Darwin's Fraudulent Tautology

[ChemEngineer]

 

Your major error is to suppose that changes to proteins in populations is random.   But it's demonstrably not so. - Barbarian

 

Your major error is to have no idea as to how each and every amino acid was "SELECTED" and provide the Darwinistic mechanism as to how this occurred. Talking circles around biochemical synthesis doesn't come close to being science.  Now since you insist on simply saying "That's wrong" without explaining the process, I don't want to spend any more time reading "that's wrong, that's wrong, that's wrong."   Synthesis inside of living organisms is not "abiotic" as you claim in the "selection" of L forms.  It's even more complicated since the probability of peptide bonds forming is roughly the same as the probability of non-peptide bonds forming.  Another complication in an inordinately long list of them.  Not the "A>B>C>D" alphabetology that evolutionary biologists preach.

 

ciao

Edited June 22, 2020 by ChemEngineer

[The Barbarian]

2 hours ago, ChemEngineer said:

Your major error is to have no idea as to how each and every amino acid was "SELECTED" and provide the Darwinistic mechanism as to how this occurred.

Observation of new proteins evolving in organisms have shown them to be via mutation and natural selection.  Where the process has been observed, the mutations can be shown.    Would you like to see an example?

Your argument says that unless we know who supplied the wine for the Last Supper, we can't conclude that it happened.    

 

2 hours ago, ChemEngineer said:

Now since you insist on simply saying "That's wrong" without explaining the process

I offered to show you why.   Want to see?

2 hours ago, ChemEngineer said:

I don't want to spend any more time reading "that's wrong, that's wrong, that's wrong." 

I know a secret for avoiding that happening to you in the future.   Only talk about things you know.    In your misattribution for Darwin, there is no possibility that he cited "random mutation followed by selection."   You've never actually read his book, and you probably never read DeVries or Mendel, so it's not surprising you got it wrong.

 

2 hours ago, ChemEngineer said:

Synthesis inside of living organisms is not "abiotic" as you claim in the "selection of L forms.

If you have to claim that I said things I did not, perhaps that's an important clue for you.   The evidence for an excess of L-forms in abiotic formation of amino acids comes from abiotic sources, not living things:

Engel et al. (1990) determined the δ¹³C values for individual amino acid enantiomers to attempt to ascertain whether the reported l-excess in Murchison amino acids (Engel and Nagy, 1982) was a consequence of terrestrial contamination, one of the original applications envisaged for CSIA of meteoritic organics (Pillinger, 1982). Similar, nonterrestrial δ¹³C values were obtained for l- and d-alanine of +27‰ and +30‰, respectively (Table 2), apparently confirming the indigenous nature of these acids. They argued that the more negative δ¹³C value for the l-enantiomer could not be explained by terrestrial contamination and that this excess was indigenous to the meteorite.

The Origin and Evolution of Organic Matter in Carbonaceous Chondrites and Links to Their Parent Bodies ; Primitive Meteorites and Asteroids

https://www.sciencedirect.com/book/9780128133255/primitive-meteorites-and-asteroids

2 hours ago, ChemEngineer said:

It's even more complicated since the probability of peptide bonds forming is roughly the same as the probability of non-peptide bonds forming.  Another complication in an inordinately long list of them.  Not the "A>B>C>D" alphabetology that evolutionary biologists preach.

You've been misinformed about that.   Since peptide bonds form abiotically:

• Prebiotic Chemistry
• Published: 23 August 2012

Abiotic Formation of Valine Peptides Under Conditions of High Temperature and High Pressure

Abstract

We investigated the oligomerization of solid valine and the stabilities of valine and valine peptides under conditions of high temperature (150–200 °C) and high pressure (50–150 MPa). Experiments were performed under non-aqueous condition in order to promote dehydration reaction. After prolonged exposure of monomeric valine to elevated temperatures and pressures, the products were analyzed by liquid chromatography mass spectrometry comparing their retention times and masses. We identified linear peptides that ranged in size from dimer to hexamer, as well as a cyclic dimer. Previous studies that attempted abiotic oligomerization of valine in the absence of a catalyst have never reported valine peptides larger than a dimer. Increased reaction temperature increased the dissociative decomposition of valine and valine peptides to products such as glycine, β-alanine, ammonia, and amines by processes such as deamination, decarboxylation, and cracking. The amount of residual valine and peptide yields was greater at higher pressures at a given temperature, pressure, and reaction time. This suggests that dissociative decomposition of valine and valine peptides is reduced by pressure. Our findings are relevant to the investigation of diagenetic processes in prebiotic marine sediments where similar pressures occur under water-poor conditions. These findings also suggest that amino acids, such as valine, could have been polymerized to peptides in deep prebiotic marine sediments within a few hundred million years.

-----

Carbonyl Sulfide-Mediated Prebiotic Formation of Peptides

Science  08 Oct 2004:
Vol. 306, Issue 5694, pp. 283-286

Abstract

Almost all discussions of prebiotic chemistry assume that amino acids, nucleotides, and possibly other monomers were first formed on the Earth or brought to it in comets and meteorites, and then condensed nonenzymatically to form oligomeric products. However, attempts to demonstrate plausibly prebiotic polymerization reactions have met with limited success. We show that carbonyl sulfide (COS), a simple volcanic gas, brings about the formation of peptides from amino acids under mild conditions in aqueous solution. Depending on the reaction conditions and additives used, exposure of α-amino acids to COS generates peptides in yields of up to 80% in minutes to hours at room temperature.

...there's no point in denying the fact.  

5 hours ago, ChemEngineer said:

Another complication in an inordinately long list of them.  Not the "A>B>C>D" alphabetology that evolutionary biologists preach.

See above.   You've assumed a lot of things not in evidence.     And you were unaware of a lot more, for which there is evidence.

[The Barbarian]

The way we know now evolution of enzymes by stepwise improvement under mutation and natural selection is simple.   It's been observed.   But your question is interesting enough to deserve a separate thread.   What say we spend some time on that one, and the evidence for it?

 

[The Barbarian]

On 6/13/2020 at 8:23 AM, ChemEngineer said:

Synthesis inside of living organisms is not "abiotic" as you claim in the "selection of L forms.

Perhaps you should show where I made that claim.   The evidence for an excess of L-forms in abiotic formation of amino acids comes from abiotic sources, not living things:

Engel et al. (1990) determined the δ¹³C values for individual amino acid enantiomers to attempt to ascertain whether the reported l-excess in Murchison amino acids (Engel and Nagy, 1982) was a consequence of terrestrial contamination, one of the original applications envisaged for CSIA of meteoritic organics (Pillinger, 1982). Similar, nonterrestrial δ¹³C values were obtained for l- and d-alanine of +27‰ and +30‰, respectively (Table 2), apparently confirming the indigenous nature of these acids. They argued that the more negative δ¹³C value for the l-enantiomer could not be explained by terrestrial contamination and that this excess was indigenous to the meteorite.

The Origin and Evolution of Organic Matter in Carbonaceous Chondrites and Links to Their Parent Bodies ; Primitive Meteorites and Asteroids

https://www.sciencedirect.com/book/9780128133255/primitive-meteorites-and-asteroids

On 6/13/2020 at 8:23 AM, ChemEngineer said:

It's even more complicated since the probability of peptide bonds forming is roughly the same as the probability of non-peptide bonds forming.  Another complication in an inordinately long list of them.  Not the "A>B>C>D" alphabetology that evolutionary biologists preach.

You've been misinformed about that.   Since peptide bonds form abiotically:

• Prebiotic Chemistry
• Published: 23 August 2012

Abiotic Formation of Valine Peptides Under Conditions of High Temperature and High Pressure

Abstract

We investigated the oligomerization of solid valine and the stabilities of valine and valine peptides under conditions of high temperature (150–200 °C) and high pressure (50–150 MPa). Experiments were performed under non-aqueous condition in order to promote dehydration reaction. After prolonged exposure of monomeric valine to elevated temperatures and pressures, the products were analyzed by liquid chromatography mass spectrometry comparing their retention times and masses. We identified linear peptides that ranged in size from dimer to hexamer, as well as a cyclic dimer. Previous studies that attempted abiotic oligomerization of valine in the absence of a catalyst have never reported valine peptides larger than a dimer. Increased reaction temperature increased the dissociative decomposition of valine and valine peptides to products such as glycine, β-alanine, ammonia, and amines by processes such as deamination, decarboxylation, and cracking. The amount of residual valine and peptide yields was greater at higher pressures at a given temperature, pressure, and reaction time. This suggests that dissociative decomposition of valine and valine peptides is reduced by pressure. Our findings are relevant to the investigation of diagenetic processes in prebiotic marine sediments where similar pressures occur under water-poor conditions. These findings also suggest that amino acids, such as valine, could have been polymerized to peptides in deep prebiotic marine sediments within a few hundred million years.

-----

Carbonyl Sulfide-Mediated Prebiotic Formation of Peptides

Science  08 Oct 2004:
Vol. 306, Issue 5694, pp. 283-286

Abstract

Almost all discussions of prebiotic chemistry assume that amino acids, nucleotides, and possibly other monomers were first formed on the Earth or brought to it in comets and meteorites, and then condensed nonenzymatically to form oligomeric products. However, attempts to demonstrate plausibly prebiotic polymerization reactions have met with limited success. We show that carbonyl sulfide (COS), a simple volcanic gas, brings about the formation of peptides from amino acids under mild conditions in aqueous solution. Depending on the reaction conditions and additives used, exposure of α-amino acids to COS generates peptides in yields of up to 80% in minutes to hours at room temperature.

...there's no point in denying the fact.  

[The Barbarian]

On 6/12/2020 at 10:56 AM, ChemEngineer said:

"Change in allele frequencies" can NEVER account for the insuperable statistics of polypeptide synthesis.

It's directly observed to do so.

Genetics. 1978 Jul; 89(3): 453–465

Experimental Evolution of a New Enzymatic Function. II. Evolution of Multiple Functions for EBG Enzyme in E. COLI

Barry G. Hall

Abstract

The evolution of ebg^o enzyme of Escherichia coli, an enzyme which is unable to hydrolyze lactose, lactulose, lactobionate, or galactose-arabinoside effectively, has been directed in successive steps so that the evolved enzyme is able to hydrolyze these galactosides effectively. I show that in order for a strain of E. coli with a lacZ deletion to evolve the ability to use lactobionate as a carbon source, a series of mutations must occur in the ebg genes, and that these mutations must be selected in a particular order. The ordered series of mutations constitutes an obligatory evolutionary pathway for the acquisition of a new function for ebg^o enzyme. A comparison of newly evolved strains with parental strains shows that when ebg enzyme acquires a new function, its old functions often suffer; but that in several cases old functions are either unaffected or are improved. I conclude that divergence of functions catalyzed by an enzyme need not require gene duplication.

On 6/12/2020 at 10:56 AM, ChemEngineer said:

Nobody has, nor will they ever, explain how proteins were "selected" by changes in allele frequencies to arrange the precise amino acid, levorotary at that, out of twenty possibilities 33,450 times in succession to synthesize titin, a protein in human muscles.   What is 1/20 to the 33,450th power please?

Your error is to assume this can only happen randomly.  But as you now see from Hall's data, it's not random.   Any rational person would realize that natural selection is necessary for the evolution of a new enzyme.

But some creationists are not rational.  They cling to the faulty assumption that enzymes must evolve randomly.

Have you realized why Darwin would not have described evolution as "mutation followed by natural selection?"

 

 

Edited June 15, 2020 by The Barbarian