At low pO2, Myoglobin’s O2 binding affinity is ______ that of Hb. a essentially the same as b higher than c lower than
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At low pO2, Myoglobin’s O2 binding affinity is ______ that of Hb.
| a |
essentially the same as |
|
| b |
higher than |
|
| c |
lower than |
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- 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 oxygenMyoglobin benefits muscle cells by ... A. binding with O2 just as strongly as hemoglobin does. B. releasing bound O2 at lower PO2 conditions than hemoglobin does. C. increasing the effectiveness of fast glycolytic muscle fibers used in short bursts. D. contributing to the elasticity of flight muscle in birds. E. using hemoglobin as a reserve source of oxygen.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.
- Hemoglobin and myoglobin both use heme as their prosthetic group and they both bind O2. However, their O2-binding curves indicate these proteins have different activities. What lind of information can be learned about the differences between the curves?Which statement is true for the heme group present myoglobin: a. Oxygen binding to heme group is influenced by serine residues within proteins’ sequences. b. Oxygen binding to heme can become irreversible as a result of interaction with certain protein residues. c. Oxygen reversibly binds to the heme prostetic group and this binding is influenced by histidine residues within the myoglobin sequence. d. The heme group dissociates from Mb after oxygen is released.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.
- Increasing concentrations of either 2,3-bisphosphoglycerate (BPG) or protons (H +) cause a ____________ ( rightward OR leftward) shift of the hemoglobin/oxygen binding curve. However, the mechanisms by which these two substances mediate this effect are distinct. Compare & contrast the way by which BPG and protons interact with hemoglobin and thereby influence its structure and functionCalculate the percent oxygen saturation of myoglobin if 7 of 15 binding sites are occupied..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?
- A person was found to have very low levels of functional beta globin mRNA and therefore very low levels of the beta globin protein. What problems would this cause for assembling functional haemoglobin molecules?Describe the structural basis for the cooperative (allosteric) binding of O2 by hemoglobin but not by myoglobin3A.Describe the difference in biological func on of myoglobin and hemoglobin in the body. How does hemoglobin’s sigmoidal O2 binding curve contribute to its biological func on?( Think binding affinity) 3B. Describe the different ways in which the affinity of oxygen to hemoglobin can be modified in vivo
