Match the colour of myoglobin to the ligand bound. brown red pink 1. carbon monoxide 2. nitric oxide 3. water
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- Which of the following are true of normal adult hemoglobin? Choice 1 of 4:can bind four Fe2+ ions Choice 2 of 4:can covalently bind four O2 molecules Choice 3 of 4:can adopt 2 different conformations, with different orientations of αβ dimers Choice 4 of 4:can bind four BPG molecules to stabilize the T stateInhibin and activin are similar molecules; however they have very different physiological roles. Discuss these differences.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).
- . In the experiments of Barrick, et al. ( observed that replacement of histidine by a noncovalently bonded imidazole not only reduced cooperativity but also increased the oxy- gen affinity of the hemoglobin. Suggest an explanation. it washe doctor also mentioned a new treatment for Sickle Cell Disease to JJ called Voxelotor (Oxbryta). Voxelotor binds to the a-globin chain and alters the structure of HbS stabilizing it in the R-state (relaxed state). Q7: In the presence of Voxelotor would you expect the affinity of HbS for O2 to increase or decrease? Q8: How would you classify the mechanism of action for Voxelotor? Q9: Voxelotor's structure is shown below. What would you expect the overall charge of the molecule to be in the blood (pH = 7.4) Pyridinium pKa = 2.6 Phenol pKa = 8.3Sketch out the binding site of Hemoglobin with oxygen bound . ( You can abstract the Heme ring out i.e. not draw each chemical bond). Please label both imported HIS residues.
- Diacylglycerol activates which of the following? RTK PKA Adenylyl cyclase Ras PKCDoes myoglobin exhibit a Bohr effect? Why or why not?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 environments
- 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 oxygenAnswer the following questions about hemoglobin. The number of high affinity binding sites in the R form of hemoglobin is .The number of low affinity binding sites in the R form of hemoglobin is .The number of O2 molecules that need to bind to convert hemoglobin from the T to R form is .The number of high affinity binding sites in the T form of hemoglobin is .The number of low affinity binding sites in the T form of hemoglobin isCalculate the percent oxygen saturation of myoglobin if 7 of 15 binding sites are occupied..
