Third Eye Vision

Its mechanism can be divided into two areas: the pathophysiology of brain structures and processes associated with autism, and the neuropsychological linkages between brain structures and behaviors.[69] The behaviors appear to have multiple pathophysiologies.[25]


Pedantic communication.

Pedantry is related to personality. One study found that extraverts were more tolerant of typing mistakes than introverts.
Etymology

The English language word "pedant" comes from the French pédant (used in 1566 in Darme & Hatzfeldster's Dictionnaire général de la langue française) or its older mid-15th century Italian source pedante, "teacher, schoolmaster". (Compare the Spanish pedante.) The origin of the Italian pedante is uncertain, but several dictionaries suggest that it was contracted from the medieval Latin pædagogans, present participle of pædagogare, "to act as pedagogue, to teach" (Du Cange).[2] The Latin word is derived from Greek παιδαγωγός, paidagōgós, παιδ- "child" + ἀγειν "to lead", which originally referred to a slave who escorted children to and from school but later meant "a source of instruction or guidance".[3][4]

The term in English is typically used with a negative connotation to refer to someone who is over-concerned with minutiae and whose tone is condescending.[5] Thomas Nashe wrote in Have with you to Saffron-walden (1596), page 43: "O, tis a precious apothegmaticall [terse] Pedant, who will finde matter inough to dilate a whole daye of the first inuention [invention] of Fy, fa, fum". However, when the word was first used by Shakespeare in Love's Labour's Lost (1598), it simply meant "teacher".


"A Man who has been brought up among Books, and is able to talk of nothing else, is what we call a Pedant. But, methinks, we should enlarge the Title, and give it to every one that does not know how to think out of his Profession and particular way of Life." ―Joseph Addison, Spectator (1711)

There is much to cross examine when considering programing languages and the biology of the world. I understand some of the ships programming is having having trouble with anyominity? I'm not sure the true correlations here but I'm sure it integrates into the equation. The folks at the lab should review keratin vs. bridges.

https://en.wikipedia.org/wiki/Keratin
Cornification is the process of forming an epidermal barrier in stratified squamous epithelial tissue. At the cellular level, cornification is characterised by:

production of keratin
production of small proline-rich (SPRR) proteins and transglutaminase which eventually form a cornified cell envelope beneath the plasma membrane
terminal differentiation
loss of nuclei and organelles, in the final stages of cornification
Metabolism ceases, and the cells are almost completely filled by keratin. During the process of epithelial differentiation, cells become cornified as keratin protein is incorporated into longer keratin intermediate filaments. Eventually the nucleus and cytoplasmic organelles disappear, metabolism ceases and cells undergo a programmed death as they become fully keratinized. In many other cell types, such as cells of the dermis, keratin filaments and other intermediate filaments function as part of the cytoskeleton to mechanically stabilize the cell against physical stress. It does this through connections to desmosomes, cell-cell junctional plaques, and hemidesmosomes, cell-basement membrane adhesive structures.

Cells in the epidermis contain a structural matrix of keratin, which makes this outermost layer of the skin almost waterproof, and along with collagen and elastin, gives skin its strength. Rubbing and pressure cause thickening of the outer, cornified layer of the epidermis and form protective calluses, which is useful for athletes and on the fingertips of musicians who play stringed instruments. Keratinized epidermal cells are constantly shed and replaced.

These hard, integumentary structures are formed by intercellular cementing of fibers formed from the dead, cornified cells generated by specialized beds deep within the skin. Hair grows continuously and feathers moult and regenerate. The constituent proteins may be phylogenetically homologous but differ somewhat in chemical structure and supermolecular organization. The evolutionary relationships are complex and only partially known. Multiple genes have been identified for the β-keratins in feathers, and this is probably characteristic of all keratins.

Disulfide bridges
In addition to intra- and intermolecular hydrogen bonds, the distinguishing feature of keratins is the presence of large amounts of the sulfur-containing amino acid cysteine, required for the disulfide bridges that confer additional strength and rigidity by permanent, thermally stable crosslinking in much the same way that non-protein sulfur bridges stabilize vulcanized rubber. Human hair is approximately 14% cysteine. The pungent smells of burning hair and skin are due to the volatile sulfur compounds formed. Extensive disulfide bonding contributes to the insolubility of keratins, except in a small number of solvents such as dissociating or reducing agents.

The more flexible and elastic keratins of hair have fewer interchain disulfide bridges than the keratins in mammalian fingernails, hooves and claws (homologous structures), which are harder and more like their analogs in other vertebrate classes. Hair and other α-keratins consist of α-helically coiled single protein strands (with regular intra-chain H-bonding), which are then further twisted into superhelical ropes that may be further coiled. The β-keratins of reptiles and birds have β-pleated sheets twisted together, then stabilized and hardened by disulfide bridges.

Filament formation