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ch07

Course Number: BIOCHEM Biochemist, Spring 2010

College/University: Wichita State

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Chapter 7: Protein Function Part I: Myoglobin and Hemoglobin Matching A) B) C) D) E) F) G) H) I) J) K) L) positively cooperative cyanosis His E7 decrease R hydrogen bonds increase symmetry His F8 ion pairs T hemolytic anemia 1. In the ______ form of hemoglobin, the iron ion is out of the plane of the porphyrin ring. Ans: K Level of Difficulty: Easy Section: 7.1.B Learning objective: Oxygen Binding to Myoglobin...

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7: Chapter Protein Function Part I: Myoglobin and Hemoglobin Matching A) B) C) D) E) F) G) H) I) J) K) L) positively cooperative cyanosis His E7 decrease R hydrogen bonds increase symmetry His F8 ion pairs T hemolytic anemia 1. In the ______ form of hemoglobin, the iron ion is out of the plane of the porphyrin ring. Ans: K Level of Difficulty: Easy Section: 7.1.B Learning objective: Oxygen Binding to Myoglobin and Hemoglobin 2. The conversion of hemoglobin from the T to the R form involves breaking C-terminal ______. Ans: J Level of Difficulty: Easy Section: 7.1.B Learning objective: Oxygen Binding to Myoglobin and Hemoglobin 3. An increase in pCO2 causes hemoglobin's affinity for oxygen to ______. Register to View AnswerLevel of Difficulty: Easy Section: 7.1.D Learning objective: Oxygen Binding to Myoglobin and Hemoglobin 4. Hemoglobin's subunits bind oxygen in a ______ manner. Register to View AnswerLevel of Difficulty: Easy Section: 7.1.C Learning objective: Oxygen Binding to Myoglobin and Hemoglobin 5. The absence of 2,3-BPG causes hemoglobin's affinity for oxygen to______. Ans: G Level of Difficulty: Easy Section: 7.1.D Learning objective: Oxygen Binding to Myoglobin and Hemoglobin 6. The ______ model of allosterism requires subunits to change conformation simultaneously. Ans: H Level of Difficulty: Easy Section: 7.1.D Learning objective: Oxygen Binding to Myoglobin and Hemoglobin 7. Sickle cell hemoglobin does not form fibers in the ______ form. Register to View AnswerLevel of Difficulty: Easy Section: 7.1.E Learning objective: Oxygen Binding to Myoglobin and Hemoglobin 8. When unstable hemoglobins are degraded, the products often cause cell lysis, leading to a condition called ______. Ans: L Level of Difficulty: Easy Section: 7.1.E Learning objective: Oxygen Binding to Myoglobin and Hemoglobin 9. When oxygen binds to heme, the oxygen forms a hydrogen bond with ______. Register to View AnswerLevel of Difficulty: Easy Section: 7.1.A Learning objective: Oxygen Binding to Myoglobin and Hemoglobin 10. Mutations that favor the oxidation of the heme iron to the +3 oxidation state can cause ______. Register to View AnswerLevel of Difficulty: Moderate Section: 7.1.E Learning objective: Oxygen Binding to Myoglobin and Hemoglobin Multiple Choice 11. Which of the following is not a ligand to the porphyrin ring Fe2+ ion in oxymyoglobin? A) His E7 B) His F8 C) Nitrogen atoms in the porphyrin ring D) Oxygen E) all are ligands Register to View AnswerLevel of Difficulty: Easy Section: 7.1.B Learning objective: Oxygen Binding to Myoglobin and Hemoglobin 12. Which gas does not bind to the porphyrin ring Fe2+ ion in myoglobin? A) NO B) CO C) CO2 D) O2 E) H2S Register to View AnswerLevel of Difficulty: Easy Section: 7.1.B Learning objective: Oxygen Binding to Myoglobin and Hemoglobin 13. Which of the following statements does not apply to the K value in the equation for the oxygen binding curve of myoglobin? A) It is numerically equal to p50. B) It is defined as that oxygen partial pressure at which half of the oxygen binding sites are occupied. C) It is a measure of the affinity of myoglobin for oxygen. D) If Y > K, then myoglobin is less than 50% saturated with oxygen. E) It is the value of pO2 at which Y = 0.5. Register to View AnswerLevel of Difficulty: Easy Section: 7.1.D Learning objective: Oxygen Binding to Myoglobin and Hemoglobin 14. When the partial pressure of oxygen in venous blood is 30 torr, the YO2 value for myoglobin is ______ while the YO2 value for hemoglobin is ______. A) 0.55, 0.91 B) 0.91, 0.55 C) 2.8 torr, 26 torr D) 0.91, 0.97 E) none of the above Register to View AnswerLevel of Difficulty: Moderate Section: 7.1.D Learning objective: Oxygen Binding to Myoglobin and Hemoglobin 15. Myoglobin and a single chain of hemoglobin have similar ______ structures. A) primary B) secondary C) tertiary D) quaternary E) none of the above Register to View AnswerLevel of Difficulty: Easy Section: 7.1.B Learning objective: Oxygen Binding to Myoglobin and Hemoglobin 16. Hemoglobin's p50 value is about ______ as great as myoglobin's p50 value. A) one-tenth B) half C) twice D) ten times E) twenty times Register to View AnswerLevel of Difficulty: Easy Section: 7.1.D Learning objective: Oxygen Binding to Myoglobin and Hemoglobin 17. The value of n in the Hill equation for hemoglobin is about ______ as great as the value for myoglobin. A) half B) twice C) three times D) five times E) ten times Register to View AnswerLevel of Difficulty: Moderate Section: 7.1.D Learning objective: Oxygen Binding to Myoglobin and Hemoglobin 18. Consider a hypothetical hemoglobin with a Hill coefficient of 1 and the same p50 value as normal hemoglobin. Choose the statement below that best describes the two proteins. A) There is a cooperative interaction between oxygen-binding sites in both the hypothetical and normal hemoglobins. B) The hypothetical hemoglobin has a greater oxygen affinity than normal hemoglobin. C) The oxygen binding curve for the hypothetical hemoglobin is hyperbolic, and the curve for normal hemoglobin is sigmoidal. D) The two hemoglobins would be able to deliver about the same amount of oxygen to the tissues. E) At pO2 less than p50, normal hemoglobin has a greater YO2 value. Register to View AnswerLevel of Difficulty: Moderate Section: 7.1.E Learning objective: Oxygen Binding to Myoglobin and Hemoglobin 19. Some abnormal hemoglobins have Hill coefficients that are ______ that of normal hemoglobin, indicating that their ability to bind oxygen cooperatively has been compromised. A) less than B) greater than C) much greater than D) about equal to E) cannot be determined from the information given Register to View AnswerLevel of Difficulty: Moderate Section: 7.1.E Learning objective: Oxygen Binding to Myoglobin and Hemoglobin 20. The Hill plot shows that the fourth oxygen binds to hemoglobin with ______-fold greater affinity than the first. A) 2 B) 5 C) 10 D) 20 E) 100 Register to View AnswerLevel of Difficulty: Moderate Section: 7.1.D Learning objective: Oxygen Binding to Myoglobin and Hemoglobin 21. Myoglobins secondary structure is primarily composed of ______________. A) parallel -sheets B) antiparallel -sheets C) -helices D) -bends E) helices Register to View AnswerLevel of Difficulty: Easy Section: 7.1.A Learning objective: Oxygen Binding to Myoglobin and Hemoglobin 22. Myoglobins primary physiological role is to facilitate oxygen ________. A) storage B) metabolism C) binding D) reduction E) diffusion Register to View AnswerLevel of Difficulty: Easy Section: 7.1.A Learning objective: Oxygen Binding to Myoglobin and Hemoglobin 23. If the gene for myoglobin is knocked out in mice, the mice: A) have larger lungs. B) respire extremely rapidly. C) have dark brown muscle tissue. D) appear normal, with lighter colored muscle tissue. E) have their growth stunted. Register to View AnswerLevel of Difficulty: Easy Section: 7.1.A Learning objective: Oxygen Binding to Myoglobin and Hemoglobin 24. Carbon monoxide binds to Heme: with A) a higher affinity than oxygen. B) resulting in the oxidation of the Fe(II) to Fe(III) C) in a manner that displaces carbon dioxide, causing CO2 poisoning. D) from the side opposite oxygen, resulting in a brown colored heme. E) with a lower affinity than oxygen. Register to View AnswerLevel of Difficulty: Easy Section: 7.1.A Learning objective: Oxygen Binding to Myoglobin and Hemoglobin 25. The primary structure of mammalian hemoglobin, an 2 2 tetramer, is approximately _____ identical to myoglobin. A) 2% B) 18% C) 50% D) 78% E) 98% Register to View AnswerLevel of Difficulty: Easy Section: 7.1.B Learning objective: Oxygen Binding to Myoglobin and Hemoglobin 26. In sickle-cell anemia, the negatively charged glutamic acid residue is replaced by the neutral amino acid ____________. A) tyrosine B) lysine C) valine D) adenosine E) glycine Register to View AnswerLevel of Difficulty: Easy Section: 7.1.E Learning objective: Oxygen Binding to Myoglobin and Hemoglobin 27. Which of the following increases the affinity of hemoglobin for oxygen: A) an increase in BPG concentration. B) the formation of N-terminal carbamates. C) increasing pH. D) all of the above E) none of the above Register to View AnswerLevel of Difficulty: Moderate Section: 7.1.D Learning objective: Oxygen Binding to Myoglobin and Hemoglobin 28. The most rapid way that erythrocytes adapt to high altitudes is: A) by producing genetically altered hemoglobins that have higher O2-binding affinities. B) by adopting the symmetry model of allosterism. C) by increasing the concentration of hemoglobin. D) by relying upon the simpler protein myoglobin. E) by increasing the intracellular concentration of BPG. Register to View AnswerLevel of Difficulty: Easy Section: 7.1.D Learning objective: Oxygen Binding to Myoglobin and Hemoglobin 29. Hemerythrin and hemocyanin are: A) human mutant hemoglobins with decreased oxygen affinity. B) hemoglobin variants that are found in animals at high altitude. C) synthetic derivatives of hemoglobins heme group used in artificial blood substitutes. D) oxygen transport proteins found in invertebrates. E) tetrameric hemoglobin derivatives containing only -chains (4 tetramers). Register to View AnswerLevel of Difficulty: Easy Section: 7.1.B Learning objective: Oxygen Binding to Myoglobin and Hemoglobin 30. The rearrangement of T-form hemoglobin to the R-form: A) occurs in each protein subunit independently when its heme binds oxygen. B) requires the binding of at least three oxygen molecules. C) increases the ion pairing interactions of the C-terminal amino acids. D) involves the movement of the Fe(II) into the heme plane. E) opens a central cavity for BPG binding. Register to View AnswerLevel of Difficulty: Moderate Section: 7.1.D Learning objective: Oxygen Binding to Myoglobin and Hemoglobin 31. Max Perutz investigation of the structure and function of hemoglobin primarily utilized___. A) X-ray crystallography B) NMR spectroscopy C) genomics D) mass spectroscopy E) genetic engineering Register to View AnswerLevel of Difficulty: Easy Section: 7.1.B Learning objective: Oxygen Binding to Myoglobin and Hemoglobin 32. While the binding of O2 to myoglobin as a function of pO2 is described by a simple __________ curve, the binding to hemoglobin is described by a more complex ______ curve. A) sigmoidal; hyperbolic B) hyperbolic; sigmoidal C) exponential; hyperbolic D) sigmoidal; bell-shaped E) hyperbolic; concave Register to View AnswerLevel of Difficulty: Easy Section: 7.1.C Learning objective: Oxygen Binding to Myoglobin and Hemoglobin 33. Hemoglobin S, the variant responsible for the misshapen red blood cells characteristic of the disease sickle-cell anemia, is potentially advantageous to heterozygotes because it confers some level of resistance to the disease _________. A) rickets B) AIDS C) cyanosis D) polycythemia E) malaria Register to View Answer Level of Difficulty: Easy Section: 7.1.E Learning objective: Oxygen Binding to Myoglobin and Hemoglobin 34. Which of the following is not true for the symmetry model of allosterism: A) the protein is an oligomer of symmetrically (or pseudosymmetrically) related subunits. B) the oligomer can exist in two conformational states which are in equilibrium. C) the ligand can bind to a subunit in either conformation. D) the molecular symmetry of the protein is conserved during the conformational change. E) none of the above. Register to View AnswerLevel of Difficulty: Easy Section: 7.1.D Learning objective: Oxygen Binding to Myoglobin and Hemoglobin 35. BPG stands for: A) biphenylglycine B) boronylphenylglutamate C) bisphosphoglycerate D) bisphenylglycerol E) betapropylglutamine Register to View AnswerLevel of Difficulty: Easy Section: 7.1.D Learning objective: Oxygen Binding to Myoglobin and Hemoglobin 36. Why is the decreased affinity of fetal hemoglobin for BPG advantageous? A) With fewer BPG molecules bound there are more heme residues available for O2 binding. B) Decreased BPG binding biases the fetal hemoglobin toward the R state. C) More free BPG is available to bind to adult hemoglobin, resulting in a shift to the R state. D) BPG is available to bind to fetal myoglobin, helping to release O2 in fetal muscle tissue. E) none of the above Register to View AnswerLevel of Difficulty: Moderate Section: 7.1.D Learning objective: Oxygen Binding to Myoglobin and Hemoglobin 37. The reaction of carbonic anhydrase catalyzes: A) the formation of carbamates with the concomitant release of protons B) C) D) E) the hydration of bicarbonate, resulting in the formation of carbonic acid the reduction of carbon dioxide with the concomitant consumption of protons the hydration of carbon dioxide, forming bicarbonate and protons the hydrolysis of carbamates with the concomitant consumption of protons Register to View AnswerLevel of Difficulty: Easy Section: 7.1.D Learning objective: Oxygen Binding to Myoglobin and Hemoglobin 38. During the T to R conformational shift, Fe(II) drags the F-helix via a bond to the side chain of ________. A) Leu F7 B) Leu F4 C) His F8 D) Leu FG3 E) Val FG5 Register to View AnswerLevel of Difficulty: Easy Section: 7.1.D Learning objective: Oxygen Binding to Myoglobin and Hemoglobin 39. If the binding of O2 to hemoglobin was characterized by a Hill constant of -1: A) hemoglobin would not be able to release bound O2. B) the O2 binding curve would be hyperbolic. C) the sequential model of allosterism would be eliminated as a reasonable model. D) the binding of the first O2 would decrease the affinity of the hemoglobin for O2. E) the binding of the first O2 would increase the affinity of the hemoglobin for O2. Register to View AnswerLevel of Difficulty: Easy Section: 7.1.D Learning objective: Oxygen Binding to Myoglobin and Hemoglobin 40. ______of the worlds human population carry a variant hemoglobin. A) 5% B) 25% C) 50% D) 75% E) 90% Register to View Answer Level of Difficulty: Easy Section: 7.1.D Learning objective: Oxygen Binding to Myoglobin and Hemoglobin

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Econ 100A: Intermediate MicroeconomicsSupplement SlidesWinter 2010(UCSC)Consumer Theory 2Winter 20101 / 14Dierent Types of Utility Functions:The following are some of the utility functions you will encounter in the course: Perfect complements Perf
UCSC - ECON - 100a
Econ 100A: Intermediate MicroeconomicsSupplement SlidesWinter 2010(UCSC)Consumer TheoryWinter 20101 / 11Consumer PreferencesAssumptions:Consumer preferences are: Complete: Any two bundles can be compared. Reexive: Any bundle is atleast as good as
UCSC - ECON - 100a
INTERNATIONAL ECONOMIC REVIEW Vol. 50, No. 3, August 2009INTERNATIONAL TRADE AND INDUSTRIAL DYNAMICS BY JOSH EDERINGTON AND PHILLIP MCCALMAN1 University of Kentucky, U.S.A.; University of California, Santa Cruz, U.S.A.In this article, industrial evoluti
UCSC - ECON - 100a
Journal of International Economics 74 (2008) 422 440 www.elsevier.com/locate/econbaseEndogenous firm heterogeneity and the dynamics of trade liberalization Josh Ederington a, Phillip McCalman ba b335 Gatton Building, Department of Economics, Universit
UCSC - ECON - 100a
Parallel Imports and the lot of a Starving ArtistAbstract This paper studies the role of copyright in the market for cultural output and how parallel imports aect the structure of incentives faced by artists. It demonstrates that parallel imports aect th
UCSC - ECON - 100a
MIDTERM REVIEW ECONOMICS 100A: Intermediate Microeconomics Instructor: Prof. Ryan Oprea Prepared by: Aadil Nakhoda BUDGET CONSTRAINTThe budget constraint can be described as the following equation: m = p1 x1 + p2 x2m = income p1 = price of good x1 p2 =