Live stream of the Nelson–Velasco debate – NOW

_{Denyse O'Leary

March 29, 2014

Intelligent Design, News, Tree of life}

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Further to “Nelson-Velasco debate: Hold it despite opposition. Anything else is “fascism,” says prof,” here’s the live stream of the debate (presumably when it starts, at 3:00 pm EST).

By the way, in case you happen to hear, during the debate, that “Creationists will be the death of science” or some such, get this, from genetcisit Todd Wood’s blog:

I just got back from the Bryan College Undergraduate Research Conference. I’m teaching an adjunct class this semester to bio majors, and two of my students were presenting. …

[evil creationists, see?]

After the conference, the department chair took me aside and shared with me the results from the latest standardized testing of the senior biology majors. The test splits up their scores in four categories: cell, organismal, genetics, and evolution. To my absolute delight, Bryan College students scored in the 99th percentile – in the evolution category! That was their highest category too. Uh oh! Who’s been teaching them evolution? Well, that would be me. The class I’m teaching this semester is called “History of Life,” which is just a euphemism for evolutionary biology. I teach straight from Freeman and Herron’s Evolutionary Analysis, and we read Darwin’s Origin of Species during the class. The students know my position on origins, and when appropriate, I bring in creationist commentary. But for the most part, it’s straight evolutionary biology. The 99th percentile means they’re outperforming most students taught by actual evolutionists.

The fact that lots of people don’t believe that a pile of kindling is a Tree of Life, doesn’t mean they can’t answer questions about what’s in the book advocating that view.

The problem is more with what’s in the book.

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Comments

Unpleasant only because you can't deal with someone who calls you on your BS. I'm sure you don't get that a lot when you cater to the scientifically illiterate. Have a nice night. <3AVS_{March 29, 2014
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Well AVS, that's enough insult for me tonight. You are a very unpleasant person to deal with. But anyways, May the God who created you, fearfully and wonderfully, bless you richly!bornagain77_{March 29, 2014
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No, the answer I got was that you had no idea what you were talking about and probably haven't even read the paper. Is that what you're doing now while you copy and paste more nonsense? Seriously, waht do those two articles have to do with the conversation. It would help if you added some of your own dialogue to your copy and paste posts. And it would definitely make me feel like you actually read the articles you are quoting.AVS_{March 29, 2014
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I'm not sure what your problem with wiki is. It is obviously not a reliable source if I am writing a scientific paper, but for you guys it does its job very well and I would venture a guess that wiki is over 90% accurate for everything it says. Now as you'll notice I quoted wiki four times, Joe, all of them supporting me. You took the first sentence of the page because it helped your argument. Obviously the first sentence is going to list everything that chaperones do. Now if you'll look at my four quotes, you'll see that helping proteins fold is not the only thing that chaperones do, in fact it is only a small portion of what chaperones do. You'll also notice that it says something about most proteins being able to fold on their own. Ring any bells? Also notice how the paper you cited is specifically talking about chaperones that aid protein folding. Of course they are going to mention the fact that chaperones help proteins fold. For the last time, the majority of chaperones do not help proteins fold. They serve many other functions and only a fraction off all proteins require chaperones to fold correctly.AVS_{March 29, 2014
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AVS, "To which I got the answer I was looking for anyway" Let me guess, Let me guess,,, The answer you knew beforehand was 'Evolution did it'! Human Genes: Alternative Splicing (For Proteins) Far More Common Than Thought: Excerpt: two different forms of the same protein, known as isoforms, can have different, even completely opposite functions. For example, one protein may activate cell death pathways while its close relative promotes cell survival. http://www.sciencedaily.com/releases/2008/11/081102134623.htm Genes Code For Many Layers of Information - They May Have Just Discovered Another - Cornelius Hunter - January 21, 2013 Excerpt: “protein multifunctionality is more the rule than the exception.” In fact, “Perhaps all proteins perform many different functions by employing as many different mechanisms." http://darwins-god.blogspot.com/2013/01/genes-code-for-many-layers-of.htmlbornagain77_{March 29, 2014
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Ah yes, the ol' "demonstrate the origination of a molecular machine" demands. I knew you'd go back to your old ways. You are quite the character. I don't think anybody is a fool for doubting anything. I think they're a fool when they ignore facts and live in a fantasy world. I asked you a simple question at the start and you have failed to answer it multiple times. You aren't going to go through the details because you either didn't read the paper or you don't understand it. And yet you chose to try to use it as evidence for your argument. I was simply being skeptical, and asked a question. To which I got the answer I was looking for anyways.AVS_{March 29, 2014
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Wikipedia:
In molecular biology, molecular chaperones are proteins that assist the non-covalent folding or unfolding and the assembly or disassembly of other macromolecular structures.
Joe_{March 29, 2014
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Only small proteins can fold on their own and the median length is well over that limit.Joe_{March 29, 2014
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OH goody we got the smug Darwinian expert quoting wiki to us now! Perhaps he can find some help from talkorigins while he is at it! :)bornagain77_{March 29, 2014
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Really AVS- are you talking about blind watchmaker evolution? If so please do elaborate.Joe_{March 29, 2014
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Wikipedia? Really? Protein Folding and Chaperones
Abstract Proteins fold via specific pathways to achieve their native structure. Protein structures are, however, inherently unstable; hence folding and unfolding are in equilibrium. Protein instability is a major concern inside the cell. Specialised proteins called molecular chaperones are, therefore, required to assist proteins in folding and to prevent aggregation of folding intermediates. Many different classes of chaperones exist that are conserved throughout all kingdoms of life, many of which are known as heat?shock proteins. Chaperones typically recognise hydrophobic patches, but the exact functions and mechanisms of action of the various chaperone classes are very different. The main chaperone classes Hsp70, Hsp90, Hsp100 and chaperonins all depend on adenosine triphosphatase (ATPase) cycles, which enable subtle activity control by co?chaperones. The molecular understanding of the mechanism of both chaperones and protein folding are key problems in today's life sciences. The importance is illustrated by the fact that many diseases are associated with these processes.
Joe_{March 29, 2014
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Really Joe? You should just see yourself out now. Quit while your ahead bud. But not reallyAVS_{March 29, 2014
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Why yes AVS, Darwinism can do all things. Even things that are completely antithetical to basic precepts of Darwinism, and you think everybody else is a fool for doubting Darwinism even though you cannot demonstrate the origination of a single molecular machine by Darwinian processes. Go figure. I call it making excuses! PS, why in blue blazes do you keep asking me my opinion on the paper when you already think you know all the answers? I'm certainly not going to go through the details with you, especially considering the typical condescending way you treat people who disagree with you.bornagain77_{March 29, 2014
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Joe, you are on the internet. Go to the wiki page for chaperones..you know what I'll do it for you. Here are some excerpts: "The common perception that chaperones are concerned primarily with protein folding is incorrect." "One major function of chaperones is to prevent both newly synthesised polypeptide chains and assembled subunits from aggregating into nonfunctional structures." Only a small subset of chaperones are highly specific 'steric chaperones' and convey unique structural (steric) information onto proteins, which cannot be folded spontaneously " Other chaperones are involved in folding newly made proteins as they are extruded from the ribosome. Although most newly synthesized proteins can fold in absence of chaperones, a minority strictly requires them for the same." Did you get that? MOST proteins can fold on their own. A MINORITY require chaperones. Don't go by what your high school biology book said, it made the mistake of over simplifying things for the laypeople.AVS_{March 29, 2014
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What does "over the course of evolution" mean?Joe_{March 29, 2014
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So you're abandoning our first topic and bringing up a bacteria that can both live in an extreme environment and is able to repair its genome? Hmmm...do we really find that odd? You might want to plug your ears for this, but I would assume that over the course of evolution, an organism that is now able to live in an extreme environment would be pretty good at repairing its DNA, keeping proteins folded, and maintaining cellular integrity. No? Call me crazy.AVS_{March 29, 2014
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Chaperones are used to get proteins to fold- long proteins. IOW you are wrong again.Joe_{March 29, 2014
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So AVS, sequential information is primary in your book? Explain how the following is possible from the reductive materialistic framework of neo-Darwinism: Extreme Genome Repair - 20 March 2009 Excerpt: If its naming had followed, rather than preceded, molecular analyses of its DNA, the extremophile bacterium Deinococcus radiodurans might have been called Lazarus. After shattering of its 3.2 Mb genome into 20–30 kb pieces by desiccation or a high dose of ionizing radiation, D. radiodurans miraculously reassembles its genome such that only 3 hr later fully reconstituted nonrearranged chromosomes are present, and the cells carry on, alive as normal. http://www.sciencedirect.com/science/article/pii/S0092867409002657bornagain77_{March 29, 2014
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Very rarely are chaperones needed for correct protein folding. Chaperones are much more often used to hold proteins in their unfolded form so that they can be translocated into organelles such as the mitochondria. They are also often used in times of stress to stop unfolded proteins from aggregating. Prions are a rare case of protein aggregation, and in my opinion are a good example of what I would call "poor design." Anything else you guys care to be wrong about?AVS_{March 29, 2014
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I'm downplaying the problem? What problem is that? Fig. 4? Where's that? Oh you copy and pasted again, gotcha. All I'm saying is that a lot of proteins are completely capable of folding on their own, driven by interactions of the primary sequence, without the help of chaperones. The folding of cytosolic and secreted proteins is governed by the burying of hydrophobic residues within the core of the protein and by the electrostatic interactions between charged residues. Each amino acid also tends to have certain bond rotation angles which are more entropically favorable, often driving the protein folding in certain directions. Proteins with multiple domains typically fold in a stepwise fashion, not all at one. The vast majority of protein folding is governed by the amino acid sequence, which is the direct product of translation of the nucleotide sequence. Now for the last time, is the source you originally cited trying to say that this is not true? Or is it that you have no idea what you are talking about. Or both?AVS_{March 29, 2014
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Yes the nucleotide sequence of a protein coding gene has an effect on the shape. However many proteins require chaperones in order for them to find their shape. And without chaperones they would just be like wet spaghetti, just a lot smaller. That means you need the right amino acid sequence AND the right chaperone(s) to get the required protein. And even then prions demonstrate that existing proteins can take on new/ different shapeJoe_{March 29, 2014
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AVS, you are downplaying the problem. Why? This understanding of protein folding was obtained from computer models (in silico) or from experiments in the laboratory (in vitro) in which an individual protein was denatured to observe it folding back into its original form. But, the situation is considerably more complex in the living cell (in vivo). Although the fundamental energy rules also apply here, folding at least of large proteins rarely takes place spontaneously, as the ribosomes do not synthesize only one protein at a time. Instead, cells contain a vast number of proteins and other biomolecules at the extraordinarily high concentration of 340 grams per litre. Ordered protein folding in this cramped chaos is only possible under the supervision of specialized molecules, called chaperones, which accompany proteins and make sure that those that are being formed at the ribosomes do not clump together prematurely (Fig. 4). Chaperones do not merely oversee the folding of the protein, they also protect its tertiary structure in situations in which the cell is under stress; for example, elevated body temperature, so these chaperones have also been classified as heat-shock proteins (HSPs).bornagain77_{March 29, 2014
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Whoa whoa whoa pump the brakes there BA. Was that a reply to my question? I can't tell, probably because 99% of it isn't even your own words. I'm going to ask one more time. Does that article you cited claim that the nucleotide sequence of a protein coding gene has no effect on the final shape of the protein? Did you even read the article? You do know that we can purify proteins, completely unfold them, and then refold them to their natural conformation right? Protein folding is largely driven by the amino acid sequence, which is entirely dependent on the nucleotide sequence within DNA. Do you have any idea what I am talking about and what you are trying to talk about?AVS_{March 29, 2014
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of note: Although it is possible to deduce the primary structure of a protein from a gene's sequence, its tertiary structure cannot be determined (although it should become possible to make predictions when more tertiary sequences are submitted to databases). It can only be determined by complex experimental analyses and, at present, this information is only known for about 10% of proteins. http://www.nature.com/horizon/proteinfolding/background/importance.html The primary structure of a peptide or protein is the linear sequence of its amino acid structural units, and partly comprises its overall biomolecular structure. http://en.wikipedia.org/wiki/Protein_primary_structure The term protein tertiary structure refers to a protein's geometric shape. http://en.wikipedia.org/wiki/Protein_tertiary_structure Francis Collins on Making Life Excerpt: 'We are so woefully ignorant about how biology really works. We still don't understand how a particular DNA sequence—when we just stare at it—codes for a protein that has a particular function. We can't even figure out how that protein would fold—into what kind of three-dimensional shape. And I would defy anybody who is going to tell me that they could, from first principles, predict not only the shape of the protein but also what it does.' - Francis Collins - Former Director of the Human Genome Project http://www.pbs.org/wgbh/nova/tech/collins-genome.html Protein folding makes Rubik's cube seem like child's play by comparison: The Humpty-Dumpty Effect: A Revolutionary Paper with Far-Reaching Implications - Paul Nelson - October 23, 2012 Excerpt: Put simply, the Levinthal paradox states that when one calculates the number of possible topological (rotational) configurations for the amino acids in even a small (say, 100 residue) unfolded protein, random search could never find the final folded conformation of that same protein during the lifetime of the physical universe. http://www.evolutionnews.org/2012/10/a_revolutionary065521.html Thus I re-reference the quantum protein folding paper: Physicists Discover Quantum Law of Protein Folding – February 22, 2011 Quantum mechanics finally explains why protein folding depends on temperature in such a strange way. Excerpt: First, a little background on protein folding. Proteins are long chains of amino acids that become biologically active only when they fold into specific, highly complex shapes. The puzzle is how proteins do this so quickly when they have so many possible configurations to choose from. To put this in perspective, a relatively small protein of only 100 amino acids can take some 10^100 different configurations. If it tried these shapes at the rate of 100 billion a second, it would take longer than the age of the universe to find the correct one. Just how these molecules do the job in nanoseconds, nobody knows.,,, Their astonishing result is that this quantum transition model fits the folding curves of 15 different proteins and even explains the difference in folding and unfolding rates of the same proteins. That’s a significant breakthrough. Luo and Lo’s equations amount to the first universal laws of protein folding. That’s the equivalent in biology to something like the thermodynamic laws in physics. http://www.technologyreview.com/view/423087/physicists-discover-quantum-law-of-protein/bornagain77_{March 29, 2014
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I'm sorry BA, is that first article in your last post trying to say that the nucleotide sequence of a protein-coding gene has no effect on the final shape of the protein?AVS_{March 29, 2014
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This following recent paper really brought this point home:
A challenge to the genetic interpretation of biology - Feb 19, 2014 When a gene, a string of bases on the DNA molecule, is deployed, it is first transcribed and then translated into a peptide – a string of amino acids. To give rise to biological properties it needs to "fold" into a protein. This process consumes energy and is therefore governed by the 2nd law, but also by the environment in which the folding takes place. These two factors mean that there is no causal relationship between the original gene coding sequence and the biological activity of the protein. http://phys.org/news/2014-02-genetic-biology.html
Moreover, this following paper shows that protein folding is, in large measure, governed by 'spooky' quantum processes, and is not governed solely by 'classical' processes.
Physicists Discover Quantum Law of Protein Folding – February 22, 2011 Quantum mechanics finally explains why protein folding depends on temperature in such a strange way. Excerpt: First, a little background on protein folding. Proteins are long chains of amino acids that become biologically active only when they fold into specific, highly complex shapes. The puzzle is how proteins do this so quickly when they have so many possible configurations to choose from. To put this in perspective, a relatively small protein of only 100 amino acids can take some 10^100 different configurations. If it tried these shapes at the rate of 100 billion a second, it would take longer than the age of the universe to find the correct one. Just how these molecules do the job in nanoseconds, nobody knows.,,, Their astonishing result is that this quantum transition model fits the folding curves of 15 different proteins and even explains the difference in folding and unfolding rates of the same proteins. That's a significant breakthrough. Luo and Lo's equations amount to the first universal laws of protein folding. That’s the equivalent in biology to something like the thermodynamic laws in physics. http://www.technologyreview.com/view/423087/physicists-discover-quantum-law-of-protein/
The failure of 'form' to be reduced to neo-Darwinian processes is not just some minor nitpicking on neo-Darwinian processes but is a failure for neo-Darwinism at the most basic level of explanation for what it seeks to explain. Namely that there is a correspondence to the linear sequences on DNA and form. I think Talbott has dome a excellent job of elucidating just how problematic trying to explain 'form' is for Darwinists:
HOW BIOLOGISTS LOST SIGHT OF THE MEANING OF LIFE — AND ARE NOW STARING IT IN THE FACE - Stephen L. Talbott - May 2012 Excerpt: “If you think air traffic controllers have a tough job guiding planes into major airports or across a crowded continental airspace, consider the challenge facing a human cell trying to position its proteins”. A given cell, he notes, may make more than 10,000 different proteins, and typically contains more than a billion protein molecules at any one time. “Somehow a cell must get all its proteins to their correct destinations — and equally important, keep these molecules out of the wrong places”. And further: “It’s almost as if every mRNA [an intermediate between a gene and a corresponding protein] coming out of the nucleus knows where it’s going” (Travis 2011),,, Further, the billion protein molecules in a cell are virtually all capable of interacting with each other to one degree or another; they are subject to getting misfolded or “all balled up with one another”; they are critically modified through the attachment or detachment of molecular subunits, often in rapid order and with immediate implications for changing function; they can wind up inside large-capacity “transport vehicles” headed in any number of directions; they can be sidetracked by diverse processes of degradation and recycling... and so on without end. Yet the coherence of the whole is maintained. The question is indeed, then, “How does the organism meaningfully dispose of all its molecules, getting them to the right places and into the right interactions?” The same sort of question can be asked of cells, for example in the growing embryo, where literal streams of cells are flowing to their appointed places, differentiating themselves into different types as they go, and adjusting themselves to all sorts of unpredictable perturbations — even to the degree of responding appropriately when a lab technician excises a clump of them from one location in a young embryo and puts them in another, where they may proceed to adapt themselves in an entirely different and proper way to the new environment. It is hard to quibble with the immediate impression that form (which is more idea-like than thing-like) is primary, and the material particulars subsidiary. Two systems biologists, one from the Max Delbrück Center for Molecular Medicine in Germany and one from Harvard Medical School, frame one part of the problem this way: "The human body is formed by trillions of individual cells. These cells work together with remarkable precision, first forming an adult organism out of a single fertilized egg, and then keeping the organism alive and functional for decades. To achieve this precision, one would assume that each individual cell reacts in a reliable, reproducible way to a given input, faithfully executing the required task. However, a growing number of studies investigating cellular processes on the level of single cells revealed large heterogeneity even among genetically identical cells of the same cell type. (Loewer and Lahav 2011)",,, And then we hear that all this meaningful activity is, somehow, meaningless or a product of meaninglessness. This, I believe, is the real issue troubling the majority of the American populace when they are asked about their belief in evolution. They see one thing and then are told, more or less directly, that they are really seeing its denial. Yet no one has ever explained to them how you get meaning from meaninglessness — a difficult enough task once you realize that we cannot articulate any knowledge of the world at all except in the language of meaning.,,, http://www.netfuture.org/2012/May1012_184.html#2
All of which begs the question, if Darwinists cannot give a coherent explanation for how even one organism is achieving its final 'form' during it's embryological development, then what in blue blazes gives Darwinists the audacity to tell us that they know for a fact how all life originated on earth?
Scant search for the Maker Excerpt: But where is the experimental evidence? None exists in the literature claiming that one species has been shown to evolve into another. Bacteria, the simplest form of independent life, are ideal for this kind of study, with generation times of 20 to 30 minutes, and populations achieved after 18 hours. But throughout 150 years of the science of bacteriology, there is no evidence that one species of bacteria has changed into another, in spite of the fact that populations have been exposed to potent chemical and physical mutagens and that, uniquely, bacteria possess extrachromosomal, transmissible plasmids. Since there is no evidence for species changes between the simplest forms of unicellular life, it is not surprising that there is no evidence for evolution from prokaryotic to eukaryotic cells, let alone throughout the whole array of higher multicellular organisms. - Alan H. Linton - emeritus professor of bacteriology, University of Bristol. http://www.timeshighereducation.co.uk/story.asp?storycode=159282
Verse and Music:
Psalm 139:13 For you created my inmost being; you knit me together in my mother's womb. Mandisa - Esther - Born For This - music video http://www.youtube.com/watch?v=ZxFCber4TDo
bornagain77_{March 29, 2014
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I thought Dr. Nelson, considering the limited time in such a format, did a fine job in today's debate. Dr. Velasco, for his part, seemed to think simply 'believing' in common descent is more important than an actual empirical demonstration that his proposed Darwinian mechanism of Natural Selection and Random Variation/Mutation is up to the task he has attributed to it. Dr. Nelson clearly showed to the audience that his proposed Darwinian mechanism of Natural Selection and Random Variation/Mutation is NOT up to the task he has attributed to it. Dr. Nelson's main point was a condensed version of this talk:
Darwin or Design? – Paul Nelson at Saddleback Church – Nov. 2012 – ontogenetic depth (excellent update) – video Text from one of the Saddleback slides: 1. Animal body plans are built in each generation by a stepwise process, from the fertilized egg to the many cells of the adult. The earliest stages in this process determine what follows. 2. Thus, to change — that is, to evolve — any body plan, mutations expressed early in development must occur, be viable, and be stably transmitted to offspring. 3. But such early-acting mutations of global effect are those least likely to be tolerated by the embryo. Losses of structures are the only exception to this otherwise universal generalization about animal development and evolution. Many species will tolerate phenotypic losses if their local (environmental) circumstances are favorable. Hence island or cave fauna often lose (for instance) wings or eyes. http://www.saddleback.com/mc/m/7ece8/ Response to John Wise - October 2010 Excerpt: A technique called "saturation mutagenesis"1,2 has been used to produce every possible developmental mutation in fruit flies (Drosophila melanogaster),3,4,5 roundworms (Caenorhabditis elegans),6,7 and zebrafish (Danio rerio),8,9,10 and the same technique is now being applied to mice (Mus musculus).11,12 None of the evidence from these and numerous other studies of developmental mutations supports the neo-Darwinian dogma that DNA mutations can lead to new organs or body plans--because none of the observed developmental mutations benefit the organism. http://www.evolutionnews.org/2010/10/response_to_john_wise038811.html
and this talk:
The Miracle of Development Part 1 - Origins with Dr. Paul A. Nelson - video - April 2013 http://www.youtube.com/watch?v=JD9qMvz6T90 The Miracle of Development Part 2 - Origins with Dr. Paul A. Nelson - video - April 2013 http://www.youtube.com/watch?v=Vz12PI3BkQ4
Darwinists simply do not have any empirical evidence that Darwinian processes can produce changes in body plans. Moreover, there is now a fairly strong case to be made that body plans are not reducible to the linear sequences on DNA, as is presupposed in neo-Darwinism, but that 'structural information' is its own separate source of information:
“Live memory” of the cell, the other hereditary memory of living systems - 2005 Excerpt: To understand this notion of “live memory”, its role and interactions with DNA must be resituated; indeed, operational information belongs as much to the cell body and to its cytoplasmic regulatory protein components and other endogenous or exogenous ligands as it does to the DNA database. We will see in Section 2, using examples from recent experiments in biology, the principal roles of “live memory” in relation to the four aspects of cellular identity, memory of form, hereditary transmission and also working memory. http://www.ncbi.nlm.nih.gov/pubmed/15888340 Not in the Genes: Embryonic Electric Fields - Jonathan Wells - December 2011 Excerpt: although the molecular components of individual sodium-potassium channels may be encoded in DNA sequences, the three-dimensional arrangement of those channels -- which determines the form of the endogenous electric field -- constitutes an independent source of information in the developing embryo. http://www.evolutionnews.org/2011/12/not_in_the_gene054071.html
This following peer-reviewed paper holds that there is a 'irreducible organizational complexity' between genetic (digital) information and epigenetic (analog/structural) information:
Refereed scientific article on DNA argues for irreducible complexity - October 2, 2013 Excerpt: This paper published online this summer is a true mind-blower showing the irreducible organizational complexity (author’s description) of DNA analog and digital information, that genes are not arbitrarily positioned on the chromosome etc.,, ,,,First, the digital information of individual genes (semantics) is dependent on the the intergenic regions (as we know) which is like analog information (syntax). Both types of information are co-dependent and self-referential but you can’t get syntax from semantics. As the authors state, “thus the holistic approach assumes self-referentiality (completeness of the contained information and full consistency of the different codes) as an irreducible organizational complexity of the genetic regulation system of any cell”. In short, the linear DNA sequence contains both types of information. Second, the paper links local DNA structure, to domains, to the overall chromosome configuration as a dynamic system keying off the metabolic signals of the cell. This implies that the position and organization of genes on the chromosome is not arbitrary,,, http://www.christianscientific.org/refereed-scientific-article-on-dna-argues-for-irreducibly-complexity/
The following papers hold that the genotype-phenotype mapping cannot be reduced to a genetic program encoded in DNA sequences:
Not Junk After All—Conclusion - August 29, 2013 Excerpt: Many scientists have pointed out that the relationship between the genome and the organism — the genotype-phenotype mapping — cannot be reduced to a genetic program encoded in DNA sequences. Atlan and Koppel wrote in 1990 that advances in artificial intelligence showed that cellular operations are not controlled by a linear sequence of instructions in DNA but by a “distributed multilayer network” [150]. According to Denton and his co-workers, protein folding appears to involve formal causes that transcend material mechanisms [151], and according to Sternberg this is even more evident at higher levels of the genotype-phenotype mapping [152]. https://uncommondescent.com/junk-dna/open-mike-cornell-obi-conference-chapter-11-not-junk-after-all-conclusion/ The Types: A Persistent Structuralist Challenge to Darwinian Pan-Selectionism - Michael J. Denton - 2013 Excerpt: Cell form ,,,Karsenti comments that despite the attraction of the (genetic) blueprint model there are no “simple linear chains of causal events that link genes to phenotypes” [77: p. 255]. And wherever there is no simple linear causal chain linking genes with phenotypes,,,—at any level in the organic hierarchy, from cells to body plans—the resulting form is bound to be to a degree epigenetic and emergent, and cannot be inferred from even the most exhaustive analysis of the genes.,,, To this author’s knowledge, to date the form of no individual cell has been shown to be specified in detail in a genomic blueprint. As mentioned above, between genes and mature cell form there is a complex hierarchy of self-organization and emergent phenomena, rendering cell form profoundly epigenetic. http://bio-complexity.org/ojs/index.php/main/article/view/BIO-C.2013.3/BIO-C.2013.3
bornagain77_{March 29, 2014
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From now on, anyone who doesn't understand evolutionary theory needs only to ask the biology graduates of Brian College, or perhaps Todd Wood. I'm sure they will straighten him/her out. :DPaul Giem_{March 29, 2014
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Well loss of intellectual integrity, or indeed, a quasi-amoral ignorance of the very concept of intellectual integrity will necessarily wreak damage on the atheists' capacity for conceptual thought, and indeed, will continue to do so exponentially. Dumber and dumber. Hence, the named, mad professors who figure so much on UD as, well.. mad professors. The phenomenon is very apparent in the UK, with the result that a place in private religious schools is coveted by upwardly-mobile parents for their sprogs, and will even move home, to be close to the school in question, meet an important qualification criterion. Truth is stranger than fiction, but, faced with this shame, militant atheists are always clamouring for the religious schools to be closed down... on the grounds that they instil religious bigotry!!!!Axel_{March 29, 2014
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Warms my heart. I once represented a young college student who had been humiliated by her Darwinist prof. She announced that she should not have to learn Darwinian theory at all. I said to her that while I would defend her legal rights, I disagreed with that statement. I told her that as an anti-Darwinist she had an obligation to understand Darwinism better than the Darwinist she would inevitably encounter. How can she critique a theory she did not understand? Smug Darwinists (I sometimes wonder if there is any other kind) often tell me the only reason I disagree with them is that I don't understand the theory. I take delight (is that delight perverse? I'll let others decide) smacking that particular trope down every time it raises its ugly little whack-a-mole head.Barry Arrington_{March 29, 2014
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