Proteins “evolve” (revisited)

By: James V. Kohl | Published on: October 20, 2017

Complex evolutionary footprints revealed in an analysis of reused protein segments of diverse lengths

Reported by Jay R. Feierman to the evolutionary psychology Yahoo Group as: Recycling at the molecular level: Protein evolution

Reuse patterns in protein space reflect 3.7 billion y of evolution (58), restrained by the underlying physicochemical qualities of covalently linked amino acids.

Autophagy links chirality from energy-dependent changes in electrons to ecosystems. For comparison, their claim is consistent with ridiculous misrepresentations of food energy-dependent biophysically constrained pheromone-controlled RNA-mediated amino acid substitutions and cell type differentiation. The truth about energy-dependent cell type differentiation is missing from this claim from Jordan et al., (2005) A universal trend of amino acid gain and loss in protein evolution.

Amino acid composition of proteins varies substantially between taxa and, thus, can evolve.

But wait, what happened to the claims about restraints by the underlying physicochemical qualities of covalently linked amino acids? Covalent bonds are energy-dependent. If you accept the claim that proteins “evolve,” you will probably accept whatever pseudoscientific nonsense is touted by any theorist. If you are a serious scientist, you already know that the physicochemical qualities of covalently linked amino acids have been detailed in the context of links from energy-dependent changes in electrons to ecosystems via the 2017 Nobel Prize winning technology referred to as cryo-EM.

See also: Codon identity regulates mRNA stability and translation efficiency during the maternal-to-zygotic transition

Figure 6 “Codon optimality code” in vertebrates provides an alternative perspective on sequence changes between paralogs in evolution and human disease.

“The bias between codons or amino acids, and mRNA expression levels has been previously recognized across species and is thought to result from selection for efficient, accurate translation, and folding of highly expressed genes…”

Simply put, natural selection for energy-dependent codon optimality links RNA-mediated amino acid substitutions in organized genomes from the physiology of reproduction to biophysically constrained viral latency via protein folding chemisty. That fact has never been addressed by neo-Darwinian theorists and probably never will be.

The fact that proteins have an energy-dependent atomic structure may never have occurred to an evolutionary theorist. If it had, a “Big Bang” cosmologist may have told the evolutionary theorist that the energy “emerged” from nothing, and that fact seems to be acceptable to all theorists.

See for comparison: Subatomic

Each player starts with the same small deck of cards that consist of Proton Cards, Neutron Cards, Electron Cards and Energy Cards and a beginning hand limit of 5 cards. They use these cards to build upon their current Atom, in an attempt to construct one of the available Atom Cards, and/or use their hand of cards to purchase more powerful atom building cards for later use, or increase their hand limit. The deck building cards are simple and clean, but offer a number of interesting combinations. Players also have an energy track that allows them to store energy, which introduces a “push-their-luck” type of mechanic enabling players to pay energy to shuffle through their deck quicker, or to offset the cost of more powerful deck building cards.

If you do not ask where the protons, neutrons and electrons come from, you can link atoms to ecosystems in all living genera outside the context of the energy[-dependent pheromone-controlled physiology of reproduction and RNA-mediated cell type differentiation.

See also: Atomic structure reveals how cells translate environmental signals

Translation is energy-dependent and the pheromone-controlled physiology of reproduction biophysically constrains virus-driven energy theft.


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