Liza Chen, Ying-Tung Lin, and Yuan Lin |
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Introduction: Proteins are high molecular weight molecules. They exist in the cells of living organisms and each part of the cell. Proteins are diverse molecules. There are thousands of different kinds of proteins. Their molecular sizes can range from the smallest peptide bonds to extremely huge polymers. Their molecular weights in a single cell can reach tens of thousands. All proteins are composed by the same ubiquitin consisting of 20 amino acids and they are almost originated in the bacteria or complex creatures. The covalent bonding of linear sequences are the special characteristics. There are many ways to break down (hydrolyze) proteins into amino acids. When an amino acid dissolves in water, it will produce the dipolar ion or zwitterion. A zwitterion can act as either an acid (proton donor) or a base (proton acceptor). This substance has a dual nature, so it is also named amphoteric electrolyte. Amino acids exhibit special titration curves because of different acid-base properties. Monoamine-monocarboxylic amino acids (with non-ionized R groups) will be dicarboxylic acid at low pH values. It will produce many different ionic forms when the pH value is increased. Usually amino acids will make ionic R groups produce more ions due to the different pH value of the medium and the pKa of the R groups. Brönsted – Lowry theory: This equation is important for understanding buffer action and acid-base balance in the blood and tissues of vertebrates. From the Lambert-Beer law, we can see that absorbance is directly proportional to the concentration of the absorbing solute. I0:the intensity of incident light From the Brönsted-Lowry theory, Henderson-Hasselbalch equation, and Lambert-Beer law, we can figure out that the concentration of peptides and proteins relate to the biological functions. No generalizations can be made from research about the relationship among the peptide bond and protein molecular weight and its functions. Even the smallest peptide bond may have its biologically important effects. Many small peptide bonds exert their effects at very low concentrations. The concentrations of amino acids or proteins are related to their pKa, pI, and absorbance. These data can affect biological functions.
The purpose of this experiment is to prove that Mr. Yuan Lin, the first successfully-evolved New Human Line, can utilize the Absolutely Constant Energy Source (ACES) and the new biological engineering techniques to duplicate and constitute the energy state of sulfuric acid with energy to activate protein and affect its relative concentration without any change in its molecular weight, structural formula, and conformation, at 25℃, 1.0 atm, and pH 7.0, in a confined and isolated space, and with no contact with catalysts, biologically active substances, chemical substances, and physical action forces.
Test 1 Table 1. Comparison of absorbance at 590 nm between two treatments. Statistical analysis: Test 2 Table 2. Comparison of absorbance at 590 nm between two treatments. Statistical analysis: From the statistical analysis, we can see significant differences between two treatments. The samples treated with the energy state of sulfuric acid, duplicated and constituted with ACES by Mr. Yuan Lin, display higher relative absorbance than the untreated control samples, probably due to an increased strength of ionic bond or ionization in the samples. Amino acids are zwitterions which can act as either proton donors or proton acceptors and at the same time, ions of R groups of amino acids will increase more different ions due to the different pH value of the medium and the pKa of the R group. H2SO4 is a strong acid which can easily donate a positive charge (i.e. the hydrogen ion). Hydrogen bonds or ionic interactions are most favorable to protein structures. And a higher absorbance means a higher concentration of the solute. We can thus see that the treatment with the energy state of sulfuric acid, duplicated and constituted with ACES by Mr. Yuan Lin can affect the relative concentration of protein.
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