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.
hemoglobin has four subunits, each of which can bind oxygen. This does not indicates the cooperative binding of oxygen to hemoglobin.
T to R state conversion is a indication because it states that O2 will bind easily.
hill coefficient is more than 1, its the indication of cooperative binding.
plot definately show because it show mid highest increase inO2 saturation
Which of the following is NOT an indication that the binding of oxygen to hemoglobin is...
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
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.
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...
Strong-binding YO Transition from weak- to strong-binding Weak-binding 20 40 60 80 Po, (mm Hg) 100 120 Analyze the binding curve by completing the following sentences. Match the words in the left column to the appropriate blanks in the sentences on the right. View Available Hints) Reset Help decrease Of the two axes in the oxygen binding curve, the y-axis shows the increase where the percentage of bound and unbound oxygen binding sites can be determined. An axis value of...
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...
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...
please explain 3) Consider this figure, which shows oxygen binding to hemoglobin under various conditions. 1.0 B 0.5 po2 a) If B is normal hemoglobin what could lead to curve hemoglobin A. (2 pt) b) If B is normal hemoglobin what could lead to curve hemoglobin C. (2 pt) c) Which curve shows the hemog Iobin with the highest O2 affinity? (2 pt) d) Which curve shows the hemoglobin with the lowest Pso? (2 pt) (Saturation
Answer all questions clearly and correctly Find an oxygen binding curve for myoglobin in your textbook. How would you describe the shape of this 2. curve? 3. Explore the structure of hemoglobin using Proteopedia, Go to the Proteopedia site (http://www.proteopedia org/wiki/index.php/Main_Page) and search for hemoglobin. On the hemoglobin page, explore the structures and answer the tollowing questions. Note that you can rotate the hemoglobin molecule using your mouse and that clicking on green links changes the image of the structure....
41. Which of the following statements about protein-ligand binding is correct? A) The K is equal to the concentration of ligand when all of the binding sites are occupied. B) The K is independent of such conditions as salt concentration and pH. C) The larger the K. (association constant), the weaker the affinity. D) The larger the K. the faster is the binding. E) The larger the K, the smaller the K. (dissociation constant) 42. The ability of O, to...
For the video response portion of this assignment, your job will be to state what would happen to the oxygen bond to Hemoglobin if the pH of the tissue was the same as that of the lungs using the logic of the person’s presentation you watched. Discuss whether or not you agree with this. The video said this: Oxygen must be transported in the blood from the lungs, because the partial pressure of oxygen (pO2) is relatively high (approximately 100...