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At Sci-News: Moths Produce Ultrasonic Defensive Sounds to Fend Off Bat Predators

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Scientists from Boise State University and elsewhere have tested 252 genera from most families of large-bodied moths. Their results show that ultrasound-producing moths are far more widespread than previously thought, adding three new sound-producing organs, eight new subfamilies and potentially thousands of species to the roster.

A molecular phylogeny of Lepidoptera indicating antipredator ultrasound production across the order. Image credit: Barber et al., doi: 10.1073/pnas.2117485119.

Bats pierce the shadows with ultrasonic pulses that enable them to construct an auditory map of their surroundings, which is bad news for moths, one of their favorite foods.

However, not all moths are defenseless prey. Some emit ultrasonic signals of their own that startle bats into breaking off pursuit.

Many moths that contain bitter toxins avoid capture altogether by producing distinct ultrasounds that alert bats to their foul taste. Others conceal themselves in a shroud of sonar-jamming static that makes them hard to find with bat echolocation.

While effective, these types of auditory defense mechanisms in moths are considered relatively rare, known only in tiger moths, hawk moths and a single species of geometrid moth.

“It’s not just tiger moths and hawk moths that are doing this,” said Dr. Akito Kawahara, a researcher at the Florida Museum of Natural History.

“There are tons of moths that create ultrasonic sounds, and we hardly know anything about them.”

In the same way that non-toxic butterflies mimic the colors and wing patterns of less savory species, moths that lack the benefit of built-in toxins can copy the pitch and timbre of genuinely unappetizing relatives.

These ultrasonic warning systems seem so useful for evading bats that they’ve evolved independently in moths on multiple separate occasions.

In each case, moths transformed a different part of their bodies into finely tuned organic instruments.

[I’ve put these quotes from the article in bold to highlight the juxtaposition of “evolved independently” and “finely tuned organic instruments.” Fine-tuning is, of course, often associated with intelligent design, rather than unguided natural processes.]

See the full article in Sci-News.

Comments
ET:
Drift is what accounted for the gene duplication in the LTEE that gave the E coli the ability to utilize citrate in an aerobic environment. That was an adaptive change.
Nope. The advantage of being able to digest citrate allows the mutant to overwhelm the wild type. It is fitter in the niche that supplies citrate. That is selection. I'm looking for a response I owe Querius and came across this. Has ET taken a break, too?Alan Fox
September 11, 2022
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PPS, and accusations that CSI and/or FSCO/I are "bogus" -- see 269, 274 etc onward, this is willful -- actually are themselves precisely examples of ascii text strings in English, typically at/beyond 72 - 143 characters. That's readily observable FSCO/I despite pretences not to know what such could mean and therefore CSI. And the objectors know better. We have here a case of objectors making confession by projection.kairosfocus
August 24, 2022
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F/N: This thread has been revealing on the balance on merits regarding the design inference. Let us particularly notice the objectors' all too typical rhetorical pattern of accusation, dismissal, setting up and knocking over strawmen, tangents, personalities etc. Such quarrelsome evasiveness reflects a subtext of ill founded contempt, and a want of substance for their objectionism. It is especially significant to see that there was/is want of familiarity with the key metric for information carrying capacity, negative log of probability; which metric then led to recognising that the Dembski X metric was an information beyond a complexity threshold metric, by reducing the logs. Base 2 was a key clue. The need for high contingency of strings, to enable them to carry a variety of messages was objected to, was even derided as if it were a gross error, and yet it remains that any of AGCT/U can follow any base, and that the tRNA CCA tip bonds to the COOH end of an AA, making this a universal joint so that encoding is by action of aminoacyl tRNA synthetases. As Yockey pointed out. (But it seems, objectors don't like to read diagrams.) Further, they imagine that complex functionally specific or more broadly specified information is dubious or "bogus," when in fact this is the very stuff of an information age. As for redundancy and linked Kolmogorov complexity/compressibility, the less said the better, it seems. Net, there is every good reason to declare knowledge independence and refuse to hold the design inference on tested sign hostage to such poorly founded objectionism. KF PS, in the cell we find complex, coded algorithms and molecular nanotech execution machinery. That's language, goal directed stepwise processes and sophisticated use of polymer technology to effect nanotech information systems. Strong signs of design, reflected in Wicken wiring diagram functionally specific, complex organisation and/or associated information, FSCO/I, the relevant subset of Orgel's Specified Complexity, i.e. complex specified information -- CSI.kairosfocus
August 22, 2022
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AF, 657 and following, which is above 672. KFkairosfocus
August 22, 2022
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Stop moving the goal posts. Drift is what accounted for the gene duplication in the LTEE that gave the E coli the ability to utilize citrate in an aerobic environment. That was an adaptive change.ET
August 22, 2022
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And drift explains biological change over time. Just ask LarrMoran.
It does not, without selection, account for adaptive change. I doubt Larry Moran disagrees but you could cite him if you want. I certainly don't accept your bald assertion.Alan Fox
August 22, 2022
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See the following, above.
Well, which is it? Following or above?Alan Fox
August 22, 2022
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F/N: Objectors need to acquaint themselves with the layercake, virtual machine model of telecomms and info systems championed decades ago by Andrew S Tanenbaum and now a common place approach: _______________ LEVEL N -- apps and user interfaces * * * _________ Level3 ___________ Level 2 ______________ LEVEL 1: Hardware and physical/chemical etc interactions ______________ KFkairosfocus
August 22, 2022
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Notice, what is being adroitly side stepped; yet again. We are seeing here, a key root of much of the controversy. Too many objectors, convinced that we cannot ever be right, refuse to recognise the objective evidence that shows that . . . surprise . . . we are right. Sad. PS: Note from 657, i/l/o my onward responses:
AF: The relationship between which amino-acid charges to which tRNA and catalyzed by which amino-acyl tRNA synthetase is, or could be, arbitrary. This does not change the fact that all such relationships are physico-chemical. KF: If there were, they could not store information. [--> a snip out of context of course, my point is we have strings and freedom of succession is key to having info-bearing chains, any of AGCT/U can follow any, including itself] AF: Well, that’s glaringly false. Though I am curious how you would begin to justify that claim?
See the following, above.kairosfocus
August 22, 2022
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Great. Alan ran away again and will repeat his oft-refuted trope.ET
August 22, 2022
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Natural selection is non-random only in that not all variants have the same chance of being eliminated. Alan doesn't understand natural selection and it shows. Natural selection is blind, mindless and purposeless. Just ask Jerry Coyne. And drift explains biological change over time. Just ask Larry Moran.ET
August 21, 2022
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Good job natural selection is a non-random process, then, as otherwise there would be no explanation for biological change over time.Alan Fox
August 21, 2022
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Evolution by means of blind and mindless processes cannot account for tRNAs. Evolution by means of blind and mindless processes cannot account for aminoacyl-tRNA synthetases. Evolution by means of blind and mindless processes cannot account for mRNAs. Evolution by means of blind and mindless processes cannot account for proof reading and error correction. Alan and JVL are just liars and bluffing cowards.ET
August 21, 2022
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Earth to JVL- Anything that you can find I have already read. So, please grow up. There isn't anything in what you posted that says that blind and mindless processes did it. You are either willfully ignorant or a bluffing foolET
August 21, 2022
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Alan Fox is a coward, liar, bluffing fool and scientifically illiterate ass.ET
August 21, 2022
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AF, consider a string of elements |x|x| . . . |x| where each element can only be succeeded by a particular other one, i.e. it has low or no contingency. Apart from mere presence, such cannot carry coded information. It is the ability to freely chain elements -- high contingency -- that allows information storage, whether for read only [programmed initially then used] or read write memory. It seems you are unfamiliar with information processing technologies. Take as an example a common mechanical storage register, a Yale type lock. A blank can have differing pin height info stored at each pin location, when it is cut. This matches pins in the lock so that the shear line will match the lock cylinder and turn to open the lock. A high, intermediate or low value freely follows any previous position. I used this very example recently but obviously you did not adequately reckon with it. In alphanumeric systems, any glyph can freely follow any other, it is coding and related grammar etc conventions or rules that encode for standard English but I am sure you have seen crawling text displays that further illustrate the point. In binary registers 1/0 freely follow in the next location. In D/RNA, any of AGCT/U can follow any other along the strand, it is between two matched strands that we have a matching constraint. Further for tRNA, the CCA tool tip couples to the COOH end of an AA, so chemically any tRNA can match any AA, it is the aminoacyl tRNA synthetase loading enzyme that matches each tRNA to the proper AA. KF PS, Wiki confesses:
An aminoacyl-tRNA synthetase (aaRS or ARS), also called tRNA-ligase, is an enzyme that attaches the appropriate amino acid onto its corresponding tRNA. It does so by catalyzing the transesterification of a specific cognate amino acid or its precursor to one of all its compatible cognate tRNAs to form an aminoacyl-tRNA. In humans, the 20 different types of aa-tRNA are made by the 20 different aminoacyl-tRNA synthetases, one for each amino acid of the genetic code. This is sometimes called "charging" or "loading" the tRNA with an amino acid. Once the tRNA is charged, a ribosome can transfer the amino acid from the tRNA onto a growing peptide, according to the genetic code. Aminoacyl tRNA therefore plays an important role in RNA translation, the expression of genes to create proteins.
And, https://pubmed.ncbi.nlm.nih.gov/24706556/
Wiley Interdiscip Rev RNA . 2014 Jul-Aug;5(4):461-80. doi: 10.1002/wrna.1224. Epub 2014 Apr 4. tRNA synthetase: tRNA aminoacylation and beyond Yan Ling Joy Pang 1 , Kiranmai Poruri, Susan A Martinis Affiliations PMID: 24706556 PMCID: PMC4062602 DOI: 10.1002/wrna.1224 Free PMC article Abstract The aminoacyl-tRNA synthetases are prominently known for their classic function in the first step of protein synthesis, where they bear the responsibility of setting the genetic code.
kairosfocus
August 20, 2022
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...demonstrate taht what KF said...
The typo is a bit of a tell, Joe. Nap? Walk in the fresh air? Glass of a cool, refreshing beverage? I'll still be here if I'm spared.Alan Fox
August 19, 2022
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ET: Wow. JVL is clueless. How it deals with the error is not the same as how it detects errors. How does the ribosome know there is a wrong amino acid? Ribosome states signal RNA quality control https://www.ncbi.nlm.nih.gov/pmc/articles/PMC8041214/
Quality control (QC) responses are often triggered as a result of ribosomes encountering sequences or environmental insults that lead to a slowing in translation. Examples of sequence-induced problems include extremely poor codon content, errors in transcription, or errors in pre-mRNA processing including splicing and polyadenylation, whereas environmental damage could include exposure of cells to oxidizing agents or UV irradiation, both of which damage nucleotides (Gordon et al., 2015; Yan and Zaher, 2019). An interesting set of observations to consider is that slow ribosomes simply signal canonical mRNA decay whereas errors such as premature polyadenylation within the ORF signal more comprehensive QC. The cell clearly distinguishes between different types of translation elongation difficulties and leverages an appropriate response. Slowly decoded codons do not signal a crisis meriting nascent peptide degradation; logically the cell needs the protein output of the ORF. Instead, slow codons are taken advantage of by the cell for the regulation of mRNA turnover (Hoekema et al., 1987; Caponigro, Muhlrad and Parker, 1993; Presnyak et al., 2015). By contrast, when there are more substantive problems with the mRNA such that the ORF is unlikely to generate a full length protein product, then the cell targets the incomplete nascent peptide for decay and often inhibits further rounds of initiation before degrading the mRNA to minimize protein output (Brandman and Hegde, 2016). We know these steps are critical since deletion of factors involved in these processes lead to the accumulation of protein aggregates and cell death in yeast (Bengtson and Joazeiro, 2010) and neurodegeneration in mammals (Ishimura et al., 2014; Martin et al., 2020).
In this review, we provide an overview of recent work in the field exploring both normal mRNA turnover and problematic mRNA quality control. Normal mRNA turnover depends on multiple pathways that are critical for overall protein expression; similarly, mRNA quality control depends on multiple overlapping pathways that process trapped ribosome complexes and target incomplete toxic proteins and mRNAs for decay. We discuss how these two major processes of mRNA turnover and mRNA quality control initiate at the ribosome and distinguish at a molecular level between normal (possibly slowly) elongating ribosomes and terminally stalled ribosomes to trigger a measured response.
There has been considerable focus in recent years on the cellular response to defective or damaged mRNAs. What is abundantly clear is that incomplete peptide products originating from such mRNAs are toxic to cells and that a robust quality control response has evolved in order to target such peptides for decay (Inada, 2020) – this will not be the focus of this review. Here we will focus on other QC events including mechanisms that have evolved to limit further translation on such mRNAs, to target the mRNAs for decay, and, to rescue the stuck ribosomes for re-entry into the cellular pools. The key first question is how does the cell distinguish between a normal mRNA being translated and a problematic mRNA that should be targeted by QC. To answer this, we will separately discuss two broad classes of problematic mRNA – those with ribosomes stalled within the ORF and those with ribosomes stalled in the poly-A tail.
There's A LOT more of course. Not that you'll read it of course. The point is that not only is there ongoing research but a lot has been discovered and is now understood.JVL
August 19, 2022
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ET No one said, thought nor implied that everything is designed. Alan is an infant.
True if you talk about functional information. If you say that the chemistry laws are not designed you imply that atoms/molecules happen to fit into the project of life by chance . The only problem : they fit way too well to be about randomness. Yes there are layers of more and more complexity but higher levels(brain) are based on a particular and exclusive "behaviour" of atoms(what we call laws of physics/chemistry).Lieutenant Commander Data
August 19, 2022
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AF, making up multiple Nobel prize winning work and its conclusions, well that is inadvertent high praise. I think Crick, Watson et al were there first. KFkairosfocus
August 19, 2022
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Alan Fox:
This does not change the fact that all such relationships are physico-chemical.
Your "facts" are total nonsense. There isn't any phyico-chemical connection between amino acid and the mRNA that represents it.
Well, that’s glaringly false.
Your ignorance with respect to information is not an argument. And you cannot demonstrate taht what KF said is "glaringly false". Your cowardice is not an argument, either.ET
August 19, 2022
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Alan Fox is clearly an illiterate coward. No one said, thought nor implied that everything is designed. Alan is an infant.ET
August 19, 2022
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The common structure of the ribosome points to a Common Design. There is no doubt of common design across all domains of living organisms.
So there we have it, folks. Everything is designed. Why we then need the bogus nonsense of "CSI" is beyond me, if the only answer it will give us is "yes, it's designed".Alan Fox
August 19, 2022
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AF, as you know...
Here he goes again making up stuff
...there is no physico-chemical determination as to what base from AGCT/U follows which in a chain for mRNA.
The relationship between which amino-acid charges to which tRNA and catalyzed by which amino-acyl tRNA synthetase is, or could be, arbitrary. This does not change the fact that all such relationships are physico-chemical.
If there were, they could not store information.
Well, that's glaringly false. Though I am curious how you would begin to justify that claim?Alan Fox
August 19, 2022
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Stuff it, Alan. You are the least knowledgeable person here. And all you can do is engage in question-begging. There isn't any naturalistic mechanism capable of producing the diversity of life. The common structure of the ribosome points to a Common Design. There is no doubt of common design across all domains of living organisms. Again, there isn't any evidence that ant ribosome evolved by means of blind and mindless processes such as natural selection and drift. there isn't even any way to test that claim. That means it is not a scientific claim.ET
August 19, 2022
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Ribosomes. No one knows how to test the claim that any ribosome evolved by means of blind and mindless processes such as natural selection and drift.
Well, sure, least of all you. But we do know that the core catalytic element of a ribosome is a ribozyme, an RNA sequence rather than a protein, which makes ribosomes a very ancient organelle possessed by prokaryotes (both Archaea and bacteria) as well as eukaryotes. There is no doubt of common descent across all three domains of living organisms.Alan Fox
August 19, 2022
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https://www.youtube.com/watch?v=52JfcJvP-Sk Michael Denton - on the heart (lucky us)es58
August 19, 2022
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AF, as you know, there is no physico-chemical determination as to what base from AGCT/U follows which in a chain for mRNA. If there were, they could not store information. Similarly for tRNA, the CCA tool tip is at the opposite end of the L-shaped folded molecule from the anticodon and it couples to the COOH end of an AA, i.e. chemically any tRNA can bond with any AA. It is the loading enzymes that add the right AA to the right tRNA, that is where encoding happens, as Yockey pointed out [surely, you have seen his comms system diagram mapping? or were you too busy sidestepping to notice?]. Worse, IIRC there are about two dozen variant codes, most notably for mitochondria. What we have is an algorithm, in a communication system and we have transcription, editing and translation involved. KF PS, note Wiki's further confessions on translation as the thumbscrews bite home:
Each tRNA is composed of 70-80 nucleotides and adopts a characteristic cloverleaf structure due to the formation of hydrogen bonds between the nucleotides within the molecule. There are around 60 different types of tRNAs, each tRNA binds to a specific sequence of three nucleotides (known as a codon) within the mRNA molecule and delivers a specific amino acid.[12] [--> they have to be loaded] The ribosome initially attaches to the mRNA at the start codon (AUG) and begins to translate the molecule. The mRNA nucleotide sequence is read in triplets - three adjacent nucleotides in the mRNA molecule correspond to a single codon. Each tRNA has an exposed sequence of three nucleotides, known as the anticodon, which are complementary in sequence to a specific codon that may be present in mRNA. For example, the first codon encountered is the start codon composed of the nucleotides AUG. The correct tRNA with the anticodon (complementary 3 nucleotide sequence UAC) binds to the mRNA using the ribosome. This tRNA delivers the correct amino acid corresponding to the mRNA codon, in the case of the start codon, this is the amino acid methionine. The next codon (adjacent to the start codon) is then bound by the correct tRNA with complementary anticodon, delivering the next amino acid to ribosome. The ribosome then uses its peptidyl transferase enzymatic activity to catalyze the formation of the covalent peptide bond between the two adjacent amino acids.[6] The ribosome then moves along the mRNA molecule to the third codon. The ribosome then releases the first tRNA molecule, as only two tRNA molecules can be brought together by a single ribosome at one time. The next complementary tRNA with the correct anticodon complementary to the third codon is selected, delivering the next amino acid to the ribosome which is covalently joined to the growing polypeptide chain. This process continues with the ribosome moving along the mRNA molecule adding up to 15 amino acids per second to the polypeptide chain. Behind the first ribosome, up to 50 additional ribosomes can bind to the mRNA molecule forming a polysome, this enables simultaneous synthesis of multiple identical polypeptide chains.[6] Termination of the growing polypeptide chain occurs when the ribosome encounters a stop codon (UAA, UAG, or UGA) in the mRNA molecule. When this occurs, no tRNA can recognise it and a release factor induces the release of the complete polypeptide chain from the ribosome.[12] Dr. Har Gobind Khorana, a scientist originating from India, decoded the RNA sequences for about 20 amino acids.[citation needed] He was awarded the Nobel Prize in 1968, along with two other scientists, for his work.
The mods are being shown the rack, hastily they admit:
The genetic code is the set of rules used by living cells to translate information encoded within genetic material (DNA or RNA sequences of nucleotide triplets, or codons) into proteins. Translation is accomplished by the ribosome, which links proteinogenic amino acids in an order specified by messenger RNA (mRNA), using transfer RNA (tRNA) molecules to carry amino acids and to read the mRNA three nucleotides at a time. The genetic code is highly similar among all organisms and can be expressed in a simple table with 64 entries. A series of codons in part of a messenger RNA (mRNA) molecule. Each codon consists of three nucleotides, usually corresponding to a single amino acid. The nucleotides are abbreviated with the letters A, U, G and C. This is mRNA, which uses U (uracil). DNA uses T (thymine) instead. This mRNA molecule will instruct a ribosome to synthesize a protein according to this code. The codons specify which amino acid will be added next during protein synthesis. With some exceptions,[1] a three-nucleotide codon in a nucleic acid sequence specifies a single amino acid. The vast majority of genes are encoded with a single scheme (see the RNA codon table). That scheme is often referred to as the canonical or standard genetic code, or simply the genetic code, though variant codes (such as in mitochondria) exist . . . . Nirenberg and Philip Leder revealed the code's triplet nature and deciphered its codons. In these experiments, various combinations of mRNA were passed through a filter that contained ribosomes, the components of cells that translate RNA into protein. Unique triplets promoted the binding of specific tRNAs to the ribosome. Leder and Nirenberg were able to determine the sequences of 54 out of 64 codons in their experiments.[17] Khorana, Holley and Nirenberg received the 1968 Nobel for their work.[18] The three stop codons were named by discoverers Richard Epstein and Charles Steinberg. "Amber" was named after their friend Harris Bernstein, whose last name means "amber" in German.[19] The other two stop codons were named "ochre" and "opal" in order to keep the "color names" theme . . . . Since 2001, 40 non-natural amino acids have been added into proteins by creating a unique codon (recoding) and a corresponding transfer-RNA:aminoacyl – tRNA-synthetase pair to encode it with diverse physicochemical and biological properties in order to be used as a tool to exploring protein structure and function or to create novel or enhanced proteins.[22][23] H. Murakami and M. Sisido extended some codons to have four and five bases. Steven A. Benner constructed a functional 65th (in vivo) codon.[24] In 2015 N. Budisa, D. Söll and co-workers reported the full substitution of all 20,899 tryptophan residues (UGG codons) with unnatural thienopyrrole-alanine in the genetic code of the bacterium Escherichia coli.[25] In 2016 the first stable semisynthetic organism was created. It was a (single cell) bacterium with two synthetic bases (called X and Y). The bases survived cell division.[26][27] In 2017, researchers in South Korea reported that they had engineered a mouse with an extended genetic code that can produce proteins with unnatural amino acids.[28] In May 2019, researchers reported the creation of a new "Syn61" strain of the bacterium Escherichia coli. This strain has a fully synthetic genome that is refactored (all overlaps expanded), recoded (removing the use of three out of 64 codons completely), and further modified to remove the now unnecessary tRNAs and release factors. It is fully viable and grows 1.6× slower than its wild-type counterpart "MDS42".[29][30]
Yes, actual genetic engineering yielding an extension to the code is a reality.kairosfocus
August 19, 2022
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Ribosomes. No one knows how to test the claim that any ribosome evolved by means of blind and mindless processes such as natural selection and drift. Imagine that! Evos don't have anything beyond begging the question!!!ET
August 19, 2022
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Wow. JVL is clueless. How it deals with the error is not the same as how it detects errors. How does the ribosome know there is a wrong amino acid?ET
August 19, 2022
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