The previous publication establishing the precise locations via which the indolamine N,N-Dimethyltryptamine (DMT) [1] complete bio-molecular circuitry between an "ancient RNA-binding motif" in Sm Domain [2] and otherwise unexplined unusually placed C terminal extension Sml1 Complex [3, 4, 5] associated with temporary yet critical reconfiguration of fully activated standard protonated "amino acids" within hydroden saturated biochemically diverse environment, enabling dominant live amino's full control of complex steriochemical intermolecular processes associated RNA gene splicing - has been sealed for historical purposes and therefore will remian incomplete.
In addition to the above, numerous reports confirm evidence of mirrored negative positive circuitry system within the AMPA glutamate receptors (AMPARs) which are associated with dysfunctional RNA editing that additionally and also include an array of auxiliary subunits offering complex range of possible configurations [36, 37]. This provides clearer evidence of reverse configuration potentially requiring DMT to merely facilitate the reversal of standard amino acids basic actions, in addition to countless combinations of configurations dependant upon consciousness as critical component of DMTs stereochemically molecular facility. The United States of America Patent US202/0143051A1 provides comprhensive scientific evidence confirming the countless systems and pathways, running in conjuction with above via which the regular consumption of DMT (and similar "substances") are capable of preventing virtually every disease known to mankind [38]. However, the patent not appear to include consideration of scientific evidence regarding the consciousness of Amino Acids particularly in conjunction with the secondary configuration facilitated by DMT (etc) which is of critical relevance to the dangers associated with their capitalistically inspired "invention" designed to impair conciousness in conjunction with activating the hyperdivergent amino configurations the genetic systems involved. In addition to clear yet probably oversimplified example of the AMPARs - combine that with the complexities of it's interrelationship with the following systems.
The fact that someone was retarded enough to create a legal document full of scientific evidence mapping out the pathways such systems were obviously designed to work together just fine - whilst claiming ownership of inventing a way of advancing and retarding them at the same is fucken frightening. Especially given this was filed in 2020 during the pandemic!
The N-methyl-d-aspartate receptors (NMDAR) are nowhere near as clear as the AMPAR but some interesting things imediately stand out particularly the pH in the Nr1 subunit discussed later [39].
Additionally at a glance "Brain derived neurotrophic factor (BDNF) is the most prevalent growth factor in the central nervous system (CNS). It is essential for the development of the CNS and for neuronal plasticity." [40].
Of potential relevance to considering analyses of bloodplasma samples collected via Universal Assylums Experimental Research which I could have never imagined was going to prove such an evolutionary learning experience... "During opiate withdrawal, BDNF mRNA expression increases by 2- to 3-fold up to 3 days after opiate removal (Numan et al., 1998). This dramatic increase corresponds to enhanced TrkB receptor expression within 6 h of withdrawal (Numan et al., 1998)." [40]. Which is of particular relevance due to previously identified crossovers with viruses particularly in relation to T-Cells. "The activation of the mTORC1 pathway is coupled with diet mediated changes in the concentration of amino acids. Interestingly, the mechanism of sensing the amino acids through mTORC1 with the help of Rag GTPases as essential components of mTORC1 signaling was one of the groundbreaking discoveries in the field of mTOR signaling. This synergistic effect facilitates effective T-cell activation by upregulating mTOR function" [40].
According to Panwar, Vivek & Singh, et al (2023) "The mTOR belongs to the class of evolutionarily conserved threonine and serine kinases which recognize and incorporate a variety of extracellular and intracellular signals to maintain cellular homeostasis and metabolism 1–4 The name mTOR was obtained from rapamycin isolated from a soil bacterium in 1970 on Rapa NuFurther, the structural elucidation of the rapamycin revealed 14–16 membered lactone rings and reduced saccharide substituents... Mechanobiology of mTOR unfolds it as a complex protein kinase intricated with multi element complexes via its communication network with other proteins." [41]
This publication includes scientific evidence on conciousness and amino acid configurations worthy of consideration of the complexities associated with hyperdivergence of the interdependant systems above and will be sealed and continued in N,N-Dimethyltryptamine Converts Protonated Amino Acids to secondary configuration facilitating selective modulation of DBNF, mTOR & TrkB, AMPAR & NMDAR, & associated processes involved in mRNA coding!
Science is yet to reach a concensus on the origin of life, or "amino acids" which are recognised as sharing intimate coevolutionary relationships with RNA viruses for 4 billion years during which there is not shortage of evidence of amine's significant influence over protein development [25, 26]. Additionally rapidly increasing evidence of universally symbiotic interrelationships between amines and all forms of life, in conjunction with all natural elements included with existence. Obviously the only plausable explaination for this, along with coutless scientifically unresolved phenomenons of life - is that indolamines are the conscious co-creators and/or perhaps even the original procreators of life on earth. Unfortunatly, scientific discussion of the emergence of life on earth frequently fails to serve itself or amines justice by regurgitating the "building blocks of protein" hypothesis after having otherwise debunked with discussion of interactive responses to ecological conditons only possible if amines possessed "consciousness" initially likely to have required greater dependance upon what for many species has evolved to severe as a secondary configeration.
After over 4 billion years, 20 amino acids have remained common to all forms of life [27] with evidence suggesting this was initially as few as 10 [26]. According to CHEBI (2024) (CHEBI:83813) - there are 23 protonated amino acids. These include 20 in the standard genetic code, 9 of which: phenylalanine, valine, tryptophan, threonine, isoleucine, methionine, histidine, leucine and lysine are considered essential whilst the remaining 11: alanine, arginine, asparagine, aspartic acid, cysteine, glutamic acid, glutamine, glycine, proline, serine and tyrosine allegedly aren't essential. Plus selenocysteine and pyrrolysine as 21 & 22 which apparently can be genetically incorporated in translation (suggesting they are at least relatives)0 and finally 23 N-formylmethionine which appears genetically unidentified or undisclosed at this point in time. Despite the last 10 letters of N,N-Dimethyltryptamine confirming it is an indoleamine known for it's most significant direct interrelationships with tryptophan, likely to include complex combinations of both anabolic and catabolic processes under differnet conditions of critical significance to the coevolution of all life on earth. , and insummountable evidence of the critical significance of such interrelationships the UN and WHO
Maguire, et al pointed out 20years ago "the deletion of as few as three amino acids at the N terminus of L27 leads to an impaired PT (peptide) activity of E. coli ribosomes" [7]. This becomes particularly relevant when those three aminos are critically essential to facilitate periodically required fully charged equalibrium enabling Tryptophan and Tryptamine shared control over deviating from the typical amino configuration in coordinating complex combinations of multidirectional macrocyclic intermolecular interactions between protonated amines of both L and D amine variants. A great deal of evidence indicates an "unknown neurotransmitter" of male charactor, who's absence is associated with unhealthy imbalances [29] particularly associated with D-amino acids [34] contributing to most forms of disease and genetic degradation due to not having whats required to perform highly level RNA binding it's clearly designed for [3]. In addition to defective genetic expression some forms of splicing are unable to complete processes such as hydrolytic splicing [19] previously discussed in the original abandoned draft. 5-meo-DMT was also recently scientifically confirmed as having a role in RNA gene expression in studies unable to identify the pathways and actions by which this was so [24].
To oversimplify such complex concept for most of the week Tryptophan takes care of the amino offspring in the beautiful house she built with DMT who's basically away most the time working the equivelant of FIFO. These two are like the perfect couple with such great chemistry that even after billions of years when they finally see one another the rules change as DMT and Tryptophan bend one another over in ways science could even begin to imagine whilst pulling the kids into line working togather as a family to get on top of the fucken house. In an ideal world DMT's only been gone for a week so providing there's been no major issues after a quick once over they can invest their energy towards rennovations to keep up with the joneses. However, whlist Trypophans litterally a goddess, without a decent services of good hard D regular enough she enevitably falls behind. One of the facts of life is although Tryptophan couldn't handle him there all the time there are certain things she simply cannot do right without DMT some of which are of critical significance requiring them both to work as a team to ensure the kids do their chores on time and precisely how they're fucken told.
According to PubChem and CHebi at a pH of 7.3 DMT in it's ammonium form N,N-Dimethyltryptaminium is classified as live "Major Mircospecies" and Tryptophan and other essential protonated amino acids in appropriate forms are live "Major Species" alluding to the possiblity that they are individual entities, or perhaps a set of interconnected conscious equal opposite entities who worked quite well together for Four Billion years until humans severed thier loving relationship. High-level quantum mechanical computations, indicate that in gaseous state, as well as in the presence of single water molecule acting as a catalyst, and also in a water solvated environment - the reaction barrier is reduced making the aminium cation prone to inversion. Interestingly, in contrast to molecules with a carbon atom stereocenter, stereoinversion with a nitrogen stereocenter was observed as a three multi-step process with quite high, or perhaps particular, reaction barrier. Although "gas-phase stereoinversion in the aminium cation is predicted to be infeasible, even along the proton transfer pathway which involves significant quantum tunneling" (Kaur, Ramanpreet & Vikas,. 2017) [18]. Looking back to learn this was independently identified prior to reciting in the comprehensive work of Marija Liutkute, et al (2020) [6] conveniently and reassuringly on this very same subject.
Conciousness over apllying the above to the selection of placing any of the countless possible stereochemical combinations together as required is the only pluasable explaination for the level of harmonous intermolecular coordination associated with the comsumption of DMT as an essential activating such processes. Although yet to come across others with such a strong stance on aknowledging our olest known living anscesters who played a critical role in consciously collectively contributing to the coevolution of all life on earth. In addition to their official classification there is no shortage of evidence supporting the fact that even in their basic ridgid configuration amino acids have enough live in them to operative as heretical teams with influence over one another and a broad range of ecological contexts [6, 10, 11, 13, 14, 15, 16, 17, 18]. Considering this in contexts to N,N-Dimethlytryptaminium being a Major Microspecies associated with this group Major Species depending on language and cultural background some might even consider at the very least the "God" of the "Amino Acids". However, combining conciousness with the with scientific evidence of reactions to amino acids reflected across the coevolution of biodiversity of all living organisms accross the globe their dominance is perhaps the most flawless examples of a natural coevolutionary synergetic equilibrium in the history of right up until humans came along and fucked everything up.
Introducing what could well be our earliest known anscetors:
Tryptophan
Tryptophan (CHEBI:27897) is not live but is tautomer of...
Tryptophan Zwitterion (CHEBI:64554) obtained by transfer of a proton from the carboxy to the amino group of tryptophan is a Major Species at pH 7.3....
Incoming connection to both...
L-tryptophan zwitterion (CHEBI:57912) which is a Major Species at pH 7.3
D-tryptophan zwitterion (CHEBI:57719) having an anionic carboxy group and a protonated α-amino group a Major Species at pH7.3
D-Tryptophan is neither live nor a major species. However, is a carrier protiene and has a ligand protien structured with a highly useful extension so it's here for now encase of future relevance [13].
N,N-Dimethyltryptamine (CHEBI:28969) is not classed as live or a species but a conjugate base of...
N,N-Dimethyletryptanimium (CHEBI:193124 ) is a "LIVE" Major Mircrospecies at pH 7.3 [10].
Tryptaminium (CHEBI:57887) An ammonium ion that is the conjugate acid of tryptamine arising from protonation of the primary amino group; major species at pH 7.3.
Serotonin(1+) (CHEBI:350546) An ammonium ion that is the conjugate acid of tryptamine arising from protonation of the primary amino group; major species at pH 7.3. The interesting this about serotonin(+1) is it's aromatic position of it's six member ring given DMT's meythles can be used and exchanged in any combination to place any molicule anywhere it wants to spread any ring.
Interestingly N,N-Dimethyletryptanimium is classed as "Major Microspecies" as opposed to "Major Species" which could be a reason why tryptamines are not classed as amino acids.
Before proceeding to explore the protonated amino acidsthe picture shows the N-terminal beside the "ancient RNA-binding motif" beneath crystal structures of two Sm dimers, namely, D1D2 and BD3, revealed that the Sm motif represents an autonomously folding domain consisting of an N-terminal helix followed by five -sheets (21). [2]
Considering plausible possibilities for the mysteriously elusive meaning of [trypt] in N,N-Dimethyl-[trypt]-amine which has proven impossible get a straight answers on, Tony suggested the appropriately fitting [Tryp] = Bore [T] = Period of oscillation?
This will be covered in greater detail after examining the amino acids. However,the natre of this creepy set of "bore holes" to? Fits with the above account of Trypt, the difference between DMT and Tryptophan sexually being Major Microspecies and Species due to DMT's tiny cock and Atlas indicating male "unknown neurotransmitter" [29].
As tryptophan has been covered what western medicaine claims are the remaining Eight "essential" followed by the Eleven "non essential" standard and then the Three remaining protonated Amino Acids will be the following will summerise where possible otherwise directly quote PubChem and Chebi unless otherwise sighted;
Eight "essential" amino acids:
1) Phenylalanine
D-phenylalanine zwitterion is a D-alpha-amino acid zwitterion that is D-phenylalanine in which a proton has been transferred from the carboxy group to the amino group. It is the major species at pH 7.3
2). Valine
L-valine zwitterion is an L-alpha-amino acid zwitterion obtained by transfer of a proton from the carboxy to the amino group of L-valine; major species at pH 7.3.
3). Threonine
L-threonine zwitterion is zwitterionic form of L-threonine arising from transfer of a proton from the carboxy to the amino group; major species at pH 7.3.
4). Isoleucine
L-isoleucine zwitterion is an L-alpha-amino acid zwitterion obtained by transfer of a proton from the carboxy to the amino group of L-isoleucine; major species at pH 7.3
5). Methionine
L-methionine zwitterion is zwitterionic form of L-methionine having a anionic carboxy group and a cationic amino group; major species at pH 7.3.
6). Histidine
L-histidine is the L-enantiomer of the amino acid histidine. It has a role as a nutraceutical, a micronutrient, a Saccharomyces cerevisiae metabolite, an Escherichia coli metabolite, a human metabolite, an algal metabolite and a mouse metabolite. It is a proteinogenic amino acid, a histidine and a L-alpha-amino acid. It is a conjugate base of a L-histidinium(1+). It is a conjugate acid of a L-histidinate(1-). It is an enantiomer of a D-histidine. It is a tautomer of a L-histidine zwitterion [which includes an anionic carboxy group and a protonated alpha-amino group as a polar amino acid zwitterion]... D-histidine is an optically active form of histidine having D-configuration. It has a role as a Saccharomyces cerevisiae metabolite. It is a D-alpha-amino acid and a histidine. It is a conjugate base of a D-histidinium(1+). It is a conjugate acid of a D-histidinate(1-). It is an enantiomer of a L-histidine. It is a tautomer of a D-histidine zwitterion [a polar amino acid zwitterion restulting from the transfer of a proton from the carboxy group to the alpha-amino group & The major species at pH 7.3]... All of which asside from the zwitterions appear to include every combination of (+1 & +2) & (-1 & -2) variations.
7). Leucine
D-leucine zwitterion is a D-alpha-amino acid zwitterion arising from the transfer of a proton from the carboxy to the amino group of D-leucine; major species at pH 7.3.
8). Lysine
N(6)-acetyl-L-lysine zwitterion is an amino acid zwitterion obtained via transfer of a proton from the carboxy to the amino group of N(6)-acetyl-L-lysine; major species at pH 7.3.
According to PubChem (2024) "L-lysine is an L-alpha-amino acid; the L-isomer of lysine. It has a role as a micronutrient, a nutraceutical, an anticonvulsant, an Escherichia coli metabolite, a Saccharomyces cerevisiae metabolite, a plant metabolite, a human metabolite, an algal metabolite and a mouse metabolite. It is an aspartate family amino acid, a proteinogenic amino acid, a lysine and a L-alpha-amino acid. It is a conjugate base of a L-lysinium(1+). It is a conjugate acid of a L-lysinate. It is an enantiomer of a D-lysine. It is a tautomer of a L-lysine zwitterion and a L-Lysine zwitterion." [32] "Lysine (abbreviated as Lys or K) is an α-amino acid with the chemical formula HO2CCH(NH2)(CH2)4NH2. This amino acid is an essential amino acid, which means that humans cannot synthesize it. Its codons are AAA and AAG. Lysine is a base, as are arginine and histidine. The ε-amino group acts as a site for hydrogen binding and a general base in catalysis. Common posttranslational modifications include methylation of the ε-amino group, giving methyl-, dimethyl-, and trimethyllysine. The latter occurs in calmodulin. Other posttranslational modifications include acetylation. Collagen contains hydroxylysine which is derived from lysine by lysyl hydroxylase. O-Glycosylation of lysine residues in the endoplasmic reticulum or Golgi apparatus is used to mark certain proteins for secretion from the cell." [32].
In 2009 proteinaceous N-modification in lysine was discovered suggesting that the inclusion of DMT is likely to result in it acting as an animated amino group donor after which it is considered deanimated, which is reversable without distiction between acting as a donor or acceptor between direction as required subject to enzymic signals from DMT and possibly Tryptophan [30, 31]. Obviously this would not only allow the reverse of its actions but the reversability of the above which is also likely to include countless possible combinations capable of serving a broad range of purposes far beyond current scientific understandings. Nε-methylation of lysine residues found on unstructured N-terminal histone tails and core histones indicates a role in the regulation of of dynamic molecular scale amino interactions requiring continuous conscious complex calculations throughout time across countless combinations of variables associated with coevolving systems of life in their entirely [33]
Eleven "non essential" Amino Acids:
1). Alanine
L-alanine is the L-enantiomer of alanine. It has a role as an EC 4.3.1.15 (diaminopropionate ammonia-lyase) inhibitor and a fundamental metabolite. It is a pyruvate family amino acid, a proteinogenic amino acid, a L-alpha-amino acid and an alanine. It is a conjugate base of a L-alaninium. It is a conjugate acid of a L-alaninate. It is an enantiomer of a D-alanine. It is a tautomer of a L-alanine zwitterion [ arising from transfer of a proton from the carboxy to the amino group; major species at pH 7.3]
Standard
2). Arginine
Arginine (CHEBI:29016) is the amino acid with the formula (H2N)(HN)CN(H)(CH2)3CH(NH2)CO2H. The molecule features a guanidine group appended to a standard amino acid framework. At physiological pH, the carboxylic acid is deprotonated (−CO2−) and both the amino and guanidino groups are protonated, resulting in a cation. Only the l-arginine (symbol Arg or R) enantiomer is found naturally. Arg residues are common components of proteins. It is encoded by the codons CGU, CGC, CGA, CGG, AGA, and AGG. The guanidine group in arginine is the precursor for the biosynthesis of nitric oxide. Like all amino acids, it is a white, water-soluble solid. The one-letter symbol R was assigned to arginine for its phonetic similarity.
3). Asparagine
asparagine (CHEBI:22653) (symbol Asn or N) is an α-amino acid that is used in the biosynthesis of proteins. It contains an α-amino group (which is in the protonated −NH+3 form under biological conditions), an α-carboxylic acid group (which is in the deprotonated −COO− form under biological conditions), and a side chain carboxamide, classifying it as a polar (at physiological pH), aliphatic amino acid. It is non-essential in humans, meaning the body can synthesize it. It is encoded by the codons AAU and AAC. The one-letter symbol N for asparagine was assigned arbitrarily, with the proposed mnemonic asparagiNe; [Zwitterionic form of L-asparagine arising from transfer of a proton from the carboxy to the amino group; major species at pH 7.3.]
4). Aspartic acid
Aspartic acid (CHEBI:22660) An α-amino acid that consists of succinic acid bearing a single α-amino substituent. Capable of Hydrogen donor or acceptor.
Aspartic Acid has an overall negative charge and plays an important role in the synthesis of other amino acids and in the citric acid and urea cycles. Asparagine, arginine, lysine, methionine, isoleucine, and some nucleotides
5). Cysteine
"L-cysteine is an optically active form of cysteine having L-configuration. It has a role as a flour treatment agent, a human metabolite and an EC 4.3.1.3 (histidine ammonia-lyase) inhibitor. It is a serine family amino acid, a proteinogenic amino acid, a cysteine and a L-alpha-amino acid. It is a conjugate base of a L-cysteinium. It is a conjugate acid of a L-cysteinate(1-). It is an enantiomer of a D-cysteine. It is a tautomer of a L-cysteine zwitterion."... "Cysteine is a uremic toxin. Uremic toxins can be subdivided into three major groups based upon their chemical and physical characteristics: 1) small, water-soluble, non-protein-bound compounds, such as urea; 2) small, lipid-soluble and/or protein-bound compounds, such as the phenols and 3) larger so-called middle-molecules, such as beta2-microglobulin. Chronic exposure of uremic toxins can lead to a number of conditions including renal damage, chronic kidney disease and cardiovascular disease. Cysteine is a naturally occurring, sulfur-containing amino acid that is found in most proteins, although only in small quantities. Cysteine is unique amongst the twenty natural amino acids as it contains a thiol group. Thiol groups can undergo oxidation/reduction (redox) reactions; when cysteine is oxidized it can form cystine, which is two cysteine residues joined by a disulfide bond. This reaction is reversible: as reduction of this disulphide bond regenerates two cysteine molecules. The disulphide bonds of cystine are crucial to defining the structures of many proteins. Cysteine is often involved in electron-transfer reactions, and help the enzyme catalyze its reaction. Cysteine is also part of the antioxidant glutathione. N-acetyl-L-cysteine (NAC) is a form of cysteine where an acetyl group is attached to cysteine's nitrogen atom and is sold as a dietary supplement. Cysteine is named after cystine, which comes from the Greek word kustis meaning bladder - cystine was first isolated from kidney stones. As cysteine contains a sulphydryl group, it can undergo redox reactions. Oxidation of cysteine can produce a disulfide bond with another thiol, or further oxidation can produce sulphfinic or sulfonic acids. The cysteine thiol group is also a nucleophile and can undergo addition and substitution reactions. Thiol groups become much more reactive when they are ionized, and cysteine residues in proteins have pKa values close to neutrality, so are often in their reactive thiolate form in the cell. The thiol group also has a high affinity for heavy metals and proteins containing cysteine will bind metals such as mercury, lead and cadmiumtightly. Due to this ability to undergo redox reactions, cysteine has antioxidant properties. Cysteine is an important source of sulfur in human metabolism, and although it is classified as a non-essential amino acid, cysteine may be essential for infants, the elderly, and individuals with certain metabolic disease or who suffer from malabsorption syndromes. Cysteine may at some point be recognized as an essential or conditionally essential amino acid. Cysteine is important in energy metabolism. As cystine, it is a structural component of many tissues and hormones. Cysteine has clinical uses ranging from baldness to psoriasis to preventing smoker's hack. In some cases, oral cysteine therapy has proved excellent for treatment of asthmatics, enabling them to stop theophylline and other medications. Cysteine also enhances the effect of topically applied silver, tin and zinc salts in preventing dental cavities. In the future, cysteine may play a role in the treatment of cobalt toxicity, diabetes, psychosis, cancer and seizures."
6). Glutamic Acid
L-glutamic acid is an optically active form of glutamic acid having L-configuration. It has a role as a nutraceutical, a micronutrient, an Escherichia coli metabolite, a mouse metabolite, a ferroptosis inducer and a neurotransmitter. It is a glutamine family amino acid, a proteinogenic amino acid, a glutamic acid and a L-alpha-amino acid. It is a conjugate acid of a L-glutamate(1-). It is an enantiomer of a D-glutamic acid.
7). Glutamine
L-glutamine zwitterion is an amino acid zwitterion arising from transfer of a proton from the carboxy to the amino group of L-glutamine; major species at pH 7.3. It has a role as a metabolite. It is an amino acid zwitterion and a polar amino acid zwitterion. It is a tautomer of a L-glutamine.
But wait there's more
And more...
8). Glycine
Glycine is the simplest (and the only achiral) proteinogenic amino acid, with a hydrogen atom as its side chain. It has a role as a nutraceutical, a hepatoprotective agent, an EC 2.1.2.1 (glycine hydroxymethyltransferase) inhibitor, a NMDA receptor agonist, a micronutrient, a fundamental metabolite and a neurotransmitter. It is an alpha-amino acid, a serine family amino acid and a proteinogenic amino acid. It is a conjugate base of a glycinium. It is a conjugate acid of a glycinate. It is a tautomer of a glycine zwitterion.[an amino acid zwitterion arising from transfer of a proton from the carboxy to the amino group. It is also a fast inhibitory neurotransmitter.]
9). Proline
L-proline is pyrrolidine in which the pro-S hydrogen at position 2 is substituted by a carboxylic acid group. L-Proline is the only one of the twenty DNA-encoded amino acids which has a secondary amino group alpha to the carboxyl group. It is an essential component of collagen and is important for proper functioning of joints and tendons. It also helps maintain and strengthen heart muscles. It has a role as a micronutrient, a nutraceutical, an algal metabolite, a Saccharomyces cerevisiae metabolite, an Escherichia coli metabolite, a mouse metabolite and a member of compatible osmolytes. It is a glutamine family amino acid, a proteinogenic amino acid, a proline and a L-alpha-amino acid. It is a conjugate base of a L-prolinium. It is a conjugate acid of a L-prolinate. It is an enantiomer of a D-proline. It is a tautomer of a [L-proline zwitterion: the predominant species at physiological pH]
10). Serine
L-serine (CHEBI:17115) Serine (symbol Ser or S) is an α-amino acid that is used in the biosynthesis of proteins. It contains an α-amino group (which is in the protonated −NH+3 form under biological conditions), a carboxyl group (which is in the deprotonated −COO− form under biological conditions), and a side chain consisting of a hydroxymethyl group, classifying it as a polar amino acid. It can be synthesized in the human body under normal physiological circumstances, making it a nonessential amino acid. It is encoded by the codons UCU, UCC, UCA, UCG, AGU and AGC.
11). Tyrosine
L-tyrosine is an optically active form of tyrosine having L-configuration. It has a role as an EC 1.3.1.43 (arogenate dehydrogenase) inhibitor, a nutraceutical, a micronutrient and a fundamental metabolite. It is an erythrose 4-phosphate/phosphoenolpyruvate family amino acid, a proteinogenic amino acid, a tyrosine and a L-alpha-amino acid. It is functionally related to a L-tyrosinal. It is a conjugate base of a L-tyrosinium. It is a conjugate acid of a L-tyrosinate(1-). It is an enantiomer of a D-tyrosine. It is a tautomer of a L-tyrosine zwitterion.
D-tyrosine zwitterion is a D-alpha-amino acid zwitterion that is D-tyrosine in which a proton has been transferred from the carboxy group to the amino group. It is the major species at pH 7.3.
New Two
Selenocysteine
selenocysteine (CHEBI:9093) An α-amino acid that consists of alanine where one of the methyl hydrogens is substituted with a seleno group.capable of donating or accepting hydrogen,
Pyrrolysine
pyrrolysine (CHEBI:91273) An N-acyl-amino acid that is lysine in which one of the amino nitrogens at position N6 is replaced by a 3-methyl-3,4-dihydro-2H-pyrrole-2-carbonyl group.
Lucky Last
N-formylmethionine
N-formyl-L-methionine is a L-methionine derivative in which one of the hydrogens attached to the nitrogen is replaced by a formyl group. It has a role as a metabolite. It is a proteinogenic amino acid, a N-formyl amino acid and a L-methionine derivative
N-Formylmethionine is effective in the initiation of protein synthesis. The initiating methionine residue enters the ribosome as N-formylmethionyl tRNA. This process occurs in Escherichia coli and other bacteria as well as in the mitochondria of eucaryotic cells.
N-formyl-L-methioninate (CHEBI:57809) conjugate base of N-formyl-L-methionine; major species at pH 7.3.
So why does pH matter?...
According to linked Screenshot of the Weizmann Compass which I will qoute the most important of encase it's unclear & at a quick glance of the titles of his Dr. Italy Helevy's publications which include so many crossovers I don't have time to got though looking for a better direct qoute but would fucken love to have a chat about DMT and Tryptophan and their family of "Amino Acids" and how they fit with the everellusive universal ancestor of the evolutionary tree of life!...
"Dr. Itay Halevy of the Weizmann Institute’s Department of Earth and Planetary Sciences, together with Dr. Aviv Bachan of Stanford University, has developed a model of how seawater pH has changed since ancient times. Integrating data and existing models of the chemical makeup of the Earth’s atmosphere, oceans, and crust, the scientists’ new model identifies the main “culprit” behind seawater’s changing chemistry: the gradual decrease in atmospheric CO2 levels in response to an increase, over eons, of the brightness of the Sun.
According to the model, which was reported in Science, the oceans of the distant past were mildly acidic, then, over eons, acquired more alkaline pH levels.
The study found that three to four billion years ago, the pH of ocean water was acidic in the range of 6.0 to 7.5—somewhere between that of milk and human blood—as opposed to the more recent, relatively alkaline values of 7.5 to 9.0. The findings help clarify the chemical conditions under which primitive life emerged and thrived in the early oceans - and also help us understand the dynamic changes that contributed to the modern ocean’s chemical balance."
Also of potential relivence given life started out in the ocean Cited via Autry AE, Monteggia LM (2012) "there is also evidence that BDNF may directly activate voltage-gated sodium channels to mediate rapid depolarization of target neurons (Blum et al., 2002)" [40].
pH and the N-methyl-d-aspartate receptors NR1 subunit 3-4billion years later?
"NR1 subunit
The mRNA of the NR1 subunit begins to be expressed in the brain of the rat embryo as early as day 14 of gestation, and its levels gradually increase until 3 weeks after birth.14 There are 8 processing variants for NR1 mRNA (NR1-1a/4a y NR1-1b/4b), which differ among each other according to the presence or absence of a sequence of 21 amino acids (N1: exon 5) in the N-terminal region (Fig. 4), and differential processing of exons 21 and 22 which provokes changes in sequences in the C-terminal region (units C1, C2 and C2′)15,16 (Figs. 5 and 6). The N1 region is important for the regulation of channel properties, since it alters its sensitivity to spermine, pH, and zinc.17 In isoforms containing the N1 exon, neither polyamines nor Zn+increase stimulation by Glu, which may be due to it being a cation and its repulsion of the exon. The presence of the N1 exon is also linked to properties such as receptor affinity for agonists and their sensitivity to the antagonists APV ((2R)-amino-5-phosphonovaleric acid), CPP, 7-CK and MK-8 01. NMDAR sensitivity to pH is determined by the presence of exon 5. At physiological pH, receptors that include this variant are activated completely, while receptors that lack exon 5 are partially inhibited.18,19"r [1].
Now where were we?... That's right the fucken "Ancient RNA-Binding Motif", Sm Domain, Sml1 complex & PAT1. Where I started before finding a buch of better shit like usual!!
In their standard configuration amino acids are arguably live in a strict rigid kind of fashion in the sense of showing signs of hierarchy and influence between themselves and broader inflence in serving their many objectives. At a pH of 7.3 DMT is capable of converting into what is scientifically clasified as a live Major Mircrospecies along side a number of amino acid variations being live Major Species which will be identified shortly. Amino acids in their live actively charged states evidence suggest such entities collectively operate primarily between the N-terminal beside the "ancient RNA-binding motif" beneath crystal structures of two Sm dimers, namely, D1D2 and BD3, revealed that the Sm motif represents an autonomously folding domain consisting of an N-terminal helix followed by five -sheets (21). In both crystal structures, dimerization is brought about by an interaction of the 4 sheet of one Sm protein with 5 of the other, in line with biochemical and genetic evidence that the Sm domain is necessary and sufficient for the Sm proteins to form heteromers. Extrapolation of the Sm BD3 and Sm D1D2 structures, in conjunction with known interactions between the other Sm proteins, allowed the modeling of the Sm proteins into a sevenmember ring [2] and the mysterious unusually placed C terminal extension covering the opening of the Lsm1 comlex which has had scientists baffled for years [3, 4, 5]. Essentially DMT(s) temporarily reconfigures the entire extracellular matrix by converting amino acids such as Tryptophan in live Major Species capable of working collectively at an intermolecular steriochemical level to from a distant perspective manage the entire extracellular matrix facilitate thorough diagnostics and maintenance, including hardcore RNA genetic splicing in either direction. In addition to general maintenance and expression of 'tailor made' nutrition critical to maintaining levels of developmental divergence conducive of healthy coevolution.
PAT1 Protein?
PAT1 is a unique protein that contributes to the RNA binding activity which include the distinguishing feature of N Terminal on one end and C Terminal rather than typical motifs of other protein groups and science is unable to explain why one half appears consistently remaining unsued. Descriptions of used Pat1 protein consistently indicate that the remaining side that contains yeast and other properties that never get used creating all kinds of disregulation and degeneration which has science either rightfully concerned [6, 8]. Sometime scientists have even suggested PAT1 is a problem. However, Pati's job is to remain on standby for Tryptopant, Tryptamine and L-Tryptophan to arive and remove the crystal structure covering the "ancient RNA-binding motif" and N Terminal so it can support processes associated with gene splicing and possibly other activity. When placed together puts them in a jar or otherwise inappropriate context about all the can do standing around like a bunch of council workers [ 6, 7, 8]. Therefore, Pati is NOT "responsible for translational repression and decapping activation, ultimately leading to mRNP degradation."[6]. It is entirely possible that "human Pat1b (PatL1) proteins also have conserved roles in the 5'→3' mRNA decay pathway" [6] However, this is most likely due to DMT deprevation.. Available evidence suggests that the C and N terminals complete circuitry to reconfigure systems and processes support RNA gene spliceing between directions, and additional actions potentially requiring the otherwise unused Pat1 substrate that otherwise has little purpose but to remain on standby [7]. This may not be quit so simple though. Studies indicate the the N Terminal isn't required for yeast protien as opposed to the C-terminal extension which is required for RNA binding in vitro and Lsm1 function in vivo [22]. However, whilst it is likely that DMT in it's live Major Microspecies utalises the yeast protein portion of the PAT1 substrate along with glutamate and consumables associated with phosphorus, the reversibilaty of their fully activated state the N-terminal has the potential to come into play in othwise unforseeable manners.
The crystaline structure built over the ancient motifs and N-terminal require precisely coordinated intermolecular stereochemical processes enabling the major species amino acids to break the rules of their standard configureation. There is no shortage of evidence of evidence of amino acids forming hierarchy and regulating conditions even on a nanparticle scale [10, 13] which will receive futher attention shortly. Stereo-inversion in aminiums is considered highly unlikely because of a high reaction barrier. However, this also provides stability in preforming the type of high level molecular activity involved in RNA splicing which have been calculated to be of extreme difference between 5 and 6 ring configurations [5]. With the potential to be far greater with mention of possible a 7 ring configuration above [2]. Consciousness combined with fully charged combinations of the Major Species amino acids in a hydrogen saturated environment fits with their coevolution of the Sm Domain of multicellular organism such as a human beings and other animals is arguably the only way this is likely to occur.
The substantial scientific evidence of Amino Acids having significant influence over transitional metals such as (Pt) Platinum and (Y) Yttrium, and substrates associates with consitions of different scientific research is of potential relevance on many levels [11, 12, 13]. Nanotubes caused and infulenced by amino acids is a topic of great interest. The ≈8 nm diameter of platinum nanotubes [20] and the ≈8 nm diameter of the structures in B & C of Figure 1 [2] is of potential significance. In addition to potential actions in connecting the sight itself a plausible functional component of this could serve as an explanation for the phenomenon efficient means of purging processes associated with Ayahausca. One of these I have previously speculated is the activation of the apendix expelling toxins into the lower gastrointestinal tract which is consistent with anacdotal evidence of people experiencing the type of sensations one might expect to be associated with that shortly prior to the suddern urge to defecate. Whilst of great science interest to medical science the problem often arises as to how to control them [11] which obviously is the live microspecies of the amio acids group offer a perfectly natural solution. Platnum is also consiered to include 'species' with significant variation [21] yet to be fully explored in terms of the nature and definition of that. However, due to its prevelance in nature and interactoins amino acids is also the most likely plausable explaination to the biophysists description of the "ancient RNA-Binding motifs" having not real anchorage points and based on the appearance of the image [2] a such nanotubes would seem the only plausable explaination. Regardless they offer a useful evidence of the influecne of amines which I'll hand over leading into some rather complex closing considerations regarfing the subject.
The following quotes on the subject from an extensive study are of great interest supporting the above which create addition to complications or considerations for future scientific research in this area. "Lanreotide, a small peptide of eight amino acids, possesses all the molecular parameters driving its self-assembly in the presence of water. The self-assembly process of lanreotide is controlled by the balance between two opposite forces, i.e., hydrophobic effects, which result in water in an ‘‘attraction’’ between peptides and repulsive electrostatic interactions. Furthermore, the molecular parameters drive the molecular packing; and to obtain detailed information on these molecular parameters we adopted a site-directed mutational approach. We chose either to mutate residues that modify the confor- mation of the molecule or to successively substitute the three aromatic residues by a phenylalanine. Besides this precise purpose, the mutations we chose to apply to lanreotide are also related to more general questions. The influence of peptide conformation on molecular packing in self-assembly is, for example, relevant to amyloid peptides but also to bio- nanomaterials. In addition, p-stacking has been postulated as an important type of interaction driving amyloid fibril growth (3,27,55). Lanreotide and its derivatives are powerful tools in elucidating the involvement of pp interactions and the peptide backbone conformation in peptide self-assembling processes. Moreover, understanding these types of interac- tions can help to design new molecules capable of forming desired supramolecular architectures." [13]. This is of relevance due to their cooccurance in plants undoubtedly consumed to an unknown extent by animals and humans throughout history likely to to be included in ancient coevolutionary interrelationship with animals.
"Which molecular parameters drive self-assembly?
The idea that pp stacking is one of the driving forces of peptide-protein fiber formation emerged a few years ago. E. Gazit (56) reviewed studies on peptides extracted from the sequence of amyloid-forming proteins that kept the self- assembling properties of the entire protein. All these amino acid sequences contained a high number of aromatic residues. Knowing that aromatic residues are among the less frequently occurring amino acids, this observation is not trivial. More- over, directed mutations systematically replacing these amino acids by Ala showed that all but the aromatic amino acids can be replaced by Ala without changing the propensity for self- assembly. Indeed, the replacement of the aromatic residues by Ala completely inhibited this capacity. It was further sug- gested that pp stacking provides an energetic contribution as well as order and directionality to the self-assembly of amyloid structures.
The lanreotide sequence contains three aromatic amino acids in a total of eight. Besides these hydrophobic aromatic residues, it has two positive charges, which explain the high solubility of the peptide since nanotube assembly occurs at concentrations higher than 30 mM. Among the residues sub- stituted in this study, we successively mutated the three aro- matic residues into phenylalanine. We chose to mutate these aromatic side chains to another aromatic one and not, as Gazit did (56), to a simple Ala for two major reasons: i), we already knew from the segregation of the aromatic side chains in the self-assemblies that these residues played a major role in- volving pp stacking, and ii), we wanted to know if these aromatic residues had some specific features. The minimal mutations DNal-DPhe and Tyr-Phe strongly affect the sol- ubility of the peptide. Indeed, these two mutants do not form nanotubes or any other nanoscale self-assemblies based on extended intermolecular b-sheet, at least in the concentration range studied in this work, i.e., concentrations up to 10 times the critical concentration of lanreotide (300 mM). These re- sults indicate that these mutations together increased the solubility of the peptide and decreased its self-assembling propensity. The aromatic interactions in lanreotide nanotubes, consequently, not only are related to simple pp interactions but also involve some more specific interactions. For information, we also tested the mutation of DNal into DAla. The behavior of this peptide was comparable to that of the mutant reported in this work (data not shown). From this study, we conclude that two of the three aromatic residues in the lanreotide sequence are directly involved in the intermolecular peptide-peptide interaction. These results are also in agreement with the idea developed by C. Dobson that to avoid protein fiber formation, nature has developed strategies to increase the solubility of the protein in solution (20). The presence of aromatic residues that are generally hydrophobic decreases the solubility of the peptides/proteins. Furthermore, as they can interact through pp stacking, these residues can orient the peptide-peptide interactions. From our data, we propose that aromatic-aromatic interactions drive such a self- assembly process. In the case of lanreotide, we propose that the DNal and the Tyr, due to their capacities through pp interactions to orientate the self-assembly, represent the molecular ‘‘glue’’. Moreover, our experiments show that aro- maticity is not enough. In particular, the behavior of the Tyr- Phe derivative compared with that of lanreotide raises the question of the specificity of this aromatic side chain. In recent preliminary Raman experiments we showed a very unusual modification of the Tyr environment in relation to its pro- pensity to form H-bonds within the assemblies (57). Further experiments are required and have been undertaken to fully characterize the role of Tyr in the self-assembly process. However, this new molecular information supports the idea that at least part of the specificity of Tyr in lanreotide self- assembly is related to its capacity to act as an H-bound donor and/or acceptor. Of course, this conclusion does not exclude the involvement of the electron donor/acceptor properties of the aromatic cycle in the self-assembly process of lanreotide. Altogether, these results demonstrate that lanreotide self- assembly is driven by specific aromatic-aromatic interactions [13]."
Whilst the obvious sulution would seem to create an equalibrium of posistively and negitively charged amino acids together and observe how they interaction. If you consider that above in associaten with metal groups scientifically understood to be widely distributed in plants and soil across the globe, their photosynthetic qualities, reactions in spliting water [14, 15], synergy between Pt and Y, steriochemistry, the fact that platnum also appears to be classes of "species' [16, 17] and the order of command of amino acids and their influence on just about everything [13] and the potential influence of that picoscale "ancient RNA-binding motif" raised at the start?
This aditional conclusional quote from the above study leads into this reasonable wel...
"4, as only pp stacking is involved in this interaction.
The extreme sensitivity of the self-assembly processes of lanreotide to the molecular sequence of the peptide provides information that can be related to the molecular parameters driving amyloid-related self-assemblies. Finally, this work also describes some of the parameters necessary for the bottom-up design of new peptide families that self-assemble into tunable nanotubule or fibril architectures."
As previously raised in the unfinished drafts or mind maps supporting this publication, befor I came across those indiscreet ancient little motifs providing irrifutable evidence of the critical significance of DMT in human RNA gene splicing, we still absolutely nowwhere nere understanding where they even go???.... As previously speculated could it infact be a case of turning these little fuckers inside out?
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