Describe the two-state allosteric model for O2 binding to hemoglobin (Hb).
Nearly all oxygen in animals is transported by haemoglobin(Hb) and Hb binds with 4 oxygen molecules one after the other.Binding of one oxygen molecule with a haem group facilitate binding of other oxygen molecule with another haem group on same protein and this binding behaviour is called cooperativity
Two state allosteric model for oxygen binding to Hb includes:
T state is dominant conformation of deoxy Hb and stabilized by ionic interactions whereas oxygen binding stabilizes R state
The binding of oxygen to a Hb subunit in the T state triggers change in the conformation to the R state
Describe the two-state allosteric model for O2 binding to hemoglobin (Hb).
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.
In the mutant hemoglobin known as HB Providence, an asparagine residue in the B-chain replaces Lys-82. In the normal hemoglobin, Lys-82 projects in the cental cavity of the hemoglobin molecule. Predict the effect of the Lys-Asn mutation of the affinity of allosteric modifiers (relative to normal Hb e.g HbA) and describe the effect the mutation would have on the function (oxygen binding) og HB Providence.
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?
3. (20 pts) Given the basic sigmoid oxygen binding curve for hemoglobin, (a) Write out the overall AGⓇ for the binding of the first O2 to hemoglobin in terms of component free energy contributions. H6+0₂ - H602 PG, Роа (b) Expand your equation to include the contribution of the allosteric effector, 2,3-DPG to the standard state free energy change. (c) Write out the chemical equations and the related free energy changes for binding the first oxygen to hemoglobin in the...
Draw the hyperbolic curve of Mb-O2 binding, the hyperbolic curve of Hb-O2 binding without 2,3 BPG and the sigmoidal curve of Hb-O2 binding with 2,3 BPG. Understand how the curve explains the affinity difference and Hb cooperative binding.
3. Hemoglobin (Hb) is similar to Mb in that it binds O2. However, there are some distinct differences. Complete the table below to illustrate some of these differences. Hb Mb Function in mammals Highest level of structure (1º, 2º, etc.) Shape of binding curve (vs Poz) (sketch the curve in the box, label the axes, and write the name of the type of curve it is) Type of Curve: Type of Curve: Where it is found in mammals 4. Let's...
For the following questions consider this equation for hemoglobin – oxygen equilibrium. Hb + 4O2⥤ Hb(O2)4 Carbon Monoxide (CO) bonds to hemoglobin approximately 230 times stronger than oxygen. How would you increase the bonding oxygen to a patient with carbon monoxide poisoning?
Dietary iron forms a 1:1 complex with hemoglobin (Hb), which is responsible for O2 transport in the body based on the following equation: Hb+4O2→Hb(O2)4 How many moles of oxygen could be transported by the hemoglobin complex formed from 6 mg of dietary iron? [ Anemia-A Limiting Reagent Problem? p. 172] Express your answer to two significant figures and include the appropriate units.
2. What the mechanisms of affecting Hb (hemoglobin) affinity to O2 -- by O2, CO2, CO, H+? Please explain in detail.
biochemistry Question 2.(12 pts) O2 binding to Fe? 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. Page 4/7 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? Question 3.(9 pts) You need to make up a 600 ml of a 40 mM solution...