The Absolute Homeostasis Energy Source Activated Protein Through 15 cm Thickness of Steel and Iron

　　

Proteins are the most versatile macromolecules in living systems and serve crucial functions in essentially all biological processes. They function as catalysts, transport and store other molecules such as oxygen, provide mechanical support and immune protection, generate movement, transmit nerve impulses, and control growth and differentiation.

Proteins can be composed of one or more polypeptides, each of which may be subject to post-translational modification. Interactions between a protein and either of the following may substantially alter the conformation of that protein: A cofactor, such as a divalent cation (such as Ca2+, Fe2+, Cu2+, or Zn2+), or a small molecule required for functional enzyme activity (such as NAD+) or a ligand (any molecule that a protein binds specifically).Four different levels of structural organization in proteins have been distinguished and defined (see Table 1.8).

Table 1.8 Levels of protein structure

Even within a single polypeptide, there is ample scope for hydrogen bonding between different amino acid residues. This stabilizes the partial polar charges along the backbone of the polypeptide and has profound effects on that protein’s overall shape. With regard to a protein’s conformation, the most significant hydrogen bonds are those that occur between the oxygen of one peptide bond’s carbonyl (C=O) group and the hydrogen of the amino (NH) group of another peptide bond. Several fundamental structural patterns (motifs) stabilized by hydrogen bonding within a single polypeptide have been identified, the most fundamental of which are described below.

The α-helix
This is a rigid cylinder that is stabilized by hydrogen bonding between the carbonyl oxygen of a peptide bond and the hydrogen atom of the amino nitrogen of a peptide bond located four amino acids away (Figure 1.27). α-helices often occur in proteins that perform key cellular functions (such as transcription factors, where they are usually represented in the DNA-binding domains). An amphipathic α-helix has charged residues on one side and hydrophobic residues on other side. Identical α-helices with a repeating arrangement of nonpolar side chains can coil round each other to form a particularly stable coiled coil. Coiled coils occur in many fibrous proteins which are long rod-like coiled coil forms such as α-keratin in hair, skin, and fingernails and fibrinogen in blood clots.

Figure 1.27 The structure of a standard α-helix and an amphipathic α-helix.
(A) The structure of an α-helix is stabilized by hydrogen bonding between the oxygen of the carbonyl group (C=O) of each peptide bond and the hydrogen on the peptide bond amide group (NH) of the fourth amino acid away, making the helix have 3.6 amino acid residues per turn. The side chains of each amino acid are located on the outside of the helix; there is almost no free space within the helix. Note that only the backbone of the polypeptide is shown, and some bonds have been omitted for clarity. (B) An amphipathic α-helix has tighter packing and has charged amino acids and hydrophobic amino acids located on different surfaces. Here we show an end view of such a helix: five positively charged arginine residues are clustered on one side of the helix, whereas the opposing side has a series of hydrophobic amino acids (mostly Ala, Leu, and Gly).The lines within the circle indicate neighboring residues－the initiator methionine (position 1) is connected to a leucine (2), which is connected to an arginine (3), which is adjacent to an alanine (4), and so on.

The β-pleated sheet
β-pleated sheets are also stabilized by hydrogen bonding but, in this case, they occur between opposed peptide bonds in parallel or anti-parallel segments of the same polypeptide chain (Figure 1.27). β-pleated sheets occur—often together with α-helices—at the core of most globular proteins.

Figure 1.28 The structure of a β-pleated sheet. Hydrogen bonding occurs here between the carbonyl (C=O) oxygens and amide (NH) hydrogens on adjacent segments of (A) parallel and (B) anti-parallel β-pleated sheets. [Adapted from Lehninger AL, Nelson DL & Cox MM (1993) Principles of Biochemistry, 2nd ed. With permission from WH Freeman and Company.]

The β-turn
The structure arises between the peptide bond CO group of n amino acid residues and the peptide bond NH group of n+3 amino acid residues to form hydrogen bonding and leads a hairpin β-turn. Abrupt changes in the direction of a polypeptide enable compact globular shapes to be achieved. It is named β-turn which can connect parallel or anti-parallel strands in β-pleated sheets.

Many more complex structural motifs, consisting of combinations of the above structural modules, form protein functional domains. After the primary structures fold up each other then the secondary structures pile up each other. Finally it forms compact area in the protein structures. Such functional domains usually represent functional units involved in binding other molecules. Another sulfhydryl (-SH) groups of two cysteines under same or different polypeptides usually combine to form disulfide bridges by covalent bonds. (Figure 1.29).

In general, the primary structure of amino acids sequences determines the sets of tertiary and quaternary structures. Secondary structural motifs (a-helix, β-pleated sheet, and β-turn) can be predicted from an analysis of the primary structure, but the overall tertiary structure cannot easily be accurately predicted. Except that some proteins form complex aggregates of simple polypeptide subunits, other many proteins still form complex compounds from aggregation of many polypeptides subunits.

Figure 1.29 Intrachain and interchain disulfide bridges in human insulin.
Disulfide bridges (-S-S-) form by a condensation reaction between the sulfhydryl (-SH) groups on the side chains of cysteine residues. They can form between cysteine side chains within the same polypeptide (such as between positions 6 and 11 within the insulin A chain) and also between cysteine side chains on different interacting polypeptides such as the insulin A and B chains.

Mr. Yuan Lin utilized the Absolute Homeostasis Energy Source to activate protein through 15 cm thickness of steel and iron. The purpose of this experiment proved that the Absolute Homeostasis Energy Source could activate protein through 15 cm thickness of steel and iron and affected the shape and structure of protein.

 

Mr. Yuan Lin and the second generation of the Sensory Humans, who is one year old, utilized the Absolute Homeostasis Energy Source to activate protein through 15 cm thickness of steel and iron. The purpose of this experiment proved that the second generation of the Sensory Humans could utilized the Absolute Homeostasis Energy Source to activate protein through 15 cm thickness of steel and iron and affected the shape and structure of protein.

 

Currently, the degree of research progress about the technique of original evolution,  we can accurately activate chromosomal DNA of cells in the body, we believe that we can apply to use this technique on each cell, tissue, organ, and system and lead human body to produce harder and tougher specific cells as muscular cells etc. to alternate evolution for aging.

This research paper is restricted by the rule of unpublished paper, only portion of the experimental outline is presented. The formal research report and the complete information of functional and technical and its practical application will be provided to the members of Chinese Association for the Human Evolution and specific responsible members of the specialized committees for the purpose of academic research for educational training whenever it is decrypted.

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