5 Examine the image of a graph of fraction bound versus ligand concentration. The protein in question binds only one ligand per protein. Different points onthe graph are indicated by lettered boxes. Which lettered box is indicating the value used to represent the binding affinity of the ligand for the protein?(Indicate your response by clicking on the lettered box.)AY[L]D During Anfinsen's experiments with ribonuclease A, after denaturation of the protein with urea and 2-mercaptoethanol, what was the outcome when bothurea and 2-mercaptoethnal were removed from the system?Re-shuffling of disulfide bonds occurredRecovery of activityRecovery of about 1% activityThe enzyme remained inactiveO000

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Examine the image of a graph of fraction bound versus ligand concentration. The protein in question binds only one ligand per protein. Differe the graph are indicated by lettered boxes. Which lettered box is indicating the value used to represent the binding affinity of the ligand for the (Indicate your response by clicking on the lettered box.) A Y B [L]

Examine the image of a graph of fraction bound versus ligand concentration. The protein in question binds only one ligand per protein. Differe the graph are indicated by lettered boxes. Which lettered box is indicating the value used to represent the binding affinity of the ligand for the (Indicate your response by clicking on the lettered box.) A Y B [L]

Introduction to General, Organic and Biochemistry

11th Edition

ISBN:9781285869759

Author:Frederick A. Bettelheim, William H. Brown, Mary K. Campbell, Shawn O. Farrell, Omar Torres

Publisher:Frederick A. Bettelheim, William H. Brown, Mary K. Campbell, Shawn O. Farrell, Omar Torres

Chapter23: Enzymes

Section: Chapter Questions

Problem 23.20P

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Similar questions

5 Which of the following is a correct statement describing the induced-fit model of enzyme action? Substrates fit into the active site: (a) because both are exactly the same size and shape. (b) by changing their size and shape to match those of the active site. (c) by changing the size and shape of the active site upon binding.
5 At a very low concentration of a certain substrate, we find that when the substrate concentration doubles, the rate of the enzyme-catalyzed reaction also doubles. Would you expect the same finding at a very high substrate concentration? Explain.
1 Food can be preserved by inactivation of enzymes that would cause spoilage—for example, by refrigeration. Give an example of food preservation in which the enzymes are inactivated (a) by heat and (b) by lowering the pH.
0 Explain the relationship between transition-state analogs and abzymes.
8 The optimal temperature for the action of lactate dehydrogenase is 36°C. It is irreversibly inactivated at 85°C, but a yeast containing this enzyme can survive for months at —10°C. Explain how this can happen.
Why is amino acid activation called the second genetic code?
7 Enzymes are long protein chains, usually containing more than loo amino acid residues. Yet the active site contains only a few amino acids. Explain why the other amino acids of the chain are present and what would happen to the enzyme activity if the enzyme’s structure were changed significantly.
2 The enzyme trypsin is synthesized by the body in the form of a long polypeptide chain containing 235 amino acids (trypsinogen), from which a piece must be cut before the trypsin can be active. Why does the body not synthesize trypsin directly?