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tanferret348Lv1

28 Sep 2019

List the stabilizing forces at tertiary level of protein structure. An enzyme containing the amino aspartic acid (pK_a of the side chain = 3.65) and histidine (pK_a of the side chain= 6) in the active (catalytic ) site has an optimal activity at a pH of 5.0. What is the major stabilizing force at the catalytic site? Using structures and 1-3 complete sentences, predict and explain what is expected to happen to the activity if the pH is increased to 8.

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Ignore the circled answers, some of them are wrong but I don't know which. What are the correct answers for questions 13-16?

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B. C. Mixed tive 8. The panereas is protected from digestion by trypsin (a proteolytic enzyme that it produces) because: A. B. C. D. Trypsin works only on denatured proteins Trypsin is specific for plant proteins Trypsin works only at the surface of membranes Trypsin is not activated until it is proteolytically modified 9. The active site of an enzyme is the region that A. binds allosteric regulators of the enzyme. B. is involved in the catalytic reaction of the enzyme C. binds noncompetitive inhibitors of the enzyme D. is inhibited by the presence of a coenzyme or a cofactor 10. According to the induced fit hypochesis of enzyme catalysis,which of the following is corect? A. The binding of the substrate depends on the shape of the active site B. Some enzymes change their structure when activators bind to the enzyme C. A competitive inhibitor can outcompete the substrate for the active site D. The binding of the substrate changes the shape of the enzyme's active site 11. Increasing the substrate concentration in an enzymatic reaction could overcome which of the following? A. denaturization of the enzyme B. allosteric inhibition C competitive inhibition D. saturation of the enzyme activity 12. Zinc, an essential trace element for most organisms, is present in the active site of the enzyme carboxypeptidase. The zinc most likely functions as a(n) A. competitive inhibitor of the enzyme B. noncompetitive inhibitor of the enzyme C. allosteric activator of the enzyme. D cofactor necessary for enzyme activity 13. Some of the drugs used to treat HIV patients are competitive inhibitors of the HIV reverse transcriptase enzyme. Unfortunately, the high mutation rate of HIV means that the virus rapidly acquires mutations with amino acid changes that make them resistant to these competitive inhibitors. Where in the reverse transcriptase enzyme would such amino acid changes most likely occur in drug-resistant viruses? A. in or near the active site B. at an allosteric site Cat a cofactor binding site D. in regions of the protein that determine packaging into the virus capsid the fever is not controlled? When you have a severe fever, what grave consequence may occur if A. destruction of your enzymes' primary structure B. removal of amine groups from your proteins C. change in the tertiary structure of your enzymes D removal of the amino acids in active sites of your enzymes 14.

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