Critical values expose virus-driven energy theft

The scientific term “pH” is an abbreviation that stands for “potential of hydrogen,” which is a measure of the acidity or alkalinity of a solution.The term, which first came into use in 1909, is Germanic in origin and is derived from the word “potenz,” meaning power, plus “H,” which is the symbol for hydrogen on the periodic table.

The energy levels in a hydrogen atom can be obtained by solving Schrödinger’s equation in three dimensions. Because most people cannot do that, it may be more important for them to know that energy-dependent changes in hydrogen-atom transfer in DNA base pairs in solution must be linked to “conditions of life.”

When too much of the potential energy is used by a living organism or a virus, the organism dies. Theorists typically do not know that, or perhaps they simply don’t care where the energy came from.  Darwin claimed it must be linked from his “conditions of life” to all biodiversity via the physiology of energy-dependent reproduction.

That explains why theorists cannot trouble-shoot their ridiculous theories. If they were required to perform a blood gas analysis in a hospital medical laboratory, they probably would not understand that human life exists only in the biophysically constrained pH that ranges from ≤7.25 or ≥ 7.6. Theorists could not link calibrations and controls that are required to report accurate results to patient outcomes. Theorists are told that the outcomes are due to mutations and evolution.

See instead:Stat Profile Prime CCS Blood Gas Analyzer from Nova Biomedical

Measuring pH links nutritional epigenetics from the innate immune system to healthy longevity via everything known about virus-driven energy theft, which links nutrient stress and social stress to the replication of viruses, which link mutations to all pathology via critical care testing of other blood gas analytes such as pCO2, pO2, Sodium, Potassium, Chloride, Calcium, Glucose, Lactic Acid, and Hematocrit.

See also: Electrolytes induce long-range orientational order and free energy changes in the H-bond network of bulk water

The energy-dependent interaction between water and ions is omnipresent in biological processes related to enzymes, ion channels and protein folding.

See for comparison: DEPENDENCE OF RNA SYNTHESIS IN ISOLATED THYMUS NUCLEI ON GLYCOLYSIS, OXIDATIVE CARBOHYDRATE CATABOLISM AND A TYPE OF “OXIDATIVE PHOSPHORYLATION” (1964)

The synthesis of RNA in isolated thymus nuclei is ATP [energy] dependent. Experiments are described which show that the required ATP is produced by reactions associated with glycolysis, the citric acid cycle, and a type of oxidative phosphorylation. These pathways can be selectively inhibited by iodoacetate, fluoroacetate, and antymycin A, and RNA synthesis is blocked in the presence of these inhibitors. However, CO, which inhibits mitochondrial oxidative phosphorylation but does not block nuclear ATP synthesis, does not affect RNA synthesis in isolated nuclei or in whole cells. The use of CO as a selective inhibitor of mitochondrial ATP synthesis has made it possible to suppress cytoplasmic protein synthesis while allowing nuclear protein synthesis to continue.

See for comparison: A Global Analysis of the Receptor Tyrosine Kinase-Protein Phosphatase Interactome

Serine/threonine phosphorylation also has important effects on RTK signaling. We consistently found numerous PSP hits in our screens, although most of their functions remain unknown.

Reported as: First complete interactome map of human receptor tyrosine kinases and phosphatases

The researchers were surprised to find that some PTPs defy convention and act to promote RTK signalling suggesting that their roles are more complex than previously thought. For example, a phosphatase called PTPRA activates the EGFR, which is mutated in many cancers, revealing a new way in which cancer might spread. They also found two new phosphatases, PTPRB and PTPRH, which work as expected by grinding EGFR signalling to a halt, with potential anti-tumour properties.

Phosphorylation has long been suspected or known to be the energy-dependent molecular mechanism that enables the fixation of RNA-mediated amino acid substitutions. Ffixation of amino acid substitutions in supercoiled DNA protects all organized genomes from virus-driven energy theft and genomic entropy. That fact is placed back into the context of evolution of the  protein phosphatases from genes in this example of gene-centric theory.

… protein phosphatases evolved from distinct genes and employ different enzymatic mechanisms (Li et al., 2013). They are traditionally divided into two classes, protein Ser/Thr phosphatases (PSPs) and protein tyrosine phosphatases (PTPs). PSPs include the PPP, PPM, and FCP/SCP families (Li et al., 2013). The cysteine-based PTP superfamily includes about 100 members (Alonso et al., 2004; Tonks, 2006) grouped into classical PTPs and dual specificity phosphatases (DUSPs). Classical PTPs play critical roles in tyrosine kinase signaling (Neel and Tonks, 1997), whereas DUSPs can dephosphorylate Tyr and Ser/Thr residues. Some DUSPs function as lipid or glycogen phosphatases. The EYA family comprises a small set with an aspartate-based catalyticdomain (Alonso et al., 2004; Jemc and Rebay, 2007).

This is a potent obfuscation of the facts known to all serious scientists who have linked ecological variation to energy-dependent ecological adaptation via what is known about biophysically constrained protein folding chemistry.

PPPs are typically multi-subunit proteins, composed of a catalytic subunit and scaffold/regulatory subunits that serve to determine their substrate specificities.

The regulatory subunits are energy-dependent RNA-mediated amino acid substitutions. Theorists know that refutes their neo-Darwinian nonsense so they pretend not to know that substrate specificities are energy-dependent and that the energy is linked to species-specific differences in morphological and behavioral phenotypes by what organisms eat.

Here’s another misrepresentation of that fact.

A Single-Cell Roadmap of Lineage Bifurcation in Human ESC Models of Embryonic Brain Development

The human brain is a complex and highly evolved structure. Mouse models do not fully recapitulate cell-type diversity or lineage trajectories of the human brain (Florio et al., 2015; Konopka et al., 2012; Pollen et al., 2015; Reilly et al., 2015; Silbereis et al., 2016; Thomsen et al., 2016). Furthermore, human neurodevelopmental diseases such as autism spectrum disorders and schizophrenia are incompletely modeled in mouse.

The only way to keep fooling people into believing that the human brain evolved, is to keep teaching them to ignore what is known about energy-dependent autophagy.

See for example: Autophagy fan club