Why is this difference in the binding curves of hemoglobin and myoglobin functionally important?
Why is this difference in the binding curves of hemoglobin and myoglobin functionally important?
Homework Answers
There is difference in the binding curves of hemoglobin and myoglobin to oxygen. Myoglobin has stronger affinity to bind with oxygen than hemoglobin with oxygen. Each myoglobin molecule binds to one oxygen molecule whereas each hemoglobin binds to four oxygen moleucle. The binding of four oxygen molecule to hemoglobin is dependent with each other. The presence of more oxygen molecules favours the binding of more oxygen molecules and if there is one oxygen molecule present, it dissociates more rapidly from a highly oxygenated species. Therefore, at low oxygen concentration, hemoglobin is less oxygenated (which is the case for tissues); however at high oxygen concentrated concentration hemoglobin is highly oxygenated (which is case in lungs). So, for oxygen transportation from lungs to tissues where oxygen concentration is more in lungs and less in tissues this difference is functionally important.
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Why is this difference in the binding curves of hemoglobin and
myoglobin functionally important?
Binding of oxygen to both myoglobin and hemoglobin in causes a conformational change in which a...
Binding of oxygen to both myoglobin and hemoglobin in causes a conformational change in which a proximal histidine is moved toward the plane of the heme ring. In hemoglobin, this results in a sigmoidal O2 binding whereas myoglobin exhibits hyperbolic O2 binding. Explain this difference.
The following results represent the oxygen binding activity of purified myoglobin, purified hemoglobin, and hemoglobin in...
The following results represent the oxygen binding activity of purified myoglobin, purified hemoglobin, and hemoglobin in human blood cells. pO2 (Torr) Fraction of purified myoglobin with O2 pO2 (Torr) Fraction of purified hemoglobin with O2 pO2 (Torr) Fraction of hemoglobin in red blood cells with O2 0.5 0.161 0.1 .00315 10.6 0.10 1.0 0.277 0.35 .0099 19.5 0.30 2.0 0.434 0.794 .0306 27.4 0.50 3.0 0.535 1.748 .0909 37.5 0.70 4.0 0.605 2.884 .24 50.4 0.85 6.0 0.697 4.467 .50...
5. Based on the binding curves of different versions of myoglobin shown below: -Myoglobin type 1...
5. Based on the binding curves of different versions of myoglobin shown below: -Myoglobin type 1 -Myoglobin type 2 20 30 40 70 80 10g 50 60 PO, (torr) a. What are the pSos for the curves? (3 pts) b. Which type of Myoglobin binds oxygen better? Explain. (4 pts)
(8) Shown in the graph below is the O2 affinity of hemoglobin and myoglobin. Explain why...
(8) Shown in the graph below is the O2 affinity of hemoglobin and myoglobin. Explain why there is a difference in the O2 affinities for these proteins and the significance of this for the function of these proteins. Myoglobin Hemoglobin Oxygen PresS ure Percent Saturation
Please write legible and simplified. Myoglobin is not cooperative and hemoglobin is. Why? Why does hemoglobin...
Please write legible and simplified.
Myoglobin is not cooperative and hemoglobin is. Why? Why does hemoglobin being a multimeric protein (specficlly tetramer for hemoglobin) make it cooperative?
What does hemoglobin have that myoglobin does not which makes positive cooperatively in binding oxygen possible?
What does hemoglobin have that myoglobin does not which makes positive cooperatively in binding oxygen possible?
Describe how the change in conformation of hemoglobin caused by allosteric binding is important in hemoglobin...
Describe how the change in conformation of hemoglobin caused by allosteric binding is important in hemoglobin function. Depict the effect of allosteric binding using a graph.
1. How can hemoglobin deliver oxygen to myoglobin in muscle tissue cells? (use oxygen binding curve,...
1. How can hemoglobin deliver oxygen to myoglobin in muscle tissue cells? (use oxygen binding curve, T-state and R-state, sigmoidal, cooperativity, Bohr effect, carbon dioxide, and 2,3-BPG)
QUESTION 9 Which amino acid stabilizes ligand binding in the binding pocket of hemoglobin and myoglobin...
QUESTION 9 Which amino acid stabilizes ligand binding in the binding pocket of hemoglobin and myoglobin via hydrogen bonding with the ligand? Distal Histidine Proximal Histidine Distal Valine Proximal phenylalanine QUESTION 10 Which of the following statement(s) is/are TRUE regarding enzymatic catalysis? Enzymes catalyze chemical transformations by altering the chemical equilibrium of the reactants and products. Enzymes catalyze chemical transformations by decreasing the free energy of the reactants. Enzymes catalyze chemical transformations by decreasing the free energy of the transition...
Iron is an important element that is necessary for the production of hemoglobin, myoglobin, and c...
Iron is an important element that is necessary for the production of hemoglobin, myoglobin, and cytochromes. The pathways by which dietary iron is distributed in the blood plasma is complicated. For this reason, the response of the body to an iron input was mapped out in mice using bolus injections of an iron tracer (56FE). This mapping yielded the following information: There are system zeros at -3 and 3 +2j There are system poles at 2j and a double pole...
5. Based on the binding curves of different versions of myoglobin shown below: -Myoglobin type 1 -Myoglobin type 2 20 30 40 70 80 10g 50 60 PO, (torr) a. What are the pSos for the curves? (3 pts) b. Which type of Myoglobin binds oxygen better? Explain. (4 pts)
(8) Shown in the graph below is the O2 affinity of hemoglobin and myoglobin. Explain why there is a difference in the O2 affinities for these proteins and the significance of this for the function of these proteins. Myoglobin Hemoglobin Oxygen PresS ure Percent Saturation
Please write legible and simplified.
Myoglobin is not cooperative and hemoglobin is. Why? Why does hemoglobin being a multimeric protein (specficlly tetramer for hemoglobin) make it cooperative?
QUESTION 9 Which amino acid stabilizes ligand binding in the binding pocket of hemoglobin and myoglobin via hydrogen bonding with the ligand? Distal Histidine Proximal Histidine Distal Valine Proximal phenylalanine QUESTION 10 Which of the following statement(s) is/are TRUE regarding enzymatic catalysis? Enzymes catalyze chemical transformations by altering the chemical equilibrium of the reactants and products. Enzymes catalyze chemical transformations by decreasing the free energy of the reactants. Enzymes catalyze chemical transformations by decreasing the free energy of the transition...
Iron is an important element that is necessary for the production of hemoglobin, myoglobin, and cytochromes. The pathways by which dietary iron is distributed in the blood plasma is complicated. For this reason, the response of the body to an iron input was mapped out in mice using bolus injections of an iron tracer (56FE). This mapping yielded the following information: There are system zeros at -3 and 3 +2j There are system poles at 2j and a double pole...
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