Exam2-2006 - BIO 361 EXAM 2 FALL 2006 NAME:_ ID:_ 1. Write...

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BIO 361 EXAM 2 FALL 2006 NAME:_________________________________________________ ID:_____________________________________________________ 1. Write Your name and ID on all pages 2. Write all answers in pen only 3. Make sure your exam has nine pages including this cover page Page 2 _______________ Page 3 _______________ Page 4 _______________ Page 5 _______________ Page 6 _______________ Page 7 _______________ Page 8 _______________ Page 9 _______________ Total _______________ Maximum of 100 points
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Name:___________________________________ ID:_________________________________ 2 A. It has been said that the accumulation of discarded unsuccessful experiments from the organic chemistry labs on the main campus into Roth Pond has led to the formation of a diversity of mutant species. Here are descriptions of the hemoglobins from some of these species. Using what you know about human hemoglobin A and recognizing that these are all mutant hemoglobins, indicate which property is most likely to be true for each of the mutant hemoglobins by circling the letter of the best answer. 1. This monomeric hemoglobin has its heme iron stabilized in the ferric (Fe +3 ) state. a. It is likely to bind oxygen with a low affinity hyperbolic saturation curve. b. It is likely to bind oxygen with a high affinity hyperbolic saturation curve. c. It is likely that this hemoglobin fails to bind oxygen at all. d. The oxygen binding curve for this hemoglobin will be hyperbolic but the information is insufficient to judge affinity. e. This hemoglobin will bind oxygen but will fail to undergo an oxygenation-linked conformational change. 2. This tetrameric mutant hemoglobin has a cavity into which pesticides can bind when the mutant protein is fully saturated with oxygen. The deoxygenated mutant protein fails to bind pesticides because the cavity is too small. The pesticides which are dumped into Roth Pond will probably: a. prevent the mutant protein from releasing oxygen. b. convert the oxygen binding curve to a hyperbolic curve without affecting the affinity of the protein for oxygen c. decrease the affinity of the mutant hemoglobin for oxygen but not necessarily eliminate sigmoidal oxygen binding. d. decrease both the affinity of the mutant hemoglobin for oxygen and the sigmoidicity of the oxygen binding curve. e. increase the affinity of the mutant hemoglobin for oxygen but not necessarily eliminate sigmoidal oxygen binding. 3. The model of cooperativity which best fits the behavior of the mutant hemoglobin in question 2 is: a. Monod-Wyman-Changeux b. Koshland-Nemethy-Filmer c. neither of the two models fits the described behavior. d. the behavior described in Question 3 is equally well explained by both models.
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Name:___________________________________ ID:_________________________________ 3 4. This tetrameric mutant hemoglobin binds oxygen with a distinctive pattern in which the apparent affinity for the first oxygen to go onto the protein is greater than that of the
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Exam2-2006 - BIO 361 EXAM 2 FALL 2006 NAME:_ ID:_ 1. Write...

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