Describe cooperativity in hemoglobin oxygen-binding activity and its structural basis.
Describe cooperativity in hemoglobin oxygen-binding activity and its structural basis.
Homework Answers
Ans : Hemoglobin's oxygen_ binding curve forms in the shape of sigmoidal curve.this is due to the cooperatively of the hemoglobin. As hemoglobin travels from the lungs to the tissues the PH value of it's surroundings decrease ,and the amount of carbon dioxide that it reacts with increases. Oxyhemoglobin is formed during physiological respiration when oxygen- binds to the heme component of the protein hemoglobin in the red blood cells.this process occurs in the pulmonary capillaries adjacent to the alveoli of the lungs.
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Describe cooperativity in hemoglobin oxygen-binding activity and
its structural basis.
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)
Biochem question 1. List positive and negative effectors for oxygen binding to hemoglobin. 2.List the structural...
Biochem question 1. List positive and negative effectors for oxygen binding to hemoglobin. 2.List the structural changes that occur when oxygen binds to the heme group in Mb, and in Hb
Describe the T and R conformaions of hemoglobin with regards to: oxygen binding affinity; change in...
Describe the T and R conformaions of hemoglobin with regards to: oxygen binding affinity; change in heme conformation upon binding to oxygen; effect that a conformational change in a single subunit has on other subunits (ex: cooperativitt)
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...
Dimoglobin as a case study in cooperativity. Note that each binding site can be occupied, ,...
Dimoglobin as a case study in cooperativity.
Note that each binding site can be occupied,
, or unoccupied,
, and that a parameter J describes the cooperativity between the O2
molecules when both states are occupied (i.e., the energy is not
just the sum of the individual binding energies).
a) Write down the weights (Gibbs factors) for each of the
different states for the dimoglobin system shown in Figure 2.
b) What is the formula that describes the energy of...
Which of the following is NOT an indication that the binding of oxygen to hemoglobin is...
Which of the following is NOT an indication that the binding of oxygen to hemoglobin is cooperative? a. Oxygen binding of one subunit induces a shift of the other hemoglobin subunits from the T state to the R state. b. A plot of hemoglobin’s fractional saturation against partial pressure of oxygen (Y versus pO2), is sigmoidal rather than hyperbolic. c.Hemoglobin has four subunits, each of which can bind oxygen. d.The Hill coefficient, n, is greater than 1.0.
O2 binding to Fe2+ in one subunit of hemoglobin changes the binding affinity of the other 3 subunits. a. Describe the ch...
O2 binding to Fe2+ in one subunit of hemoglobin changes the binding affinity of the other 3 subunits. a. Describe the change in the shape of the heme that results in O2 binding. b. How is the heme shape change communicated to the other subunits c. What is the role of Bisphosphoglycerate (BPG) in hemoglobin mediated oxygen transport?
1. Fetal erythrocytes contain a structural variant of hemoglobin, HbF, consisting of two a and two y subunits (azy),...
1. Fetal erythrocytes contain a structural variant of hemoglobin, HbF, consisting of two a and two y subunits (azy), whereas maternal erythrocytes contain HbA (022). Consider the oxygen saturation curve shown below and answer the questions that follow: a) Which hemoglobin has a higher affinity for oxygen? Explain how you made that interpretation. +BPG 0.5 -BPG b) What is the physiological significance of the different 02 affinities? 8 10 4 6 po, kPa) 2. In the context of O, binding...
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.
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.
Dimoglobin as a case study in cooperativity.
Note that each binding site can be occupied,
, or unoccupied,
, and that a parameter J describes the cooperativity between the O2
molecules when both states are occupied (i.e., the energy is not
just the sum of the individual binding energies).
a) Write down the weights (Gibbs factors) for each of the
different states for the dimoglobin system shown in Figure 2.
b) What is the formula that describes the energy of...
1. Fetal erythrocytes contain a structural variant of hemoglobin, HbF, consisting of two a and two y subunits (azy), whereas maternal erythrocytes contain HbA (022). Consider the oxygen saturation curve shown below and answer the questions that follow: a) Which hemoglobin has a higher affinity for oxygen? Explain how you made that interpretation. +BPG 0.5 -BPG b) What is the physiological significance of the different 02 affinities? 8 10 4 6 po, kPa) 2. In the context of O, binding...
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