Uncommon Descent Serving The Intelligent Design Community

Writing Biosemiosis.org

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In September of 2009 I started a new document on my computer entitled “A System of Symbols”, where I was going to write about the part of design theory that interested me the most – that is, the representations that are required for self-replication (von Neumann, Pattee). My goal was to inventory all the physical conditions necessary for one thing to represent another thing in a material universe. I wrote and rewrote that essay for more than four years — reading, learning, and sharing along the way. As it turns out, writing that essay was my way of coming to understand the issues, and I spent a great deal of that time trying to articulate things I had come to understand conceptually, but could not yet put into words. Eventually I came into contact with the types of scientists and researchers who had substantial experience with these issues, up to and including those who had spent their entire careers on the subject. It was a humbling experience to share my thoughts with people of that caliber, and have them respond by sending me papers of their own that reflected the same concepts.

Then In 2014, I retired that essay and began writing Biosemiosis.org in its place. Since that work is available to any reader, I won’t recapitulate it here, but there are a couple of concepts I’d like to highlight – particularly the discontinuity found in the translation of recorded information. Read More

[I’d like to thank Barry and Uncommon Descent for allowing me to publish this introduction to my two projects]

Comments
Alicia Cartelli:
I haven’t disputed that fact?
No, you haven't. Do you follow your own posts/arguments? I mean, seriously. Earlier you confused me with someone else: Alicia Cartelli:
Just take a look at the conversation I’m having with Mung, you’ll see that nature has already demonstrated that many of the amino acids in the majority of proteins do not need to be preserved when comparing across species (they can and often are replaced with amino acids of a similar type) and this is in organisms who must maintain a high level of fitness.
When and where did you and I have this conversation?
I haven’t disputed that fact?
No, you haven't. If you're following our conversation, as I have been doing, you haven't claimed that the enzyme does not exist, you've merely quibbled over what it's name is. Alicia Cartelli:
I haven’t disputed that fact? Why do you think I’m asking for the name of the enzyme? I know you won’t come up with one because I know it doesn’t exist. The only enzyme “that detaches the amino acid from the tRNA so that it can be added to the peptide chain” is not an enzyme, it is a ribozyme and it is called the ribosome.
Make up your mind. It doesn't exist. It exists but doesn't have a name. It exists and it's name is "the ribosome." But really, it's a ribozyme. If it's a ribozyme, surely you can tell me it's name. The ribosome itself is composed of two sub-units, and these have to be brought together during the process of translation. So when the authors say:
The ribosome … has enzymes that detach the amino acid from the tRNA, attach it to the growing amino acid chain, and release the tRNA, which can now be used again.
You could at the very least explain why they are wrong. You could also explain why the following is wrong:
Acyltransferases that use AMINO ACYL TRNA as the amino acid donor in formation of a peptide bond. There are ribosomal and non-ribosomal peptidyltransferases.
But you won't. You didn't even have the good sense to do your research. Apparently you thought you could rest easy assuming I would not do mine. Your bad.
The ribosomal peptidyl transferase center (PTC) resides in the large ribosomal subunit and catalyzes the two principal chemical reactions of protein synthesis: peptide bond formation and peptide release.
Just as I had said. Further, dispelling all doubt:
The crystallographic structures compellingly confirmed that peptidyl transferase is an RNA enzyme.
Now, please tell me again why you are right and I am wrong. Please go easy on me. I'm just an IDiot. A "scientifically illiterate, biological science-challeneged UDer." Alicia Cartelli:
...there are really no “peptidyl transferase” enzymes...
The ribosomal peptidyl transferase center: structure, function, evolution, inhibition.Mung
November 7, 2015
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Alicia Can we use you as a guinea pig? Let's stop the regulatory systems in your cells and see how long you last? Deal?Andre
November 7, 2015
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Over at TSZ Reciprocating Bill admonished me for bumping a similar prior thread here at UD a couple years ago and not recalling the relevant contents of that thread. May this thread go as long and have the same results! still unrefutedMung
November 7, 2015
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I'll drop in here for the 400-ish comment: Biosemiosis.org is now one week old. Looking at the site analytics, the site has now been viewed in 167 cities in 32 countries. It is amazing how much of Europe is represented in discussions of biosemiosis. The sister site Complexity Cafe has been viewed in 129 cities in 26 countries. In both cases the volume must be improved, but I am satisfied given that it has only been announced in this one article for seven days, and has been off the front page of UD for four of those days. Bottom line: I have much work to do. Thank you to all who have participated.Upright BiPed
November 7, 2015
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I haven't disputed that fact? Why do you think I'm asking for the name of the enzyme? I know you won't come up with one because I know it doesn't exist. The only enzyme "that detaches the amino acid from the tRNA so that it can be added to the peptide chain" is not an enzyme, it is a ribozyme and it is called the ribosome. And my model does translate, thank you. If it's so childish, the. It shouldn't be too hard for you to pick it apart.Alicia Cartelli
November 7, 2015
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Care to explain why I'm dead wrong Andre? Or are we just supposed to believe that you know what you're talking about. All signs point to no. Usually when I use the phrase "a lot" I'm talking about a significant portion of a whole, Gpucc. Feel free to list these "hundreds of proteins." Evolution was never part of the conversation. We were simply looking at sequence conservation. You really are lost. Good chat.Alicia Cartelli
November 7, 2015
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Alicia Cartelli:
I’m still waiting for the name of an enzyme “that detaches the amino acid from the tRNA so that it can be added to the peptide chain.”
Why? You've already conceded that biologists suck at naming things. Whatever it's name is, it's not "the ribosome." Suffice it to say that such an enzyme exists. Even you have not disputed that fact. Meanwhile, your toy model is just that, a toy. Not something for grownups. It's not something capable of translation. Do get back to us when you have something of substance.Mung
November 7, 2015
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To all (except Alicia Cartelli): Moving the goalposts? My statement: "“That’s probably why a lot of aminoacid sequences are so conserved, even from prokaryotes to humans (see ATP synthase, and a lot of others. Histones, for example).”" Alicia Cartelli: "We are arguing whether or not the majority of proteins have highly conserved sequences, of which you used the two wide-ranging examples ATP synthase and histones." Well, a lot does not mean the majority. I could list hundreds of proteins which have extremely high conservation, and therefore very high functional constraint. Which certainly qualifies as "a lot", but certainly does not qualify as "the majority". And, obviously, we have always been "arguing about the evolutionary importance of sequence similarity", because the evolutionary importance of sequence similarity means functional constraint, and that's what we were arguing about. Before Alicia Cartelli moved the goalposts and tried to squirm away. Not so intelligently. Now, I am really finished with this person.gpuccio
November 7, 2015
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Alicia Hold on a minute... these first organisms.did not need that much regulation? Hahahaha hahahaha you are absolutely wrong. Dead wrong.Andre
November 7, 2015
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“a chain of amino-acids sorted on size and hydrophobia is in your opinion similar to the functional proteins we find in organisms?” Yes. I don’t know why you guys are so obsessed with the word “sorting,” but yes. If you can repeatedly create a chain of amino acids not with an exact sequence, but at least with the same general types of amino acids (large/small, hydrophobic/philic) in the same order, then it would be very similar to the proteins we see in organisms today. Just take a look at the conversation I’m having with Mung, you’ll see that nature has already demonstrated that many of the amino acids in the majority of proteins do not need to be preserved when comparing across species (they can and often are replaced with amino acids of a similar type) and this is in organisms who must maintain a high level of fitness. For the first living organisms, things did not need to be nearly as regulated, efficient, etc. And to your last question; a nucleic acid sequence is being translated to an amino acid sequence.Alicia Cartelli
November 7, 2015
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Alicia: “Amino acids with similar properties and folds” sounds to me like “repeatable production of proteins,” which, last I checked, is the basis of translation.
So, a chain of amino-acids sorted on size and hydrophobia is in your opinion similar to the functional proteins we find in organisms? Tell me more about the "translation" you envision. For one thing, what is being translated?Box
November 7, 2015
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Carpathian
That is not philosophical at all.
Anything related to the logical possibility that the God of Genesis could or could not create something from nothing is a philosophical proposition. Science has nothing to say about it.
It’s logic based on premises kairosfocus provided.
No, it is based on your false interpretation of kairosfocus' comment. He said nothing about God and Genesis. It was you who introduced that element. You appear to know nothing about the scientific inference to the best explanation. Please take this opportunity to tell us how you think it works.
If a lab created life, whoever ran the lab could not have been alive.
This statement is illogical twice over. If someone is "running" the lab, then that same someone is doing the creating. Also, any "whoever" would be alive by definition. I don't know of any "who's" who are not alive. Do you?
No IDist has ever stepped through the processes involved in ID, not even Dembski.
Again, you are talking nonsense. How can you know if any IDist has ever stepped through the process if you don't know what that process is? Obviously, you cannot. Describe the ID process so that we can know that you are not just writing aimlessly for effect.StephenB
November 7, 2015
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That's why I said "ribozyme," mungy. I'm still waiting for the name of an enzyme “that detaches the amino acid from the tRNA so that it can be added to the peptide chain."Alicia Cartelli
November 7, 2015
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Alicia, "the ribosome" is not an enzyme. So why would I say that the name of the enzyme is the ribosome? Here's how a book on molecular biology puts it:
As the peptide chain continues to grow it is constantly cut off from the tRNA holding it and joined instead to the newest amino acid to be brought by its tRNA into the A-site, hence the name "acceptor" site.
Now I can understand why your "model" has no tRNA. It doesn't have a ribosome either. Nor does it have proteins. Lots of imagination, it has lots of that. You're still faced with the problem that's already been pointed out. You have to re-create the entire system again. Oh, and in addition to the things I've already pointed out: Initiation Complex Elongation Factors Release Factors Get busy.Mung
November 7, 2015
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Mungy, I will concede as soon as you provide me with the name of an enzyme “that detaches the amino acid from the tRNA so that it can be added to the peptide chain.” Provided that enzyme (ribozyme) name isn’t “the ribosome.” Gpuccio, this was your original statement: “That’s probably why a lot of aminoacid sequences are so conserved, even from prokaryotes to humans (see ATP synthase, and a lot of others. Histones, for example).” We are not arguing about the evolutionary importance of sequence similarity. Don’t try to twist what the original conversation was about. Evolution was never part of the conversation. We are arguing whether or not the majority of proteins have highly conserved sequences, of which you used the two wide-ranging examples ATP synthase and histones. Then you had to backtrack and say “oh I only meant the alpha and beta subunits of ATP synthase.” So, like I said, you specifically picked the most conserved peptide sequences to support your claim that “a lot of amino acid sequences are so conserved.” This is the definition of confirmation bias. No need to write a novel about how you moved the goalposts. What you should have done was provide some statistic that this % of proteins have at least this % of sequence conservation. But you didn't. What about the 50 amino acids present in our beta-subunit and not in that of A. halopraeferens? They certainly weren’t conserved, but your 82% doesn’t reflect that.Alicia Cartelli
November 7, 2015
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gpuccio, You are always a gentleman so it is not within my heart to offer you insults in exchange for kindness.
I can really see no other possible explanation.
Maybe common descent is false. Do you think perhaps Alicia doesn't accept common descent? ;)Mung
November 7, 2015
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Mung: Excuse me if again I take you as interlocutor for my personal ramblings. You are an old friend, and I confide that you will pardon me. Seeing that Alicia Cartelli (#370) has profited so much of my "basic biology lesson", I am tempted to offer her some basic methodology and epistemology lesson, too. Always ready to perform some good action! :) The point is, if a sequence (in this case, the beta subunit of ATP synthase, human form, but the same would be valid for the alpha subunit) exhibits a striking homology with at least a hundred bacterial forms of the same molecule, which in the evolutionary tree are distant at least 2-3 billion years, in terms of any possible evolutionary theory, and especially of the neutral model of evolution, there can be one and only one reasonable explanation for that: a very, very strong functional constraint on the sequence. Let's see. For the sake of simplicity, we can consider just two sequences: the human sequence, and the first hit in my blast: Azospirillum halopraeferens. Now, we can observe that the two sequences exhibit 392 identities (82% of the alignment). How is it possible? Can it be a casual outcome? No. Absolutely not. The expect value is given here as 0.0. That is, more or less, the number of similar results expected by chance in a database of sequences such as the one we are using. IOWs, there is really no chance at all to observe such an homology by chance. Maybe the sequence has just remained as it was 3 billion years ago? But, if that were the case, the whole evolutionary theory, and especially the neutral model, would be complete bullshit. I think we can exclude that. Neutral mutations do happen, and in 3 billion years a sequence has all the time in the world to change deeply, to become completely different from the original one, if no functional constraint is working. Therefore, we are left with one and only one explanation: the 392 AAs which are identical in the human and bacterial form (Maybe a few more, maybe a few less), have been under very strong functional constraints for about 3 billion years. I can really see no other possible explanation. Now, that is simply true, whatever the results of any other comparison with other species are. The simple fact is that the observed homology cannot be a random outcome. Now, I will try to explain what a confirmation bias is. Wikipedia will help, as usual: "Confirmation bias is the tendency to search for, interpret, favor, and recall information in a way that confirms one's beliefs or hypotheses, while giving disproportionately less consideration to alternative possibilities. It is a type of cognitive bias and a systematic error of inductive reasoning. People display this bias when they gather or remember information selectively, or when they interpret it in a biased way." So, my reasoning about the beta subunit of ATP synthase in no way represents a confirmation bias. Why? Because in no way I am "giving less consideration to alternative possibilities". Very simply, there are no alternative possibilities at all. Let's see again. I start with a question: are there biological sequences which are highly conserved for billions of years, and therefore exhibit strong functional constraints, according to all forms of evolutionary theories? To answer that, I take a few sequences, let's say all the sequences of ATP synthase, and blast them. The result? Some are strongly conserved, like the alpha and beta subunits, others are less conserved. Indeed, all those sequences exhibit some conservation, but it is very different from sequence to sequence. So, I can answer my initial question: Yes, there are sequences which exhibit strong conservation. In this group, for example, the alpha and beta subunits do exhibit that, while other sequences are less conserved. Where is the confirmation bias? Nowhere to be seen. I started with a clear question, and I gave a clear, unbiased answer. Please note that I never assumed that any protein sequence, or any sequence in the ATP molecules, needs to be strongly conserved. If my question had been: are all the sequences in ATP synthase strongly conserved? The answer would have been: no. Some are strongly conserved, some others are not. But I have never in my life assumed or proposed that all proteins sequences need to be highly conserved. I just look for those that are, and I affirm functional constraints for those sequences. Now, just to close, I would like to give here the definition for "cognitive bias", which is the larger category which includes also confirmation bias. Again, Wikipedia will help: "A cognitive bias refers to a systematic pattern of deviation from norm or rationality in judgment, whereby inferences about other people and situations may be drawn in an illogical fashion." Now I will make a judgement, and I take full responsibility for it: To affirm that there is confirmation bias in the reasoning of another person, while there is none, is a good example of cognitive bias: an inference about other people drawn in an illogical fashion.gpuccio
November 7, 2015
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Alicia Cartelli, Do you think physicochemical processes can A) produce your ribozyme B) provide the raw materials to carry on and C) be capable of evolving new functions? I know why you would want to avoid those questions. But by not answering them you prove to be a hoax. Also the fact that you confuse correlation with a chemical connection proves tat you are incapable of learning.Virgil Cain
November 7, 2015
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By the way, Alicia, did you bother following the wikipedia links yourself? Enzymes that catalyze the transfer of an aminoacyl group from donor to acceptor resulting in the formation of an ester or amide linkage. here Acyltransferases that use AMINO ACYL TRNA as the amino acid donor in formation of a peptide bond. There are ribosomal and non-ribosomal peptidyltransferases here I was willing to give you the benefit of the doubt. Why?Mung
November 7, 2015
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Alicia Cartelli:
Biologists often do a poor job in the naming convention department, sorry.
You're not a biologist? They don't just have a problem with naming:
The ribosome ... has enzymes that detach the amino acid from the tRNA, attach it to the growing amino acid chain, and release the tRNA, which can now be used again. - John Maynard Smith and Eors Szathmary. The Origins of Life. p. 41
https://en.wikipedia.org/wiki/John_Maynard_Smith https://en.wikipedia.org/wiki/E%C3%B6rs_Szathm%C3%A1ry Silly Biologists. Telling tales. Fooling the poor dumb IDiots.Mung
November 7, 2015
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“At best, he gets piles of amino acids with similar properties and folds.” What does that even mean, box? What is a “pile of amino acids?” Because to me it sounds like they’re trying to describe a protein, without actually saying the word “protein.” (But that’s just how evolutionnews works) “Amino acids with similar properties and folds” sounds to me like “repeatable production of proteins,” which, last I checked, is the basis of translation. You do know what a protein is right? A polymer of amino acids with specific folds, and in nature we see proteins with similar folds and properties performing the same function? Again, you are lost. When will you guys learn?Alicia Cartelli
November 7, 2015
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StephenB:
Carpathian: Show me how a non-living, non-god entity, that cannot control the physics of the universe, is able to design and then distribute life. StephenB: Bad logic. That is a second order philosophical question that ID’s scientific methodology cannot address.
That is not philosophical at all. It's logic based on premises kairosfocus provided. If a lab created life, whoever ran the lab could not have been alive.
Carpathian: Walk me through that process? StephenB: If you don’t know ID’s process, why would you presume to evaluate it? Isn’t that putting the cart before the horse? How can you say that ID’s methods are flawed if you don’t know what they are? Isn’t that illogical?
It is not ID's processes I was asking KF about, it was the idea of a lab creating life that was run by something alive. No IDist has ever stepped through the processes involved in ID, not even Dembski.Carpathian
November 7, 2015
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Alicia: What, Box? “Evolution” and “sorting” is not what is being compared or contrasted or anything.
It isn't?
Alicia: You are completely lost.
Am I? Alicia, get a grip on yourself. Read again — this time with comprehension:
At best, he gets piles of amino acids with similar properties and folds. That's not selection; that's just sorting. You can find that in riverbeds where rocks of various sizes sort themselves out in layers. Those "patterns" are even "preserved", but that constitutes neither a code nor a specification. [evolutionnews.org] [my emphasis]
Box
November 7, 2015
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Carpathian
Show me how a non-living, non-god entity, that cannot control the physics of the universe, is able to design and then distribute life.
Bad logic. That is a second order philosophical question that ID's scientific methodology cannot address. The primary scientific question is this: Based on empirical evidence that can be measured, was the cause of life natural or artificial. Using philosophical methods, one can, indeed, show that only a supernatural God could create a material universe out of nothing. That has nothing to do with ID science. Please explain why you think it does.
Since the ID designer pre-dates life, he cannot be alive and also cannot be God if ID is to be taken as science.
There you go again, conflating traditional philosophical methods with ID's scientific methods, neither of which you appear to be familiar with.
Walk me through that process?
If you don't know ID's process, why would you presume to evaluate it? Isn't that putting the cart before the horse? How can you say that ID's methods are flawed if you don't know what they are? Isn't that illogical?StephenB
November 7, 2015
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Correct Mung, my translational system is based largely on the papers that demonstrate the polar/nonpolar, purine/pyrimidine dichotomy and that this dichotomy is preserved at high temperatures. Later evolution of tRNA molecules, from portions of the original ribozyme I suggest, would make the system more efficient and increase the selectivity for amino acids. Yes, it is very difficult for me to admit that you are right….because you aren’t right. Wiki is on the verge of being wrong, that page and some related ones are very disorganized and confusing especially to the layman. Bottom line is if you go to the bottom of the page under external links, you’ll see that there are really no “peptidyl transferase” enzymes, just the ribosome. There is Gamma-glutamyl transpeptidase and transglutaminase, but both of these enzymes either connect R-groups of fully formed proteins or attach functional groups to proteins. Biologists often do a poor job in the naming convention department, sorry. What, Box? “Evolution” and “sorting” is not what is being compared or contrasted or anything. You are completely lost. And just because it’s not a linear sequence of letters that we have assigned to certain chemical structures, but instead is a 3-dimensional structure that specifies binding of certain amino acids, doesn’t mean it cannot be considered a “code.” I can arrange the atomic coordinates of the 3D structure into a long line of text if that would make you feel better about calling it a code.Alicia Cartelli
November 7, 2015
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Alicia Cartelli on the take-down of Carter and Wolfenden at evolutionnews.org :
AC: The points evolutionnews tries to make amount to stabs in the dark. First they play word games with “selection” vs. “sorting” and “piles of amino acids”.
Alicia, we both know that this is not playing word games. The crucial difference between “evolution” and “sorting” is befittingly pointed out. The first may be going somewhere, the second certainly not.
AC: The question is how is a genetic code produced? And the researchers propose that an early code emerged which recognized amino acids based on hydrophobicity and size via early tRNA molecules. Again this system is not as precise as the one we see today, but the ability to consistently add hydrophobic or hydrophilic amino acids or large or small amino acids or some combination of these properties would be plenty to produce proteins.
What are you going on about? You do understand that there is no code whatsoever, right?
AC: This certainly is a “code” or “specification” although it is not as simple as the codon-amino acid code that we see today.
I take it that you are jesting. For now I simply refuse to believe that there are people out there who hold that sorting on size and hydrophobia is a “code” and/or “specification” which is relevant to the problems at hand.Box
November 7, 2015
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Alicia And I have already said no hypotheticals, no assumptions just the facts please.Andre
November 7, 2015
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Alicia Calling people little and by design spelling their name in small letters won't really get you any conversations sorry.Andre
November 7, 2015
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Oh little andre, I'm not trying to blow any houses down, don't worry. All I wanted to do was have a conversation about a hypothetical early translational system, but that is obviously asking way too much from a bunch of scientifically illiterate, biological science-challeneged UDers. Don't know why I ever bothered in the first place.Alicia Cartelli
November 7, 2015
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Alicia Cartelli:
The question is how is a genetic code produced? And the researchers propose that an early code emerged which recognized amino acids based on hydrophobicity and size via early tRNA molecules.
A feature missing from your model:
My system does not use tRNA...
Which, you claim, is based on these papers:
...my hypothetical “first translational system” was based on some of the findings in these papers.
Mung: There’s also an enzyme that detaches the amino acid from the tRNA so that it can be added to the peptide chain. Alicia Cartelli: What enzyme is that? Mung: Peptidyl transferases. Alicia:
Mung, the only thing that “detaches the amino acid from the tRNA so that it can be added to the peptide chain” is the ribosome.
Is it really that difficult for you to admit I was right? Or is the wiki page wrong?Mung
November 7, 2015
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