please explain 3) Consider this figure, which shows oxygen binding to hemoglobin under various conditions. 1.0...
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.
6. Which of the following amino acid residues would provide a side chain capable of increasing the hydrophobicity of a binding site? A) aspartic acid B) lysine C) isoleucine D) arginine E) serine 7. Consider a hypothetical hemoglobin with a Hill coefficient of 1 and the same pso value as normal hemoglobin. Choose the statement below that best describes the two proteins. A) There is a cooperative interaction between oxygen-binding sites in both the hypothetical and normal hemoglobins. B) The...
A. In the chart above, where the solid line represents the
binding affinity of hemoglobin for oxygen with NO drug treatment.
Which curve above (dotted or dashed) represents
the affinity of hemoglobin of oxygen after drug treatment?
Explain.
B. How does the drug effect hemoglobin’s affinity for
O2 and how would this achieve the desired patient
result?
Increases Affinity, Decreases Affinity, No Change to Affinity?
Explain.
With hospital funding going down, local hospitals are looking for any way to cut...
Which box the indicates the oxygen binding curve of
Hemoglobin?
po, in tissues pO2 in lungs B 12 16 8 pO2 (kPa)
oxygen binc ,the oxygen binding curves below for questions 3-6. The curves below represent ing to two types of hemoglobin-"normal" -which has a Kd of 27 torrs and a mutant form of hemoglobin called Beth Israel. The third curve shows oxygen binding to " strippe Beth Israel. 3. (2 pts) The y-asxis in Figure I represents? Clearly explain, in a few words, what this Cleary means. 4.(3pts) Clearly label the curves. HbBI for hemoglobin Beth Israel, HbA for normal hemoglobin,...
During aerobic activity, we depend on hemoglobin to pick up oxygen in the lungs and deliver it to tissues in a cooperative manner. Which of the traces on the graph shown accurately shows cooperative binding/release of oxygen from hemoglobin? 1.0 0.8 B 0.6 Y (fractional saturation) 0.4 0.2 0.0 0 50 200 100 150 pO2 (torr) Figure OA OB С
How does BPG, or 2,3-biphophoglycerate produce the shift in
the oxygen bunding curves shown? (BPG works to effect the binding
of oxygen to hemoglobin) Circle the correct choice.
a) BPG binds to the R state of hemoglobin tetramer.
b) BPG binds to the T state of hemoglobin tetramer.
c) BPG binds to the heme group, which blocks access to the
oxygen
d) BPG oxidizes the iron (II) in the heme group to the iron
(III), preventing oxygen from binding.
1.0...
The measured Hill coefficient for Oz binding to hemoglobin under physiologic conditions, which has four binding sites for O2, is only about 3. Why is this?
In plain language, describe what the oxygen-hemoglobin
dissociation curve shows. Under normal conditions, the curve can
shift to the right and left. A right shift can be induced by
increased temperature and lower pH among other things. Describe
what a right shift means in terms of hemoglobin’s relationship to
oxygen. In your answer, be sure you address what is actually
happening at the level of the protein (hemoglobin is a protein).
Discuss what types of molecular interactions that can cause...
Please help with all parts... I am a bit confused and the prof
is no help.
20.) A newly discovered oxygen binding protein (OBP) has been discovered. The Hill plot shown below was generated based on the oxygen binding parameters of OBP (dashed lines) and compared to hemoglobin ( solid line). 1 Yoz 1-Y02 Log Log po (a) (2 pts) Which of the two proteins has the higher oxygen affinity? (b) (2 pts) Calculate the hill coefficient for OBP. n...