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- A person was found to have very low levels of functional beta globin mRNA and therefore very low levels of the beta globin protein. What problems would this cause for assembling functional haemoglobin molecules?Sketch 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.Myoglobin ... A. has higher affinity for O2 than hemoglobin does. B. consists of four polypeptide chains, just as hemoglobin does. C. has a lower affinity for O2 than hemoglobin does. D. is found in the interstitial fluids, in contrast to hemoglobin that is found in red blood cells. E. can bind four O2 molecules at once.
- The binding affinity of hemoglobin for oxygen is... Weaker at lower pHs Stronger at lower pHs Less cooperative at lower pHs Independent of pHThe first thing that happens when O2 binds to Hemoglobin (Hb) is that: a Hb shifts to the Relaxed state. b Tension on Heme causes a hydrogen bond to break. c The pH of the bloodstream increases. d BPG binding increases.Which occurs when a hemoglobin molecule binds oxygen in the lungs? a The first O2 molecule binds more easily than the last O2 molecule. b Each heme group can reversibly bind four O2 molecules simultaneously. c Salt bridges between subunits break as the first O2 binds. d Cooperative binding of O2 causes the four subunits to dissociate e An iron atom is removed from a porphyrin group.
- A molecule of hemoglobin ________.a. is shaped like a biconcave disk packed almostentirely with ironb. contains four glycoprotein units studded withoxygenc. consists of four globin proteins, each bound to amolecule of hemed. can carry up to 120 molecules of oxygenWhy does Fe2+ not fit perfectly into the center hemoglobin's heme pocket, while Fe3+ does ift perfectly into center hemoglobin's heme pocket? A) Fe2+ has a larger effective nuclear charge than Fe3+ . B) Fe2+ is to reactive to stably fit into hemoglobin's heme pocket. C) Fe2+ had a wrinkled shirt D) Fe2+ is repelled by the heme's coordinating nitrogens E) Fe3+ is denser and has a smaller ionic radius than Fe2+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
- The 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.Which of the following is true about the T (tense) -->R (relaxed) transition of hemoglobin? A. The T state of hemoglobin binds oxygen with a higher affinity than the R state. B. The binding of O2 to a subunit T state can cause the transition of other subunits to the R state. C. The T state has a narrower pocket between b subunits than does the R state. D. When hemoglobin undergoes the T--> R transition, the structures of the individual subunits change dramatically.In addition to O2 binding, changes in other chemical conditions can result in changes in hemoglobin structure and function. Increases in blood H+ result in oxygen binding curves for hemoglobin that are shifted to the right. The effect of H+ can be understood in terms of the equilibrium:H-Hb+ + O2 → Hb-O2 + H+How does the difference in pH in the lungs and tissues help hemoglobin do its job of delivering oxygen? Use the equilibrium equation in your argument.
