or turn them into energy, build and repair cellular membranes, relay mechanical, chemical or electrical messages—the list goes on and on, and new discoveries add to it all the time. It is virtually impossible to imagine how a cell’s machines, which are mostly protein-based catalysts called enzymes, could have formed spontaneously as life first arose from nonliving matter around 3.7 billion years ago. Dr. Jack Szostak - Nobel Laureate and leading Origin of Life researcher who, despite the evidence he sees first hand, still believes 'life' simply 'emerged' from molecules http://www.scientificamerican.com/article.cfm?id=origin-of-life-on-earth
Mr. Fox will you do the proper thing by now acknowledging your mistake and gratefully thanking those who corrected you on your error? Or will you, as usual, ignore the correction only to wait and make the same bogus claim down the road when you think no one who knows your error is looking?bornagain77
August 8, 2013
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BTW Dr Durston, I'd be interested to hear if any cross-pollination has occurred between you and Janet Thornton and her group at Cambridge. This paper looks interesting.Alan Fox
August 8, 2013
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KD, Thank you very much for taking the time to respond to my questions. Is your first paper reproduced in Able's book The First Gene? If not, and I ask your indulgence if you've already mentioned it earlier in the thread, to which paper are you referring? I'm moving, my book on modular protein domains is in storage, if you're still around when I get my internet service back and can access that book again perhaps I'll have a followup. Until then, as a biophysicist, have you had a chance yet to read Life's Ratchet? If so, care to comment?Mung
August 7, 2013
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Jack Szostak’s work with ATP binding showed the way.
Showed the way to what?
The Lenski experiment (still ongoing) showed that is possible with the citrate digestion ability that needed two successive mutations.
It already had that ability- to digest citrate. The mutations just allowed it to digest citrate in an aerobic environment. And Lenski still hasn't shown that the mutations were random in any sense of the word. What Lenski has demonstrated is evolutionary processes are very limited. No new proteins, no new protein configurations, nothing that can be extrapolated into macroevolution.Joe
August 7, 2013
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I think the hypothesis you are suggesting is that functional sequences may be common enough in sequence space such that an evolutionary process would be reasonably likely to find a sufficient number of different functional proteins to enable the full diversity of life we see today.
Yes. Except I don't think of the process of evolution as a search for anything, rather stumbling upon variations close to the primitive protein. Evolutionary processes don't take huge leaps in the dark.
This is a reasonable hypothesis. Anyone interested in Darwinian theory or ID theory needs to seriously consider it. Furthermore, recent work suggests that randomly sequenced non-biological proteins can bind to particular molecules, thus qualifying as ‘functional’ so far as their ability to bind to something.
I agree. Jack Szostak's work with ATP binding showed the way.
Now let us consider that hypothesis a little more carefully.
OK Your first point is context. And I take the point. But remember that nothing rules out co-evolution. The Lenski experiment (still ongoing) showed that is possible with the citrate digestion ability that needed two successive mutations.
2. stable 3D structured proteins are extremely rare in sequence space … so rare that scientists recognize it as futile to randomly search for them.
But we are back to the same point. You will have to clarify how one can make a claim about unsearched sequence space when it remains, well, unsearched. I would be amazed if blind search of sequence space will be any more productive than monkeys on typewriters. The holy grail of biochemistry would be a way of predicting functionality without having to synthesize and examine the properties of a previously unknown protein.
My own work coupled with work done on estimating the number of different protein folds, indicates that these stable, 3D structured protein families are so rare...
I'd be most interested in the evidence and methods that brought you to that conclusion. Is it in a specific paper that is available on-line?
No sane person who, having understood the design requirements for even the ribosome, could for an instant even entertain the absurd notion that some sort of evolutionary search could cobble that together,...
I can't rule out the possibility that I am insane and nobody around me has noticed but there may be others who have still not given up on the possibility of evolutionary explanations. Three billion years and unimaginably large populations of rapidly turning over prokaryotes is a big laboratory in which to test the basic chemistry, which all seems to have been in place proir to the diversification into sexually reproducing eukaryotes and beyond into multi-cellularity.
If 9 out of 10 random sequences of amino acids perform some sort of binding function, then why is it that life seems to have ignored them and gone for a set of tens of thousands of globular proteins which we know (and all our science verifies this) are mind-boggling rare in sequence space.
We don't know what proteins were in use by organisms that have left no trace of DNA to examine. For all we know, different proteins were in use and were superseded. Regarding globulins, a paper that covers the issue of how to estimate their rarity as functional proteins would be most appreciated, as noted above.
...we must conclude that the kind of proteins life requires are far more sophisticated and rare than mere random sequences of amino acids that bind to something in the lab.
I don't think we can be so cut-and-dried. For one thing, we don't know what transitionals may have existed back in that 3 billion years or so for which we have no direct evidence. But thanks for taking the time to respond and I'll look out for any further comments.Alan Fox
August 7, 2013
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