Does Poly-Glutamate Concentration Effect Hydrophobic...

Does Poly-Glutamate Concentration Effect Hydrophobic...

(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 ... Show more content on Helpwriting.net ...The main reason why pineapple needs to be cooked when added to gelatin is its proteases will disrupt gelatin setting. This functional class of enzyme – proteases – promotes the formation of peptide bonds. This is done through hydrolysis reaction between amino acids; as a consequence, proteins become its consisted amino acids. The activity of proteases will interfere gelatin setting, which in other words, it will prevent the formation of collagen chains. Collagen triple–helix chains are unable to form since the enzyme will degrade each collagen strands into amino acids. Cooking pineapple by applying a large amount of thermal energy will denature enzymes contained in this fruit, including proteases. This denaturation will prevent proteases from its activity, and will not interfere with gelatin from

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