Enzyme Catalysis Lab

Enzyme Catalysis Lab - Enzyme Catalysis Lab NAME CLASS...

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Enzyme Catalysis Lab NAME CLASS TEACHER
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Abstract: After reviewing the basics of enzymes and catalysis, we take a dive into the wonderful world of catalase. Beginning with establishing a base line of just how much hydrogen peroxide there is in 5.0mL of the reacted solution; to figuring out exactly how much actually reacted after 300 seconds of catalyzed reaction. Follow the experiment from the beginning steps right to the end as you see where the students went wrong, interpretation of the results, and great answers to work sheet questions. Now, dive into the amazing world of catalase catalysis.
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Background Information: Enzymes are catalytic proteins, meaning they speed up – but do not create – chemical reactions, without being used up or altered permanently in the process. Although various enzymes use different methods, all accomplish catalysis by lowering the free energy of activation – activation energy – for the reaction, thus allowing it to occur more easily. Enzymes employ a variety of methods for performing catalysis. Some provide a micro environment within the active site where some of the side chains are H+ or OH- donors or receivers. Other enzymes work by bringing together substrates that would not normally meet outside the enzyme, or orienting them in a manner in which they would otherwise not occur. Still other enzymes stress the bonds of substrate molecules in order to make them easier to break; some take this a step further by actually forming temporary covalent bonds with the substrate molecules. Regardless of how it is done, all enzyme catalyzed reactions are reversible and will turn around when necessary. Each enzyme has a unique and highly complex structure, which is given rise to through the four levels of protein organization. The specific arrangement of the amino acids via polypeptide bonds is the primary structure of the protein. Formed by ribosomes and encoded in mRNA, the primary structure gives rise to all other levels of organization. Secondary structure is formed of α-helices and β-pleated sheets which are formed when twisting and folding polypeptides form hydrogen bonds along the nitrogenous backbone of the protein. The third level of organization, tertiary structure, consists of irregular loops and folds which form as the protein folds and are held in place be disulfide bridges and hydrophobic interactions. Disulfide bridges are strong covalent bonds that occur between the sulfurs of various amino acids; hydrophobic interactions occur when large numbers of hydrophobic side chains come together and ‘stick’ to one another. Quaternary structure, the fourth and final level of protein organization, occurs only when multiple polypeptides come together in a single protein. This structure is the final overall three- dimensional shape of the protein. As a result of four levels of organization, an enzyme has a very specific shape, which is
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Enzyme Catalysis Lab - Enzyme Catalysis Lab NAME CLASS...

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