Be able to describe the hemoglobin binding curve and why it is S shaped. Why is the shape important for loading and off-loading Oxygen? What is subunit cooperativity?
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Be able to describe the hemoglobin binding curve and why it is S shaped. Why is the
shape important for loading and off-loading Oxygen? What is subunit cooperativity?
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- In a molecular disease of hemoglobin, Hemoglobin Rainier, Tyr 145β is replaced by Cys, which forms a disulfide bond with another Cysresidue in the same subunit. This prevents the formation of ion pairs that normally stabilize the T state. How does hemoglobin Rainier differ from normal hemoglobin with respect to (A)oxygen affinity, (B)the Bohr effect, and (C)the Hillcoefficient? Explain your answers.(No more than one page). Explain why quaternary structure is necessary for cooperativity and allosteric regulation. Use hemoglobin as an example. Include the various allosteric effectors that influence oxygen binding.Comparison of Fetal and Maternal Hemoglobins.Studies of oxygen transport in pregnant mammals show that the O2-saturation curves of fetal and maternal blood are markedly different when measured under the same conditions. Fetal erythrocytes contain a structural variant of hemoglobin, HbF, consisting oftwo a and two g subunits (α2γ2), whereas maternal erythrocytes contain HbA (α2β2). a)Which hemoglobin has a higher affinity for oxygen under physiological conditions, HbA or HbF? Explain. b)What is the physiological significance of the different O2 affinities? c)When all the BPG is carefully removed from samples of HbA and HbF, the measured O2-saturation curves (and consequently the O2affinities) are displaced to the left. However, HbA now has a greater affinity for oxygen than does HbF. When BPG is reintroduced, the O2-saturation curves return to normal, as shown in the graph. What is the effect of BPG on the O2affinity of hemoglobin? How can the above information be used…
- A variant of hemoglobin (Boston variant; mutation His E7(58)α → Tyr) promotes methemoglobin formation involving the α (alpha) subunits. What is the maximum value of the Hill constant (n) that you could measure for the Boston variant of hemoglobin? log (YO2 / 1 - YO2 ) = log pO2 - logP50 Please break down each step of the Hill equation and explain why the result for n is valid from a logical standpoint.A team of biochemists uses genetic engineering to modify the interface region between hemoglobin subunits. The resulting hemoglobin variants exist in solution primarily as αβ dimers (few, if any, α2β2 tetramers form). Are these variants likely to bind oxygen more weakly or more tightly? Explain your answer.Why does the dissociation constant change for hemoglobin in high and low 02 concentrations? O Hemoglobin is a tetramer and subunits have decreased dissociation of 02 when a neighboring subunit has bound 02 O Hemoglobin is a monomeric protein with increased dissociation of 02 when a neighboring molecule has bound 02 O Hemoglobin is a tetramer and subunits have increased dissociation of 02 when a neighboring subunit has bound CO O Hemoglobin is a tetramer and subunits have increased dissociation of O2 when a neighboring subunit has bound O2
- Please fill in the following blanks with the options that correctly finishes the sentence. a. At a low O₂ pressure the [Select] hemoglobin is in a [Select] [Select] [Select] 9 [Select] " bond with [Select] heme, and the protein's central channel is [Select] b. The proximal histidine forms a(n) [Select] state is stabilized. In this conformation state, the heme prosthetic groups is each subunit's heme is more likely to be the proximal histidine is [Select ] bond with while the distal histidine forms a(n) [Select] to theMyoglobin stores O2 in muscle tissue to be used by the mitochondria only when the cell is in oxygen debt, whereas hemoglobin can effectively transport O2 from the lungs and deliver it discriminately to cells in need of O2. Describe the structural features that allow these two proteins to accomplish separate functions.The primary and tertiary structures of hemoglobin and myoglobin are very similar and both contain the 'heme' group as an oxygen-binding prosthetic group. However this There are important functional differences between the two proteins. Hemoglobin oxygen transport protein, myoglobin functions as oxygen storage protein. Hemoglobin and consider the structural differences and oxygen binding curves between myoglobin why myoglobin is a good oxygen transport protein, while hemoglobin Explain why it cannot be a good oxygen storage protein.
- List 4 different actiated carrier molecules, for each one, list both the oxided and reduced formsIn a molecular disease of hemoglobin, Hemoglobin Rainier, Tyr 145β is replaced by Cys, which forms a disulfide bond with another Cysresidue in the same subunit. This prevents the formation of ion pairs that normally stabilize the T state. How does hemoglobin Rainier differ from normal hemoglobin with respect to the Hill coefficientThe T state of hemoglobin is converted to the R state by what event? Select one: The binding of oxygen destabilizes a more planar heme ring which alters the position of the proximal histidine and subsequently, residues between the alß2 interface. а. b. None of these. The binding of oxygen stabilizes a more planar heme ring which alters the position of the proximal proline and subsequently, residues between the alß2 interface. С. d. The binding of oxygen stabilizes a more planar heme ring which alters the position of the proximal histidine and subsequently, residues between the alß2 interface. The binding of oxygen destabilizes a more planar heme ring which alters the position of the proximal proline and subsequently, residues between the alß2 interface. е.