11. Which of the following best describes what happens when hemoglobin bindsbisphosphoglyceric acid (BPG)?A. Binding of BPG leads to tighter binding of oxygen.B. Binding of BPG allows maternal (adult) Hb to bind oxygen more tightly than fetal Hb.C. Binding of BPG is important to the allosteric nature of hemoglobinD. Binding of BPG causes the subunits of hemoglobin to separate.

Hemoglobin is a globular protein, ie it is roughly spherical. It is a tetramer of two types of…

Answered: 11. Which of the following best…

Biology: The Dynamic Science (MindTap Course List)

4th Edition

ISBN:9781305389892

Author:Peter J. Russell, Paul E. Hertz, Beverly McMillan

Publisher:Peter J. Russell, Paul E. Hertz, Beverly McMillan

Chapter44: The Circulatory System

Section: Chapter Questions

Problem 12TYK

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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
3. When muscles are more active physiological conditions change to affect oxygen binding to Hemoglobin. Briefly describe the changes that occur and why this affects hemoglobin function. Draw the shifted curve on the graph above. A. What physiological conditions change during exercise (levels of what molecules are increasing/decreasing)? B. How do these molecules directly affect Hb’s structure ? What interactions does this stabilize ? C. How do these interactions affect the affinity of Hb for O2? How would this affect the binding curve for Hb? Draw on the graph provided. D. How will this shift in the binding curve affect the function of Hemoglobin ? E.Where does the physiological pO2 in the tissues fall on the O2 binding curve ? In the lungs ? Why is this physiologically important?
2.HbF is the predominant hemoglobin of embrions.It has two γ-and two α-subunits(α2γ2).HbF does not bind 2,3-BPG well.What is the affinity of oxygen binding for HbF in compare with HbA?For answer: 1）Explain the function of HbA and the role of 2,3-BPG in the regulation of O2 binding. 2）Draw the oxygen-binding curves of HbA and HbF. 3）Mark the Biology significance of the difference in O2 affinity for HbA and HbF.
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.
The O2-binding curve for Hemoglobin (Hb) is sigmoidal because: a O2 binding to Hb increases the binding affinity of Hb for additional O2. b The pH of blood is near the pKa of histidine. c The pH of the bloodstream changes with changes in O2 concentration. d Hb’s O2-binding affinity changes with changes in pH.
7. Draw a diagram of the heme complexes in deoxyhemoglobin and oxyhemoglobin (complete porphyrin structures are not required, but show all iron coordination positions).
People suffering with sickle cell anemia have a structural defect in hemoglobin (HB). The major reason for this structural change is mutation of glutamic acid to valine. This leads to a Exposure of polar amino acids, leading to disintegration of hemoglobin. b Burying of polar amino acids, leading to disintegration of hemoglobin. c Exposure of non-polar amino acids leading to long fiber formation. d Burying of non-polar amino acids thereby increasing hydrophobic interactions and formation of long fibres.
Why is the decreased affinity of fetal hemoglobin for BPG advantageous? With fewer BPG molecules bound to heme, there are more heme residues available for O2 binding. O A. 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. BPG is more available to bind to fetal myoglobin. helping to release O2 in fetal muscle tissue. D. 47
A The following plots show an oxygen binding curve for hemoglobin under a certain set of conditions. For each plot, sketch (with reasonable accuracy) a second curve showing how the binding oxygen to hemoglobin would be altered by the change in conditions noted. 2. a. Increase in pCO2 b. Dissociation of native Hb into aß dimers 1 0.8 0.8 0.6 Y 0.4 0.6 Y 0.4 0.2 0.2 poz pO2
3A.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
In mammals, the developing fetus obtains O₂ from its mother's blood via the placenta. For this to occur... A. The fetal hemoglobin must have a higher Pso than the maternal hemoglobin B. The O₂ equilibrium curve of the fetal hemoglobin must be left-shifted with respect to the curve for the maternal hemoglobin C. The maternal hemoglobin must have a higher O₂ binding affinity than the fetal hemoglobin D. The O₂ carrying capacity of the fetal hemoglobin must be greater than that of the maternal hemoglobin E. None of the above

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