18. Sketch curves of Y vs. O2 for myoglobin and hemoglobin on the same graph. In words, explain what your curves indicate about O, binding in each of these proteins and indicate how that is relevant for their particular functions in the body.
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- Which of the following statements is false concerning the structure of hemoglobin? a. The binding of BPG stabilizes the T-state of Hb b. The R-state of Hb is favored under environments of high concentrations of O2 c. Hemoglobin's affinity for oxygen increases as protons ionize from the N-terminal tails d. Hemoglobin is stabilized in the low affinity state in the presence of high concentration of protons e. Hemoglobin favors the R-state in basic environmentsThe O2-binding curve for Hemoglobin (Hb) is sigmoidal because: a O2 binding to Hb increases the binding affinity of Hb for additional O2. b The pH of blood is near the pKa of histidine. c The pH of the bloodstream changes with changes in O2 concentration. d Hb’s O2-binding affinity changes with changes in pH.The graphs below show 02-binding curves of several proteins including myoglobin (Mb) and hemoglobin (Hb). If curve 3 (-) represents the 02 binding behavior of normal hemoglobin, which curve represents an 02-binding transporter with the same p50 as normal hemoglobin? 1.0- YO, 0.5 0.0 pO,(torr) O A. 1 B. 2 O C. 4 O D. 5 E. Both "2" and "4"
- The primary and tertiary structures of hemoglobin and myoglobin are very similar and both contain the 'heme' group as an oxygen-binding prosthetic group. However this There are important functional differences between the two proteins. Hemoglobin oxygen transport protein, myoglobin functions as oxygen storage protein. Hemoglobin and consider the structural differences and oxygen binding curves between myoglobin why myoglobin is a good oxygen transport protein, while hemoglobin Explain why it cannot be a good oxygen storage protein.What is the role of 2, 3-Bisphosphoglycerate (2,3-BPG) in the function of haemoglobin as an oxygen carrier molecule? Explain the binding mechanism and effect of 2,3-BPG leading to the reduced oxygen binding affinity for haemoglobin and transitions in the T (deoxygenated) and R (oxygenated) states of haemoglobin.One molecule of 2,3-BPG binds to one tetramer of hemoglobin in a central cavity of the hemoglobin molecule. Is the interaction between BPG and hemoglobin stronger or weaker than it would be if BPG bound to the surface of the protein instead? Explain your answer (hint: think about how these different situations affect the dielectric constant).
- What qualitative effect would you expect each of the following to have onthe P50 of hemoglobin?(a) Increase in pH from 7.2 to 7.4(b) Increase in PCO2 from 20 to 40 mm Hg(c) Dissociation into monomer polypeptide chains(d) Decrease in 2,3-BPG concentration from 7 mM to 5 mM in red cells.One molecule of 2,3-BPG binds to one tetramer of hemoglobin in a central cavity of the hemoglobin molecule. Is the interaction between BPG and hemoglobin stronger or weaker than it would be if BPG bound to the surface of the protein instead? Explain your answer (hint: think about how these different situations affect the dielectric constant). (Please provide clear and sufficient explanation for the question, thank you!)To study the chemical properties of the blood hemoglobin of a vertebrate, it might seem convenient to remove the hemoglobin from the red blood cells so that hemoglobin is in simple aqueous solution. However, removing the hemoglobin from red blood cells often promptly alters its O2-binding characteristics. Explain why?
- To study the chemical properties of the blood hemoglobin of a vertebrate, it might seem convenient to remove the hemoglobin from the red blood cells so that the hemoglobin is in simple aqueous solution. However, removing the hemoglobin from red blood cells often promptly alters its O2-binding characteristics. Why?I now know the structure difference between myoglobin and hemoglobin , however which exctaly structure difference make myglobin become a oxygen storage ? and not a oxygen transport?? Be specific! details describe how the structure connect to their role. also which exctaly structure difference make hemoglobin become better oxygen transport?? I need the specific structure that contribute to their unique role. I KNOW THE STRUCTURE DIFFERENCE , but don't understand which specific part make myoglobin only bind to oxygen, and not release oxygenWhy does release of BPG in the blood system help counter the effects of high altitude induced hypoxia? O BPG binds each hemoglobin tetramer and leads to formation of a confirmation that binds 02 more strongly allowing uptake of 02 in the lungs BPG binds myoglobin and leads to formation of a confirmation that binds 02 more strongly allowing uptake of O2 in the lungs BPG binds myoglobin and leads to formation of a confirmation that binds 02 more weakly allowing release of 02 in oxygen starved tissues O BPG binds each hemoglobin tetramer and leads to formation of a confirmation that binds 02 more weakly allowing release of 02 in oxygen starved tissues