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Ascertaining Non-Function

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One of the main arguments to support evolution appeals to shared non-functional structures between organisms. Since design entails design for function, shared non-functional structures would suggest common ancestry in the absence of common design. But how can we tell whether something is truly non-functional? Here are some insights from a colleague that address this point:

As a programmer, sometimes I spend a lot of time designing error-detection and/or error-correction algorithms (especially for dealing with user input). Some of these functions may never, ever be used in a real-life situation. There are also various subroutines and functions that provide either exotic or minor capabilities that, likewise, maybe be used very seldom if at all. But they are there for a reason. Good programming practice requires considerable extra design and implementation of features that may only rarely, if ever, be used.

If someone were to cut out and eliminate these sections of code, repairing what’s left so that the program still functions, the program may work perfectly well for just about all situations. But there are some situations that, without the snipped code, would create havoc if the program tried to call on a function that was no longer there or that was replaced by some different function that tried to take its place. (Ask yourself what percent of the functionality of your spreadsheet or word processor program you use, and then ask if you would even notice if some of the lesser-known functionality were removed.)

I think biological life is like that. It seems to me that if some DNA code can be successfully removed with no apparent effects, one possibility is that the removed portion is rarely used, or the impact of it not being there has effects that are masked or otherwise hidden.

Perhaps redundancy is what was removed, meaning the organism will now not be quite as robust in all situations as before. I can give a kidney to someone else and suffer no ill effect whatsoever… until my remaining kidney fails and cannot be helped by the redundant one that I gave up (which situation may never, ever really occur due to my general good health).

P.S. Being able to snip something with no apparent ill effect may in fact provide support for ID by showing that the system was so well engineered that it could automatically adjust to a certain degree, and in most cases completely (apparently). It would be interesting to see some ID research into some of the evo cases that are being used to support the various flavors of junk DNA, to see what REALLY happens long term with the new variety now missing something snipped.

Comments
PPS: pardon, Cytosine Ckairosfocus
August 20, 2009
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PS: This, from Wiki on folding of proteins bears emphasis [they cannot hide EVERYTHING . . . ], given the dismissive tendencies of our resident Darwinists once confronted withthe fact of FSCI: _________ >> The essential fact of folding, however, remains that the amino acid sequence of each protein contains the information that specifies both the native structure and the pathway to attain that state >> ______________ (And of course, in turn, that functionally specific and complex information traces to the codon sequence in the DNA string that is templated by mRNA and sequentially read codon by codon in the ribosome, with tRNA's supplying the AA chain, from START to STOP.)kairosfocus
August 20, 2009
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Nakashima-san: I think you need to look at how the Dryden et al Abstract begins: "We suggest . . ." In short, the paper is long on speculation, short on substance. In fact protein folding is an extremely complex computational challenge, and with the existence of prions as known misfolding based diseases [scrapies, mad cow disease], we know that there are not unique and simple solutions tot he folding. (Observe how in vitro folding is aided post-chaining by chaperoning molecules.) Wiki, on prions:
A prion (pronounced /?pri?.?n/ ( listen)[1]) is an infectious agent that is composed of protein. To date, all such agents that have been discovered propagate by transmitting a mis-folded protein state; the protein does not itself self-replicate and the process is dependent on the presence of the polypeptide in the host organism.[2] The mis-folded form of the prion protein has been implicated in a number of diseases in a variety of mammals, including bovine spongiform encephalopathy (BSE, also known as "mad cow disease") in cattle and Creutzfeldt-Jakob disease (CJD) in humans. All known prion diseases affect the structure of the brain or other neural tissue, and all are currently untreatable and are always fatal.[3] In general usage, prion refers to the theoretical unit of infection. In scientific notation, PrPC refers to the endogenous form of prion protein (PrP), which is found in a multitude of tissues, while PrPSC refers to the misfolded form of PrP, that is responsible for the formation of amyloid plaques that lead to neurodegeneration. Prions are hypothesized to infect and propagate by refolding abnormally into a structure which is able to convert normal molecules of the protein into the abnormally structured form. All known prions induce the formation of an amyloid fold, in which the protein polymerises into an aggregate consisting of tightly packed beta sheets. This altered structure is extremely stable and accumulates in infected tissue, causing tissue damage and cell death.[4] This stability means that prions are resistant to denaturation by chemical and physical agents, making disposal and containment of these particles difficult.
Similarly, Wiki on Protein folding:
The amino-acid sequence (or primary structure) of a protein defines its native conformation. A protein molecule folds spontaneously during or after synthesis. While these macromolecules may be regarded as "folding themselves", the process also depends on the solvent (water or lipid bilayer),[5] the concentration of salts, the temperature, and the presence of molecular chaperones. Folded proteins usually have a hydrophobic core in which side chain packing stabilizes the folded state, and charged or polar side chains occupy the solvent-exposed surface where they interact with surrounding water. Minimizing the number of hydrophobic side-chains exposed to water is an important driving force behind the folding process,[6]. Formation of intramolecular hydrogen bonds provides another important contribution to protein stability.[7]The strength of hydrogen bonds depends on their environment, thus H-bonds enveloped in a hydrophobic core contribute more than H-bonds exposed to the aqueous environment to the stability of the native state.[8] . . . . The essential fact of folding, however, remains that the amino acid sequence of each protein contains the information that specifies both the native structure and the pathway to attain that state. This is not to say that nearly identical amino acid sequences always fold similarly.[10] Conformations differ based on environmental factors as well; similar proteins fold differently based on where they are found. Folding is a spontaneous process independent of energy inputs from nucleoside triphosphates. The passage of the folded state is mainly guided by hydrophobic interactions, formation of intramolecular hydrogen bonds, and van der Waals forces, and it is opposed by conformational entropy . . . . De novo or ab initio techniques for computational protein structure prediction is related to, but strictly distinct from, studies involving protein folding. Molecular Dynamics (MD) is an important tool for studying protein folding and dynamics in silico. Because of computational cost, ab initio MD folding simulations with explicit water are limited to peptides and very small proteins. MD simulations of larger proteins remain restricted to dynamics of the experimental structure or its high-temperature unfolding. In order to simulate long time folding processes (beyond about 1 microsecond), like folding of small-size proteins (about 50 residues) or larger, some approximations or simplifications in protein models need to be introduced. An approach using reduced protein representation (pseudo-atoms representing groups of atoms are defined) and statistical potential is not only useful in protein structure prediction, but is also capable of reproducing the folding pathways.[17]
Bearing that in mind, we should then read with a fairly critical eye, and make a few annotations: ______________ >> Before turning to a discussion of the second assumption, we wish to summarize information showing [a word that usually calls for something demonstrative, empirical or logical or both . . . not "suggestions," material gaps and speculations . . .] the first assumption, namely that the sequence space is vast, to be false. A typical estimate of the size of sequence space is 20^100 (approx. 10^130) for a protein of 100 amino acids in which any of the normally occurring 20 amino acids can be found. [the number is based on the possibilities of chaining AA's in essentially any order, i.e. any AA can be followed by any other due tot he basic AA structure: H2N-CR-COOH, so the acid and amine groups can chain with very little reference to the R side-group. It is the R group that gives functional properties to the AA.] This number is indeed gigantic but it is likely to be a significant overestimate of the size of protein sequence space. [But, the issue is not PROTEIN sequence space but polypetide sequence space -- i.e what space is che3mically feasible for a chain of given length, not what space is actually used by biologically observed proteins . . . i.e this is begging the question that is at stake; and of course is a dig at the Durson metric; based on q-begging Cf. my discussion of FSCI, the search space and "hypothesine" in light of the sequences actually used for Cytochrome-C]] For example, Dill and colleagues used simple theoretical models to suggest (Lau & Dill 1990; Chan & Dill 1991; Dill 1999), and experimental or computational variation of protein sequence provides ample evidence (Cordes et al. 1996; Riddle et al. 1997; Plaxco et al. 1998; Larson et al. 2002; Guo et al. 2004; Doi et al. 2005), that the actual identity of most of the amino acids in a protein is irrelevant. [Not os; in remarking on Cytosine-C, a commonly studied protein of about 100 AA's that is used for taxonomic research, I noted that it "typically varies across 1 - 5 AA's in each position, with a few AA positions showing more variability than that. About a third of the AA positions are invariant across a range from humans to rice to yeast. That is, the observed variability, if scaled up to 232 AA's [for the "hypothesine" model used int eh discussion], would be well within the 10^150 limit suggested; as, e.g. 5^155 ~ 2.19 * 10^108." In short, Dryden et al are playing two sides of the issue: where AA positions are pinned to one or a few molecule possibilities, that drops "protein sequence space" and where relatively wide variability may ne observed, that means that AA sequence is "irrelevant." That "logic with a swivel" approach sounds rather like the conclusion was written before the argument was made and before the evidence was seriously consulted.] >> ________________ In short, there is much more to the story than this paper presents. GEM of TKIkairosfocus
August 20, 2009
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Since DNA seems to contain something similar to computer code (software), and computer code can only be created by intelligent agents, I think ID researchers should look for the actual instructions, in the form of program code, that make the DNA perform its different routines. That will require reverse engineering or decompilation of the DNA's "machine code" to get the source code. In the process of getting the source code, the smoking gun evidence for ID will be the historic discovery of the first "comments" line and what it says.rprado
August 19, 2009
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Mr Lamarck, Sorry, I'm not following your reference. Can you quote or link to the statement you are thinking of? This study, How much of protein sequence space has been explored by life on Earth? is an example of how thinking in terms of hydrophobic/hydrophillic, etc can collapse the search space.Nakashima
August 18, 2009
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Mr. Nak, "Suddenly the “alphabet” has collapsed from 20 to 2." I'm sure you don't think the rest of the FCSI doesn't matter though. There was the quote earlier, the interview, about how one base pair leads to another and another to make a statement.lamarck
August 18, 2009
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Lenoxus @ 25: So let's say, for instance, that our hypothesis for some of these knocked out regions that don't seem to affect global fitness is that they serve as error correction mechanisms for some obscure cellular function, as Dembski's programmer friend has suggested could be the case. If so, then if that error never occurs, the mechanism would never activate and thus never affect global fitness. To test this hypothesis we could either: A) Do a near infinite number of mutagenesis experiments to see if the area of interest begins to affect global fitness B) Directly investigate the area of interest based on it's coding and three-dimensional structure and try to find if it interacts with any other area of the genome. I would think option B would be more likely to generate a timely result. In other words, an experiment based on global fitness is not really any help here, since it's already been established that these regions can be knocked out without affecting fitness. One possibility is that this error correction mechanism only works during replication. It's so efficient and the system it acts on is so critical that an organism without it either nevers starts its life (is aborted at fertilization or meiosis for example), or simply doesn't manifest any error in the critical system at all and survives just fine.tragic mishap
August 18, 2009
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So is this now like an election? Each amino acid substitution gets one vote? Whoever gets the most votes becomes the rule and the rest are exceptions? lol, how many exceptions would it take to change the so-called "generality" you just described.tragic mishap
August 17, 2009
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KF-san, I was aware that I was only speaking in generalities, and that there are many exceptions to what I was saying.Nakashima
August 17, 2009
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Nakashima-san, I think you overlook that [a] enzymes have active region clefts, [b] 3-D structures based on chains can be destabilised by as few as one inner AA that is incompatible. For instance, think of a proline "aa" [technically an imino acid,I know] which will pin its location due to the internal binding back of the R-group to the N atom. Similarly, a hydrophilic or hydrophobic out of order will have adverse impacts on folding and function. there is a reason why life forms form proteins step by step per sequences of instructions. GEM of TKIkairosfocus
August 17, 2009
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I've heard of Colin Reeves in the GA field, though I don't know what he's published in the field since 2000.Nakashima
August 16, 2009
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Mr Lamarck, Yes, both of these studies, the long knockout and the ultra-conserved knockout, were for non-coding regions that wre interspersed with functional genes. I agree with your scepticism, once a previusly functional area starts to erode, it is harder and harder to come back to any kind of functionality, new or old. I'm not sure if we can generalize about genes. Certainly most genes today create proteins with very precise grooves, channels, etc and a pattern of electric charges on the surface. But rather than being the effect of specific amino acids in the primary structure ( the unfolded protein chain) a lot of this can be boiled down to the choice of hydrophobic versus hydrophillic amino acids. Suddenly the "alphabet" has collapsed from 20 to 2. There also even larger protein motifs, such as alpha sheets and beta coils. All of these mean that some AA changes due to a change in the DNA don't actually have much effect on the functionality of the protein. You might generalize that the AAs on the outside of the protein (after it folds into its final 3D tertiary structure) are the ones most likely to influence the FSCI calulation. However, the cube-square law gives us the clue that as proteins grow larger, relatively fewer on the surface, so the ratio of important to less important AAs will go down in larger proteins. (That is a very crude approximation, since a lot of proteins are far from spherical!) If DNA starts down the path towards disuse, I don't expect much to come of it. i think the time after a gene duplication event while both copies are still functional is crucial. The gene can wander in the neighborhood of its original function (as we have just shown, many sites are free to change without affecting function) and if it hits on a new function, great. That's how we got tri-color vision again. With frameshifts and inversions, there are examples even in English of palindromes, and two words which are the reverse of each other. Apparently it happens in the world of proteins also. Again, it might help to think in terms of a two letter (phobic/phillic) alphabet to see that it is less unlikely than out intuition might otherwise lead us to believe. This depends on how often the genetic code maps phobic to phobic and phillic to phillic when the triples are reversed. i don't know that off hand! :)Nakashima
August 16, 2009
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Missed this bit of News! Biologic Institute: New Talent, New Places Gosh and I thought they said ID was squished. Hmmmm, more talent joins in the pursuit of Design challenges. Fantastics, Congrats to all of you at UD and Discovery! No, you're not "big" yet, but you're attracting some of the brightest! WTG guys.DATCG
August 16, 2009
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What does a Darwinist call tonsils and appendices today btw? Has "vestigial organs" been removed from textbooks?DATCG
August 16, 2009
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Nakashima, The analogy can only take you so far if you're talking about an "advanced civilization" of aliens such as that mentioned by Richard Dawkins. As is the fancy of Darwin and his followers, one can make conjectures that are "reasonable" hypothetics and consider a more advanced species would have elimintated comments from any program of this type of analogy. These areas much like all the other areas that were predicted wrong by the Darwinist at the time can be simply out of reach right now of current understanding. Just like removing tonsils and an appendix does not kill or eliminate reprodutivity, this could be an areas where enough expertise simply does not recognize the value of information, just like they failed to recognize the value of formerly named "vestigial organs"DATCG
August 16, 2009
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tragic mishap:
Lenoxus, if a function were to be uncovered yet did not affect fitness, what would Darwinism be able to say about the origins of that function?
That's a very good question. However, it's my understanding that all functions affect fitness, if only in the slightest way. Even an organism's eye color can make a fitness difference. (Though maybe not its lung or liver color… hmm… maybe it would affect its perceived tastiness to predators?)Lenoxus
August 16, 2009
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Mr. Nak, I think you're talking about non coding regions interspersed within functional dna sequences? I know about that but I'm not sure if you disagree with me or not. The reason I'm skeptical about non-coding regions of the genomes eventually coming up with something meaningful is; natural selection isn't weeding out their mutations if they're truly non-functional. So they just become more and more non-FCSI based. Isn't it also true that a coding gene by and large has to have FCSI? That is, you can have a meaningless segment here and there, but thousands of parts of real meaningful language need to line up. So how can dna go further and further towards chaos and you expect something to come of it? This is a related question to what I said on the whale evolution thread. How can a large frameshift, or an inversion, where all the base pair switched partners, even remotely come close to coding for something? Yet this is observed to happen a lot of times. Making I'm missing something fundamental here?lamarck
August 16, 2009
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Lenoxus, if a function were to be uncovered yet did not affect fitness, what would Darwinism be able to say about the origins of that function?tragic mishap
August 16, 2009
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bFast: Actually, that report was on a different study; the one you are probably thinking of was reported by Science Daily here. Indeed, as an evolutionist, I have to say that that particular study, first brought to my attention here at UD (unless that was yet another study!), is incredible, and seemingly difficult to reconcile with basic common descent; the interviewed scientists themselves seem startled. (I have since read about GRNs and suchlike, but can't claim to fully understand them.) That said, I'm not aware of any IDer who specifically predicted something like this in advance — instead, the repeated insistence has been that there is zero or close to zero non-functional DNA, on the assumption that the designer is responsible for the whole genome and therefore wouldn't waste any of it. (In the usual narrative, it's always the evolutionists who refuse to see the possible purposes of this or that portion of the genome, instead close-mindedly sequestering it as junk forevermore.) The funny thing about this study is that in order to use it as evidence against ordinary evolution, the relevant DNA must always remain truly non-functional in terms of fitness value to its current species, because otherwise its conserved-ness would no longer be a mystery. Even then, though, it remains merely a mystery, and not evidence for ID. In order for it to be evidence for ID, its design purpose must roughly be shown or inferrable — for example, perhaps it encodes a mathematical sequence, or functions as the "program comments". (That would certainly fit well with Remine's Message Theory.)Lenoxus
August 16, 2009
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To contunue with the programming analogy, there are also blocks of comments and commented out code which are guaranteed non-functional, as well as code that analysis can prove is impossible to reach. Counting accumulated spelling errors in these areas would be similar to what is proposed for non-coding DNA.Nakashima
August 16, 2009
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Mr Lamarck, In the case of a duplicate gene, at first both genes are working, neither is junk. Later mutation might cause one of them to become non-functional or shift to a different function, coding for a different protein. You are correct that is one copy becomes non-functional, the theory is that it will start to accumulate more mutations at some background rate, thereby providing a clock of sorts that started ticking when it lost function.Nakashima
August 16, 2009
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Regarding the so-called non-function, non-coded regions. I remember reading about Meta-Information or multi-layer information after the ENCODE project was done. There is for to much unknown still to determine why certain blocks or regions can be knocked out and yet not represent any known damage to a lab rat or mouse. It could be certain regions are only engaged based upon external stimuli of the environment. It could also be possible FrontLoading arrangements for future adaptations. As the Darwinist here are always fond of saying, just because we do not know now, does not mean we will not discover the answer in the future.DATCG
August 16, 2009
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PaulB, "It would indeed be interesting to see some ID research of any sort, particularly if the term “intelligent design” appeared in the article, and if the article appeared in an actual science journal." You mean besides Reverse Engineering of nature every single day? There was an attempt to publish an ID paper. Once the Darwinist found out, they acted like Hitler and Stalin. They squashed the attempt, acting like a bunch of fearful fascist Darwinist at Smithsonian and acted like thugs against Dr. Sternberg for his attempt at open discussion by Stephen Meyer. They should've lost their jobs, been reprimanded or dismissed to other areas. But this is the double-standards you live by. So, there is ID research going on at the Biologic Institute now where fascist cannot take peoples keys away and lock them out. What a joke. Darwinist are so scared of any information that counters them, they turn in to little Hitlers and burn books. Biologic Institute Research and Selected Publications Let me know Paul the day you write the Smithsonian Institute on behalf of Dr. Sternberg and strongly protest the fascist actions of the Darwinians in control there.DATCG
August 16, 2009
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Is this mouse study the same one DaveScot used to refer to all the time as an example disproving Darwinian evolution? On the page there is a similar study where by conserved parts of the genome were eliminated and the mice functioned just fine. So why was the conserved region still identical after 80 million years but when knocked out had no effect? Interesting!jerry
August 16, 2009
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Mr bFast, Yes, it seems to be the same lab as did the knockout of an ultra-conserved non-coding region.Nakashima
August 16, 2009
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What about darwinists postulating on the latent potential of duplicate genes etc becoming useful later? Isn't this considered junk DNA till functional? Seems like the harm would be less mutations per generation when you remove the junk, so it can't adapt?lamarck
August 16, 2009
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Nakashima, 2.3 million divided by 2.7 billion is only about 0.085%.Joseph
August 16, 2009
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Shared non-functional structures and common ancestry is counter-intuitive. I take it that is why it is used as evidence for it.Joseph
August 16, 2009
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Nakashima, interesting post. This report seems to be of the same experiment where much of the DNA which was knocked out was highly conserved. I find it interesting, and highly anti-Darwinian that highly conserved DNA could be knocked out of mice without the resultant animals showing ill effects.bFast
August 16, 2009
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Of course, thanks for the article. Dr. Dembski is suggesting we do research on the portions that were knocked out in experiments like this and investigate them for functions, perhaps taking as a clue advice from his programmer colleague.tragic mishap
August 16, 2009
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