Protein Folding Thwarts Any Theory of Abiogenesis

 Which came first—protein folding or cellular life? Clearly, protein folding never occurred outside the cell, because any protein folded outside the cell, even under laboratory-assisted mechanisms, would never have a “natural-selection” fit for a cell’s useful life. So, protein folding first occurred in a cell. How was the nucleosome’s genetic code able to code for all the processes before natural selection could blindly work it all out for determination of when and how a cell's needed proteins are  made and folded? Let us focus, though, on folding of an amino acid sequence, a polypeptide chain, into a 3-dimensional structure that proteins possess. The folding of a polypeptide chain must occur in fractions of a second if the cell is to have any use in its relatively short life span for the resultant protein. How serious is the problem?

“Some researchers noted that [, in a search made by a computer program for a correct folding of a specific protein,] the accuracy is not high enough for a third of its predictions, and that it does not reveal the mechanism or rules of protein folding for the  [protein folding problem](https://en.m.wikipedia.org/wiki/Protein_folding_problem)  to be considered solved.

“When studied  [outside the cell](https://en.m.wikipedia.org/wiki/In_vitro), the slowest folding proteins require many minutes or hours to fold.

“In 1969, Cyrus Levinthal noted that, because of the very large number of degrees of freedom in an unfolded polypeptide chain, the molecule has an astronomical number of possible conformations. An estimate of 3^300 or 10^143 was made in one of his papers.[70]  [Levinthal's paradox](https://en.m.wikipedia.org/wiki/Levinthal%27s_paradox)  is a thought experiment based on the observation that if a protein were folded by sequential sampling of all possible conformations, it would take an astronomical amount of time to do so, even if the conformations were sampled at a rapid rate (on the  [nanosecond](https://en.m.wikipedia.org/wiki/Nanosecond)  or  [picosecond](https://en.m.wikipedia.org/wiki/Picosecond)  scale).[71] Based upon the observation that proteins fold much faster than this, Levinthal then proposed that a random conformational search does not occur, and the protein must, therefore, fold through a series of metastable  [intermediate states](https://en.m.wikipedia.org/wiki/Reaction_intermediate) .”

That polypeptide chain (PC) undergoes folding by the ribosome for production of a stable protein. The fascinating thing here is how a PC  interacts with a ribosome for determination of the correct folding to be imposed on the PC.  A PC is capable of being folded into any one of an astronomically large number of different ways by the ribosome. How is the correct folding given the PC by the ribosome? Only one of a myriad possible foldings that a PC can assume, were it not for regulatory mechanisms (e.g., chaperone proteins) assisting the ribosome, will be imposed for the production of a complex protein crucial to a certain function/process/manufacture in a certain cell, and not be for production of a protein that would be not merely unnecessary for the cell, but could easily be for production of a protein that would ultimately be lethal to that cell’s reason for existence. There are, moreover, different types of ribosomes, each type having been specially coded for that type ribosome's existence with its type-specific capability to assist in normative imposition on the PC of the correct folding that the PC should assume (for it, in turn, to become the correct and stable protein needed), for “each type of ribosome manufactures characteristically distinct types of proteins.” These proteins might be any of a number of different designs/shapes. Some are exported from the cell, and others are for exclusive use within the cell for making all the cell’s structures in the cytoplasm, and some proteins are for the different types of ribosomes that are manufactured in the nucleosome. These ribosome-building proteins exit the cytoplasm and are then found in the nucleus through mediation of a number of different transport receptors  (karyopherins or importins); all this is for construction of more and various types of ribosomes in the nucleosome, they being readied for export into the cytoplasm, or they become part of a duplicate population of ribosomes needed before cell replication can proceed. 

Now, the aforementioned fact about ribosomal proteins being delivered from the cytoplasm to the nucleus squares the miracle.  How so? Consider the following quote (see source at [Ribosomes: Manufactured by Design, Part 1 - Reasons to Believe](https://reasons.org/explore/blogs/the-cells-design/ribosomes-manufactured-by-design-part-1))

“Because ribosomes are needed to make the proteins needed to make ribosomes, it becomes difficult to envision how this type of chicken-and-egg system could emerge via evolutionary processes. Protein synthesis would have to function optimally at the onset. If it did not, it would lead to a cycle of auto-destruction for the cell.

"Ribosomes couldn’t begin as crudely operating protein-manufacturing machines that gradually increased in efficiency—evolving step-by-step—toward the optimal systems, characteristic of contemporary biochemistry. If error-prone, ribosomes will produce defective proteins—including ribosomal proteins. In turn, defective ribosomal proteins will form ribosomes even more prone to error, setting up the auto-destruct cycle. And in any evolutionary scheme, the first ribosomes would have been error-prone.”

[Mark Roseman](https://www.quora.com/profile/Mark-Roseman-5) Biochemistry Professor (Emeritus in 2020) at Uniformed Services University of the Health Sciences (1979–present) says:  “To make proteins you need L-amino acids, which require complex metabolic pathways, which requires dozens of enzymes—[themselves] proteins—which require DNA for coding. A membrane does no good without transport proteins and an unbelievably complex apparatus for correctly inserting them into bilayers.

“You need an energy source to drive protein synthesis, something like an ATP cycle.

“Researchers in abiogenesis all agree that several elements are required to make a cell, and for a long time they pursued various ways that things can happen sequentially. But most of these hypothetical schemes find themselves stalled at some stage with chicken-and-egg dilemmas…. 

“[It is] hard to explain abiogenesis via a sequence of steps.” [end of quote]

Yes, it's difficult for anyone even to conceive any plausible scenario other than that in one fell swoop a creative act had to have occurred for the life of the first living cells of their kind, this in order that they should also have ability to replicate themselves before dying, and so on and so on.

 Do you think that ribosomes having ability to assist in imposing just the correct folding on a PC,  for result of a stable and needed protein, are the product of random mutations in the genetic code resident in a cell’s nucleosome? That is not a reasonable speculation, is it? No, certainly not! Far more reasonable is our recognition of the existence of a purposeful Creator who has wisdom and power for designing life forms suitable for existence and replication here on earth. The Bible identifies him by the name “Jehovah,” and the Bible says this about him: “With you is the source of life; By your light we can see light” (Psalm 36:9). 

For more information on the origin of life, follow this link: 

https://www.jw.org/finder?srcid=jwlshare&wtlocale=E&prefer=lang&pub=lf