Advantages And Disadvantages Of Surfactant

When the pH is not at its optimum, the differing pH's will disrupt the bonding between the R groups of the amino acid causing its structure and the shape of the activation site to change

When some nonrenewables are processed, byproducts are created. These byproducts can be useful. For example, the byproducts of crude oil processing can be used to create chemicals, plastics, and common consumer items like bicycle tires and

Surfactants, when dropped in water, will try to spread across the surface of the water. While spreading along, it is also pushing away from the surface of the water. So when an object is placed onto the water, the surfactant is pushing the object away from the water, (while spreading), causing it to

(1) The attached graph from the assignment guide sheet demonstrates the conformation of poly-glutamate and poly-lysine in terms of their rate of specific rotation in relation to pH. In terms of poly-glutamate, which consists of multiple acidic amino acid glutamates, there is rapid change in conformation when pH has increased from 3 to 5. This amino acid becomes deprotonated when the pH increases, in which the concentration of hydrogen ion decreases correspondingly. For poly-lysine, which is the multiple basic amino acid lysines, there is rapid change in conformation when pH has decreased from 11.5 to 9.5. The decrease in pH indicates the increase in hydrogen ion concentration, and the lysines' side groups will be protonated. These deprotonation

More than 700,000 gallons of this dispersant was used above the sea surface and near the well head below the surface. Dispersants break up large globs of oil into smaller droplets to greater bacterial access and easier consumption, potentially increasing the rates of oil degradation. Surface area to volume ratio of oil greatly impacts the rate of bioremediation [1]. These chemicals, however, are highly toxic and have even been banned in the United Kingdom. Studies have shown that two years after the spill, artificial dispersants had increased the oil toxicity by 52 times [5].

Glutathione (GSH) is manufactured from three amino acids, and they are: cysteine, glutamine, and glycine.

Soluble state favors mere closer to protein in folding state which is like real functional environments.

are soluble in water and alcohol. Their NH group makes them pharmacologically active and are

In other words, l-homoarginine and l-arginine are homologous series, this implies that homoarginine and arginine have similar structure and the same chemical formula but differ by – CH2. Compounds within the same homologous series typically have a fixed set of functional groups that gives them similar chemical and physical properties. However, these properties typically change gradually along the series, and the changes can be explained by mere differences in molecular size and mass. Homoarginine is a solid in nature and has a melting point of 213-215oC. Homoarginine has a chemical formula C7H16N4O2 and a molecular weight of 188.231 g/mol and was first synthesized by Steib in 1926 and later identified in biological substance (e.g. plants) by Bell in 1962. The cationic amino acid homoarginine was later described by Ryan to be synthesize in animals including humans from arginine and lysine (Ryan and Wells, 1964a; Ryan et al., 1968; Ryan et al., 1969a), anaerobically rat liver, kidneys and the small intestine {Frenay, 2015 #202}; {Hou, 2015 #459}; {Pilz, 2015 #218}, including human brain {Bernstein, 2015 #176}, has the ability to synthesize

The fundamental texture of the film is made out of amphiphilic or double cherishing, phospholipid particles. The hydrophilic or water-cherishing regions of these particles are in contact with the watery liquid both inside and outside the cell. Hydrophobic, or water-loathing atoms, have a tendency to be non-polar. A phospholipid atom comprises of a three-carbon glycerol spine with two unsaturated fat particles connected to carbons 1 and 2, and a phosphate-containing bunch joined to the third carbon. This game plan gives the general atom a zone depicted as its head (the phosphate-containing gathering), which has a polar character or negative charge, and a territory called the tail (the unsaturated fats), which has no charge. They interface with

The specific and unique order in the polypeptide chain is determined by the information from the cellular genetic code of the protein. Having one amino acid in the structure causes the amino acid to not function properly or at all. There are four levels of protein structures, the primary structure, secondary structure, tertiary structure, and quaternary structure. The primary structure explains the order of which the twenty amino acids in proteins are held together to form a proper protein. The following amino acid structural characteristics are, carbons, hydrogen atoms, and carboxyl groups. Alpha Carbon is a necessity to hydrogen atoms, carboxyl groups, and the amino groups in protein structures. The secondary structure causes the structure to fold, curve, and make loops, that gives the protein its' dimentinal shape. The two types of secondary structures are alpha helix structures and beta pleated sheet. The alpha helix structure looks like a coil and is bonded by multiple hydrogens. The beta pleated sheet is folded and held together by hydrogen bonds in between polypeptide units. The third level, the tertiary structure is a broad dementinal structure that has several types of bonds and forces to keep the protein in tact. The shaping of a protein is caused by the hydrophobic interactions. Amino acids and hydrophilic will make a great amount of contact with their

Fortunately, the "side" chain R groups in silk are not very bulky. The basic primary structure of silk consists of a six amino acid unit that repeats itself. The sequence where every other unit is glycine in silk is: -gly-ala-gly-ala-gly-ala-. Although glycine and alanine make up 75-80% of the amino acids in silk, another 10-15% is serine and the final 10% contain bulky side chains such as in tyr, arg, val, asp, and glu.

Amino acid involves the organic compounds that are made of hydrogen, carbon, nitrogen and oxygen and in some circumstances, sulfur joined in typical formations. The sequences of amino acids structure proteins. Approximately 500 amino acids are identified even though 20 only appear in the genetic code and might be categorized in several ways. They may be classified according to the central structural useful groups ' parts as alpha- (α-), gamma- (γ-), beta- (β-) or delta- (δ-) amino acids. The other categories transmit to  pH level, polarity and side-chain group form included aromatic, acyclic, aliphatic, containing sulfur or hydroxyl. In proteins, amino acids encompass the second-largest constituent of cells as well as other tissues. Separate

The advantages are closely related to the diverse role of the organic solvent (ethers, alcohols, ketones or aldehydes) and organic constituents of the precursor (alkoxides or acetylacetonates) involved in the reaction mixture (Iqbal, et al. 2013). They act as oxygen-supplying agent for the formation of metal oxide and strongly influence particle size, shape, surface and assembly properties, and, in selected cases, even composition and crystal structure as well. Moreover, stabilizer plays vital role in sol-gel process. It prevents uncontrolled growth of particles and also prevents particles from aggregation. Amino ethanol’s such as monoethanol, diethanol and triethanol amines act as bidentate ligands to stabilize the solution against any precipitation thus producing clear

Chemicals can be injected into reservoirs to improve oil recovery and efficiency. Surfactants like alkaline have a tendency to alter the interfacial tension properties when injected which improves oil production. The main challenge introduced while flooding with chemicals is the adsorption and