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lucaspa

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For anyone wanting to argue against protocells, like any scientific theory, you have to address the data.  So, to start off, here is some of the data on protocells -- their formation, composition, and  capabilities.  I have taken the time to obtain and read the papers (part of my own critical evaluation of Fox's claims).  Anyone can walk me thru the papers and try to show where the data is wrong.  This will be in two posts due to length limitations.

Web sites:
http://www.siu.edu/~protocell/
http://www.theharbinger.org/articles/rel_sci/fox.html
First papers:
    Fox, S.W. and K. Harada. 1958. Thermal copolymerization of amino acids to a product resembling protein. Science 128: 1214.
    Fox, S. W., K. Harada, and J. Kendrick. 1959. Production of spherules from synthetic proteinoids and hot water. Science 129: 1221-1223.
    Hayakawa, T, Windsor, CR, Fox, SW.  Coploymerization of the Leuchs anhydrides of the eithtten amino acides common to proteins.  Arch. Biochem. Biophys. 118: 265-272, 1967.
    Melius, P, Sheng, YY-P.  Thermal condensation of a mixture of six amino acids.  Bioorg. Chem. 4: 385-391, 1975.

Protocells under prebiotic conditions:
    Snyder WD and Fox, SW.  A model for the origin of stable protocells in a primitive alkaline ocean.  BioSystems 7: 222-229, 1975.
   Rohlfing, DL.  Thermal polyamino acids: synthesis at less than 100°C.  Science 193: 68-70, 1976.
   Syren RM, Sanjur A, Fox SW  Proteinoid microspheres more stable in hot than in cold water.  Biosystems 1985;17(4):275-80  (protocells at hydrothermal vents)
   Yanagawa, H. and K. Kobayashi. 1992. An experimental approach to chemical evolution in submarine hydrothermal. systems. Origins of Life and Evolution of the Biosphere 22: 147-159.
   Marshall, W. H. 1994. Hydrothermal synthesis of amino acids. Goechimica et Cosmochimica Acta 58: 2099-2106.
    McAlhaney WW, Rohlfing DL.  Formation of proteinoid microspheres under simulated prebiotic atmospheres and individual gases.  Biosystems 1976 Jul;8(2):45-50
     Fouche-CE Jr; Rohlfing-DL   Thermal polymerization of amino acids under various atmospheres or at low pressures.  Biosystems. 1976 Jul; 8(2): 57-65
   SW Fox, Thermal polymerization of amino-acids and production of formed microparticles on lava.  Nature, 201: 336-337, Jan. 25, 1964.
   Hennon, G, Plaquet, R, Biserte, G. The synthesis of amino acid polymers by thermal condensation at 105° without a catalyst.  Biochimie 57: 1395-1396, 1975.
   Heinz, B, Reid, W.  The formation of chromophores through amino acid thermolysis and their possible role as prebiotic photoreceptors.  BioSystems 14: 33-40, 1981.
  
Structure and internal ordering:
   Turcotte, PA, Paolillo, L, Ferrara, L, Benedetti, E, Andini, S.  Structural characterization of thermal prebiotic polypeptides.  J. Mol. Evol. 7: 105-110, 1976.
   Rohlfing, DL.  Thermal poly-a-amino acids containing low proportions of aspartic acid.  Nature 216: 657-659, 1967.
   Tyagi S, Ponnamperuma C  Nonrandomness in prebiotic peptide synthesis.  J Mol Evol 1990 May;30(5):391-9 
    Melius P. Structure of thermal polymers of amino acids. Biosystems 1982;15(4):275-80 Jul;8(2):45-50
   SW Fox, Stereomolecular interactions and microsystems in experimental protobiogenesis.  BioSystems 7: 22-36, 1975
  SW Fox, Self-sequencing of amino acids and origins of polyfunctional protocells.  Origins of Life, 14: 485-488, 1984.
  Temussi, PA, Paolillo, L, Ferrara, L, Benedetti, I, Aninin, S.  Structural characterization of thermal prebiotic polypeptides.  J. Mol. Evol. 7: 105-110, 1976.
  Pivcova, H, Saudek, V, Drobnik, J, Vlasak, J.  NMR study of poly (aspartic acid) I. a- and b-peptide bonds in poly(aspartic acid) prepared by thermal polycondensation.  Biopolymers 20: 1605-1614, 1981.
  Nakashima, T, Jungck, JR, Fox, SW, Lederer, E, Das, BC.  A test for randomness in peptides isolated from a thermal polyamino acid.  Intl. J. Quantum Chem. QBS4: 65-72, 1977.
   Luque-Romero MM, de Medina LS, Blanco JM.  Fractionation and amino acid composition of an aspartic acid-containing thermal  proteinoid population.  Biosystems. 1986;19(4):267-72.
  Bahn, P. and A. Pappelis. 2001. HPLC evidence of nonrandomness in thermal proteins. In First Steps in the Origin of Life in the Universe. Julián Chela-Flores, Tobias Owen, and François Raulin, eds., Kluwer Academic Publishers, Dordrecht, The Netherlands. Pp. 69-72.
   Bahn, P. and A. Pappelis. 2001. IR spectra of protein, thermal protein, and thermal glycoprotein. In First Steps in the Origin of Life in the Universe. Julián Chela-Flores, Tobias Owen, and François Raulin, eds., Kluwer Academic Publishers, Dordrecht, The Netherlands. Pp.73-76.

Thermal proteins from DL and nonproteinous amino acids
   Saunders MA and Rohlfing DL, Inclusion of nonproteinous amino acids in thermally prepared models for prebiotic protein.  Biosystems 6. 81-92, 1974.
 
Metabolism:
  Rohlfing, DL, Fox, SW.  Catalytic activities of thermal polyanhydro-a-amino acids. Advances Catal. 20: 373-418, 1969.

Hydrolysis (energy gaining):
  p-nitrophenyl acetate
      Fox, S., Harada, K. Rohlfing, DL  The thermal copolymerization of a-amino acids. In Stahmann, MA (ed) Polyamino Acids, Polypeptides, and Proteins (Univ. of Wisconsin Press, Madison) 47-54, 1962
      Rohlfing DL and Fox, SW.  The catalytic activity of thermal polyanhydro-a-amino acids for the hydrolysis of p-nitrophenyl acetate.  Arch. Biochem. Biophys. 118: 127-132, 1967.
      Usdin, VR, Mitz, MA, Killos, PJ.  Inhibition and reactivation of the catalytic activity of a thermal a-amino acid copolymer.  Arch. Biochem. Biophys. 122:  258-261, 1967.
 
  p-nitrophenyl phospate
       Oshima, T.  The catalytic hydrolysis of phosphate ester bonds by thermal polymers of amino acid.  Arch. Biochim. Biophys. 126: 478-485, 1968.
  
  Decarboxylation
       Glururonic acid:  Fox, SW and Krampitz, G.  The catalytic decomposition of glucose in aqueous solution by thermal proteinoids.  Nature 203: 1362-134, 1964
       Pyruvic acid:  Hardebeck, HG, Krampitz, G, Wulf, L.  Decarboxylation of pyruvic acid in aqueous solution by thermal proteinoids.  Arch. Biochem. Biophys.  123: 72-81, 1986.
       Oxaloacetic acid:  Rohlfing, DL  THe catalytic decarboxylation of oxaloacetic acid by thermally prepared poly-a-aminoacids.  ARch. biochem. Biophys. 118: 468-474, 1967.
  
  Deamination
       Krampitz, G, Haas, W. Baas-Diehl, S.  Glutaminsaure-Oxydoreductase-Aktivitat von polyanhydro-a-aminosauren (proteinoiden).  Naturwissenschaften 55: 345-346, 1968.

Anabolism:
   Amination:  Krampitz, g, Baars-Diehl,S, Haas, W, Nakashima,T.  Aminotransferase activity of thermal polylysine.  Experientia 24: 140-142, 1968. 
Kolesnikov, M.P. 1991. Proteinoid microspheres and the process of prebiological, photophosphorylation. Origins of Life and Evolution of the Biosphere 21: 31-37.  ADP + Pi + light  yields ATP
  
    RNA/DNA:  JR Jungck and SW Fox, Synthesis of oligonucleotides by proteinoid microspheres acting on ATP.  Naturwissenschaften, 60: 425-427, 1973.
  
   Peptides:
      T Nakashima and SW Fox, Synthesis of peptides from amino acids and ATP with lysine rich proteinoid.  J. Mol. Evol. 15: 161-168. 1980.
      Fox, SW, Jungck, JR, Nakashima, T. From proteinoid microsphere to contemporary cell: formation of internucleotide and peptide bonds by proteinoid particles. Origins of Life 5: 227-237, 1974.
      Nakashima, T, Fox, SW.  Formation of peptides by single or multiple additions of ATP to suspensions of nucleoproteinoid microparticles.  BioSystems 14: 151-161, 1981.
      Paecht-Horowitz M, Katchalsky A. J  Synthesis of amino acyl-adenylates under prebiotic conditions. Mol Evol 1973;2(2-3):91-8

Oxidoreductions:   H2O2 (catalase) and H2O2 and hydrogen donors (peroxidase reaction)
       Dose, K, Zaki,L.  The peroxidatic and catalase activity of hemoproteinoids. Z. Naterforsch 26b: 144-148, 1971.

   Photoactivated decarboxylation -- glycoxylic acid, glucuronic acid, pyruvic acid.
      Wood, A, Hardebeck, HG.  Light-enhanced decarboxylations by proteinoids. In Rohlfing, DL and Oparin, AI (eds) Molecular Evolution (Plenum, New York), 233-245, 1972. 

  Hormone:  Fox, SW, Wang, C-t.  Melanocyte-stimulating hormone activity in in thermal proteins of a-amino acids.  Science 160: 547-548, 1968.

Compartments within protocells:
  Brooke S, Fox SW. Compartmentalization in proteinoid microspheres.Biosystems. 1977 Jun;9(1):1-22.
  
Photosynthesis:
    Bahn PR, Fox SW.  Models for protocellular photophosphorylation.  Biosystems. 1981;14(1):3-14.
     Masinovsky Z, Lozovaya GI, Sivash AA, Drasner M.  Porphyrin-proteinoid complexes as models of prebiotic photosensitizers.  Biosystems 1989;22(4):305-10.
     Masinovsky Z, Lozovaya GI, Sivash AA.  Some aspects of the early evolution of photosynthesis.  Adv Space Res 1992;12(4):199-205.

Response to stimuli
  Przybylski AT. Excitable cell made of thermal proteinoids. Biosystems 1985;17(4):281-288.
  Vaughan G, Przybylski AT, Fox SW. Thermal proteinoids as excitability-inducing materials. Biosystems. 1987;20(3):219-23.
   Ishima Y, Przybylski AT, Fox SW.  Electrical membrane phenomena in spherules from proteinoid and lecithin.  Biosystems. 1981;13(4):243-51.
  Pappelis, A., S. W. Fox, R. Grubbs, and J. Bozzola. 1998. Animate protocells from inanimate thermal proteins: Visualization of the Process. In Exobiology: Matter, Energy, and Information in the Origin and Evolution of Life in the Universe. J. Chela-Flores and F. Raulin, eds., Kluwer Academic Publishers, Dordrecht, The Netherlands, Pp.195-198.

Growth and Reproduction:
   Fox, SW, McCauley, RJ, Wood, A  A model of primitive heterotrophic proliferation.  Comp. Biochem. Physiol. 20: 773-778, 1967.
   Fox, SW.  Molecular evolution to the first cells. Pure Appld. Chem. 34: 641-669, 1973.
 
Communication:
    Hsu, LL, Brooke, S, Fox, SW.  Conjugation of proteinoid microspheres: a model of primordial communication.  Curr. Mod. Biol. (now BioSystems) 4: 12-25, 1971.
 

lucaspa

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Protocells as units of evolutionary selection:
Matsuno K Natural self-organization of polynucleotides and polypeptides in protobiogenesis: appearance of a protohypercycle. Biosystems 1982;15(1):1-11
Kenyon, DH. Prefigured ordering and protoselection in the origin of life. In Dose, K, Fox, SW, Deborin, GA, and Pavlovskaya, TE (eds) The Origins of Life and Evolutionary Biochemistry (Plenum Press, New York), 207-220, 1974.
Fox SW. Molecular selection and natural selection. Q Rev Biol. 1986 Sep;61(3):375-86.

Beginnings of genetic code:
Nakashima T, Fox SW. Selective condensation of aminoacyl adenylates by nucleoproteinoidmicroparticles (prebiotic-lysine-model system-genetic code).Proc Natl Acad Sci U S A. 1972 Jan;69(1):106-8.
Yuki A, Fox SW. Selective formation of particles by binding of pyrimidine polyribonucleotides orpurine polyribonucleotides with lysine-rich or arginine-rich proteinoids.Biochem Biophys Res Commun. 1969 Aug 15;36(4):656-63.

Protocells as new domain of life
Pappelis A, Fox SW. Domain Protolife. Journal of Biological Physics 20: 129-132, 1994.
http://www.asa3.org/archive/evolution/199907/0062.html
 
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lucaspa

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A number of objections have been raised to the protocells in the forum. 

1.  "the statements being made these days about Fox's claims is dismissive, not favorable. "

I have looked thru the web. The following are couse notes, textbooks, and other sources where Fox's claims are not dismissed. The list is by no means exhaustive because I haven't completed the research yet.

http://www.resa.net/nasa/origins_life.htm

Courses mentioning protocells:
http://faculty.uca.edu/~johnc/cellev.htm
http://www.mhhe.com/biosci/genbio/maderbio6e/outlines/ch20out.mhtml
http://www1.br.cc.va.us/monger/Biology/Lecture/OriginandHistoryofLIfe.htm
http://www.gpc.peachnet.edu/~larmstea/1403originlifenot1.html
http://www.tufts.edu/as/wright_center/cosmic_evolution/docs/text/text_chem_4.html
http://www.tufts.edu/as/wright_center/cosmic_evolution/docs/text/text_chem_5.html
http://www.xs4all.nl/~sbpoley/abiog/virginiaorigin.htm
http://www.bios.niu.edu/Parrish/205.htm
www.kpbsd.k12.ak.us/sohi/rife/AP%20Biology/ AP%20Bio%20Ch%2016%20CMR%20Lect%20'00%20-.DOC
www.greenvilletech.com/biology/LesleyWilson/ Bio102Ch16notes.doc
http://www.bios.niu.edu/Parrish/205.htm
http://www.physics.queensu.ca/~phys214/lecture10.html
 http://dekalb.dc.peachnet.edu/~jaliff/evolutn.htm

Textbooks mentioning protocells
http://www.mhhe.com/biosci/genbio/maderbio6e/outlines/ch20out.mhtml
http://www.mhhe.com/biosci/genbio/raven6b/graphics/raven06b/other/ch04.pdf
http://www.planetarybiology.com/download/origin_of_earth_and_life.pdf
Principles of Cell and Molecular Biology_, Second Edition (1995) by Lewis J. Kleinsmith and Valerie M. Kish.

 

 
 
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lucaspa

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2. Protocells aren't like "real" cells.  Summarized in DNAunion's statement: "my objections to their being actual living cells is NOT based on contemporary cells – it is based on cells in general, even those that existed billions of years ago."

"In trains of electrical spiking action potentials are beginning to have a bedside flavor for a cardiology ward. Dr. Yoshio Ishima of the Tokyo Medical School studied those displaying regular rhythm and said he could not distinguish some from the recording of a heart. Hundreds of types of microspheres made from thermal protein all exhibit electrical activity. The principal ways in which the laboratory protocell meets the definition of life in the dictionary are in displaying growth, metabolism, reproduction and responsiveness in cells made by synthesis. By the process of cellular engineering, we can do a more meaningful job of arriving at a definition of life than by describing behavior of modern cells. This is a theme in a recent book titled Defining Life edited by Professor Martino Rizzotti of Padova, Italy, 1996. "  http://www.skeptictank.org/sidfox.htm

Look at that. Electrical activity that can't be told from heart cells!

"the coagulations do seem to resemble morphologically some of the most ancient microfossils as well as modern blue-green algae cells. These curious chemical proteinoids appear to possess many of the attributes of bona fide living organisms: they are cell-like spheres a few microns across, each possessing a thick shell-like membrane; most even appear to exhibit a primitive metabolism, with some dissipating away while others swell and bud (fig. 4). "  http://history.nasa.gov/CP-2156/ch0.htm

"They have a shape and size similar to bacteria, they have osmotic properties, they can catalyze some kinds of chemical reactions in their interiors, they grow and divide like coacervates, they have a selectively semipermeable double outer layer similar to a cell membrane, they take in polynucleotides, and they even exhibit primitive metabolic pathways."  http://pw1.netcom.com/~rogermw/Reich/bions.html

"microspheres have two-layered boundary which is osmoticallyactive, are gram - when stained"  http://www.anselm.edu/homepage/jpitocch/evolution/evolmacroevolution.html

Look at that one again.  Protocells are gram negative just like modern bacteria!

"microscopic examination they looked like tiny spherical (coccoid) bacteria, and were of the same size as such organisms. Taking time-lapse moving pictures of them, he believed he saw them undergo fision, or division of one globule into two. He called the coccoid objects proteinoids. He then examined them under the electron microscope. This revealed that these proteinoids possessed a membrane structure strikingly like that seen in cells. "  http://www.redlandsfortnightly.org/howell90.htm

"Florida biologist Sidney W. Fox has shown that simple heating of dry amino acids (as might happen on a dry planet) can create protein molecules. Once water is added, these proteins form the round, cell-like objects called microspheres, which take in material from the surrounding liquid, grow by attaching to each other, and divide. ..., microspheres resemble bacteria so much that experts have trouble distinguishing them by appearance."  http://zeno.as.arizona.edu/~lknutson/webdan/Textbook/CHAP_28.html%25
 
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Aceldama

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I had to re-read that a few times to understand it but it was worth it! Lucaspa your real cool! Although you most likely won't have a creationist reply to this thread, your hard work on this forum will open many minds and enhance everyones knowledge of the sciences.  

Three cheers for Lucaspa everyone!

 
 
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Late_Cretaceous

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I guess you just can't argue with all that evidence. Well, acutally you can. You could conduct research that would ultimately support of defeat the conclusions raised by these papers. You could also analyze the papers themselfs to find flaws in the methodology, statistical analysis or conclusions. Of couse this all takes time, which is probably what some diligent creationists are doing right now - and which is why none have posted any comprehensive rebuttals. Yet.


And now we wait.
 
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DNAunion

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Proteinoids (objections to their relevance)
Another, this time more skeptical, background quote will be provided.


Proteinoids are not proteins since: (1) their structures are branched because many bonds form between the wrong functional groups, (2) they contain both enantiomeric forms of amino acids, and (3) their sequences are not repeatable. And because no template is used for their production, proteinoids also lack genetic continuity: as a result, their ability to evolve is severely restricted, if it exists at all. In addition, despite Fox’s claims, their geological relevance is doubtful (that is, the conditions required for their production are considered by many to be unlikely in a real prebiotic setting).




“As noted in chapter 19, the proteinoids are not considered relevant to the origin of life by most researchers…” (Noam Lahav, Biogenesis: Theories of Life’s Origins, Oxford University Press, 1999, p284)
 
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Three Amino Acids Require Special Conditions
Three of the twenty amino acids found in contemporary cells decompose easily during the process of proteinoid formation.


Special measures must be taken in order for these three amino acids to be present in the final product.


Incorrect Bonds and Branching
In biological proteins, only alpha-peptide bonds occur. But in proteinoids, other forms exist as well.



 
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Both Enantiomers of Amino Acids



Before reading the next quote, one needs to have a basic understanding of the process of racemization. As explained elsewhere, amino acids come in two enantiomeric forms designated L- (left handed) and D- (right handed). A mixture that contains equal amounts of both forms is said to be racemic, while a mixture that contains only one of the forms is said to be pure (or resolved). If one starts with a pure mixture of L-amino acids and during the series of reactions some of them are converted into D- amino acids, such that the result is a racemic (50/50) mixture, then (complete) racemization has occurred.

 
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Unlikely Conditions for Formation


 
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Sequence Not Repeatable – No Genetic Continuity and No Ability to Evolve


 
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Proteinoid Microspheres (objections to their relevance)

Individual proteinoids can be coaxed into undergoing further physical changes that result in a spherical structure of bacterial size. These structures, called proteinoid microspheres, are claimed to possess many “cell-like” properties: but they don’t.





Perhaps Dean Kenyon summarizes the flaws of proteinoid microspheres the best.

 
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Metabolism?

It is sometimes claimed that proteinoid microspheres metabolize. If this claim is meant to relate somehow to cellular metabolism, it is false.


And surely Fox would not make the following statement if his proteinoid microspheres could already metabolize:


A likely explanation for this apparent misunderstanding by proteinoid microsphere supporters is that in some experiments, the microspheres did metabolize: but the reactions were actually carried out by enzymes extracted from true cells, and not by proteinoids themselves.

 
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Growth?

Cells that are actively progressing through the cell cycle undergo growth prior to division. This growth comes from within, as synthesis of proteins, DNA, and organelles occurs. Proteinoid microspheres, on the other hand, do not grow in a biological sense – they grow from the outside as simple attractive forces cause free proteinoids to aggregate to the microspheres and accrete on them.


 
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Binary Fission?

Another claim is that proteinoid microspheres can “reproduce” by “binary fission”. This process is also unrelated to the true biological processes.

“[Proteinoid microspheres] can be induced to undergo cleavage or division by suitable changes in pH or when exposed to MgCl2.” (Biochemistry: Second Edition, Albert L. Lehninger, Worth Publishers, 1975, p1047)


An external stimulus, such as a change in the pH, can cause them to divide – but there are no internal mechanisms behind this process.


So the division is not caused by any kind of a biological trigger, but rather by either merely exceeding a physical threshold (the microspheres enlarge to a point where the volume-to-surface-area ratio becomes too great and they split) or by manipulations of the pH.
 
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Bud Like Yeasts?

Another form of putative “reproduction” is that the “budding” process of proteinoid microspheres is similar to that of yeasts. This flawed belief is most likely due to the following sentence, from Lehninger’s first edition of Biochemistry:

“Moreover, if suspensions of microspheres are allowed to stand for 1 or 2 weeks, they undergo a budding process, akin to that of yeasts.” (Biochemistry, Albert L. Lehninger)

However, in his next edition, Lehninger modified that sentence, leaving off the words “akin to that of yeasts”. It should be pointed out that the reference to yeasts was not simply moved to a preceding or following sentence and/or paragraph – it was dropped completely.

“Moreover, if suspensions of microspheres are allowed to stand for 1 or 2 weeks, they undergo a budding process.” (Biochemistry: Second Edition, Albert L. Lehninger, Worth Publishers, 1975, p1047)

Others have noted the dissimilarities between the budding of proteinoid microspheres and yeasts.


That the buds do not have the metabolic properties of yeasts is only logical since proteinoid microspheres themselves do not metabolize.


“Buds” form “spontaneously” because of mere physical attraction of nearby, unbound proteinoids. That is not how yeasts form their buds. In addition, yeasts do not require mechanical agitation for their buds to become detached.


Yeasts don’t need to have someone heat them, spark them with electricity, or physically jolt them for their buds to separate.


“Reproduction” (Summary)
Even Fox refrains from attributing proteinoid microsphere “reproduction” to biological mechanisms.

 
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Synthesize Proteins?

The most outright “refutation” of the claim that proteinoid microspheres can produce protein comes directly from Fox himself.


A further indication that proteinoid microspheres cannot synthesize their own protein is stated by Fox later in his book, in a section entitled Evolution from the Protocell to the Contemporary Cell:


One needs to keep in mind several points when he or she encounters a statement such as the following.


First, the mentioned amino acids that join to form an oligopeptide are pre-activated – it is not the “protoribosome” itself that performs this task. In addition, the “protoribosome” was not composed simply of proteinoid – it also contained polynucleotides, which have not been synthesized under any plausible prebiotic conditions, let alone under those dry, high-heat conditions associated with proteinoid formation.
 
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Cell-Like Membrane?

Cells have membranes in which phospholipids are the primary structural component, and in which membrane-spanning proteins transport materials across the barrier the membrane forms. However, the “membranes” of proteinoid microsphere are lipid-free and do not carry out the functions of cellular membranes.


 
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