Please answer all obWhich of the following is true about myoglobin and/or hemoglobin?snaa. The iron in hemoglobin is in the ferric (Fe³+) state pe od 1911Ab. Myoglobin is commonly found in the circulatory systemswoldc. Both myoglobin and hemoglobin contain a fold of 8 a-helicesd. Hemoglobin is homotetramersnsonco muhdillups arb 1911A .bWhich of the steps below happens first in the O₂ binding to Mb and Hb?a. The proximal histidine moves toward heme noiden s to onerob. O₂ binds to the iron of heme6ta noitianstad to noissitids12.6c. The F helix moves toward heme: 101 risq svitemstis obivo19 dd. Iron moves into the plane of hemel 2016112duz to noiiconsho16luaslomFor reversible binding between a protein P and a ligand Lowolba. The units of Kare M-1 no noftsmotansit stilodstom ribirb. The larger the Ka the higher the affinity between P and Lc. The larger the Ka the higher the affinity between P and Lbno.6d. K₂ is equal to Kd is a direnoisbyils Muldezizylo byHGiven the O₂ binding curve to Mb in muscle (right) we can say:holtashamoa. Most of the O₂ binding sites are empty in resting muscleb. Mb acts primarily as an O₂ transporter.c. The lower pO₂ in active muscle leads to release of 0₂from Mbd. Most O₂ binding sites are empty in active muscle.0.90 of ba3 3 3 3 3 3 3O, is releas

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Human Physiology: From Cells to Systems (MindTap Course List)

9th Edition

ISBN:9781285866932

Author:Lauralee Sherwood

Publisher:Lauralee Sherwood

Chapter11: The Blood

Section: Chapter Questions

Problem 1SQE

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a) How much more O2 can be transported by the blood when erythrocytesleave the lungs? Consider that a normal adult has a concentration of 15 g hemoglobin/100 mL of bloodand that the hemoglobin is 98% saturated with O2 at the usual pO2 of 100 torr in the lung at sea level. b) On the basis of the graph, explain how myoglobin facilitates the diffusion of O2 through muscle cells. Would myoglobin be effective as an O2-transport protein in cells of other tissues? Explain.
Heart and muscle cells, where myoglobin resides, maintains an intracellular pO2 of about 2.5 torr. Calculate the fractional saturation (for human myoglobin) if a small change (1 torr) in oxygen partial pressure occurs in either direction (ie what happens at 1.5 torr, what happens at 3.5 torr?) and explain how a small change in oxygen pressure dramatically changes the myoglobin oxygen binding.
A new oxygen transport protein that exhibits cooperative binding has been isolated and is beingstudied in the lab. Calculate the KD value if Y = 0.76 when pO2 = 18 torr (assume n = 2.5). Howdoes this compare to the KD value for hemoglobin? Does this protein bind more or less tightly tooxygen compared to hemoglobin?
Myoglobin ... A. has higher affinity for O2 than hemoglobin does. B. consists of four polypeptide chains, just as hemoglobin does. C. has a lower affinity for O2 than hemoglobin does. D. is found in the interstitial fluids, in contrast to hemoglobin that is found in red blood cells. E. can bind four O2 molecules at once.
Which of the following is true about the T (tense) -->R (relaxed) transition of hemoglobin? A. The T state of hemoglobin binds oxygen with a higher affinity than the R state. B. The binding of O2 to a subunit T state can cause the transition of other subunits to the R state. C. The T state has a narrower pocket between b subunits than does the R state. D. When hemoglobin undergoes the T--> R transition, the structures of the individual subunits change dramatically.
Which of the following statements is false concerning the structure of hemoglobin? a. The binding of BPG stabilizes the T-state of Hb b. The R-state of Hb is favored under environments of high concentrations of O2 c. Hemoglobin's affinity for oxygen increases as protons ionize from the N-terminal tails d. Hemoglobin is stabilized in the low affinity state in the presence of high concentration of protons e. Hemoglobin favors the R-state in basic environments
The dissociation constant is defined by p50 = 2.8 torr for myoglobin binding to oxygen. What is partial pressure of oxygen when half of the myoglobin proteins in solution are bound to oxygen?
Myoglobin’s oxygen-binding curve exhibits a shape best described as— serpentine. hyperbolic. straight. sigmoidal. bell.
In addition to O2 binding, changes in other chemical conditions can result in changes in hemoglobin structure and function. Increases in blood H+ result in oxygen binding curves for hemoglobin that are shifted to the right. The effect of H+ can be understood in terms of the equilibrium:H-Hb+ + O2 → Hb-O2 + H+How does the difference in pH in the lungs and tissues help hemoglobin do its job of delivering oxygen? Use the equilibrium equation in your argument.
I now know the structure difference between myoglobin and hemoglobin , however which exctaly structure difference make myglobin become a oxygen storage ? and not a oxygen transport?? Be specific! details describe how the structure connect to their role. also which exctaly structure difference make hemoglobin become better oxygen transport?? I need the specific structure that contribute to their unique role. I KNOW THE STRUCTURE DIFFERENCE , but don't understand which specific part make myoglobin only bind to oxygen, and not release oxygen
One molecule of 2,3-BPG binds to one tetramer of hemoglobin in a central cavity of the hemoglobin molecule. Is the interaction between BPG and hemoglobin stronger or weaker than it would be if BPG bound to the surface of the protein instead? Explain your answer (hint: think about how these different situations affect the dielectric constant).
Calculate the percent oxygen saturation of myoglobin if 7 of 15 binding sites are occupied..

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