Below is a list of hypothetical Hemoglobinvariants. Circle the name of the variant that ismost likely to show an increase in BPG binding.Does such a hypothetical variant cause anincrease or decrease in hemoglobin's affinity foroxygen?A. Hb Miami: Leu is substituted with Pro in analpha helixB. Hb California: Val is substituted with Lys at pH7.0C. Hb New york: Tyr is substituted with Met,which disrupts the hydrogenbonding at the a131 interface.D All of the above

Hemoglobin exists in the T and R state during the absence and presence of oxygen respectively. In…

Answered: Below is a list of hypothetical…

Human Physiology: From Cells to Systems (MindTap Course List)

9th Edition

ISBN:9781285866932

Author:Lauralee Sherwood

Publisher:Lauralee Sherwood

Chapter11: The Blood

Section: Chapter Questions

Problem 3SQE

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People suffering with sickle cell anemia have a structural defect in hemoglobin (HB). The major reason for this structural change is mutation of glutamic acid to valine. This leads to a Exposure of polar amino acids, leading to disintegration of hemoglobin. b Burying of polar amino acids, leading to disintegration of hemoglobin. c Exposure of non-polar amino acids leading to long fiber formation. d Burying of non-polar amino acids thereby increasing hydrophobic interactions and formation of long fibres.
Will a mutation from Distal histidine to phenylalanine shift the binding curve of hemoglobin?Will it shift the curve to the left or right, shift to myoglobin or no longer bind to O2?
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
What is the molecular basis for the difference in the electrophoretic pattern between normal hemoglobin A and hemoglobin S?
a) How does the fetal hemoglobin differ from the maternal hemoglobin in regards to structure and function? b) Explain the Bohr effect by drawing oxygen dissociation curves on a single graph that highlight changes in the hemoglobin affinity for O2 c) Describe the molecular basis of sickle cell anemia. Be specific
Suppose a hypothetical "molecule X" binds to hemoglobin (at a different site than the O2 binding site) and stabilizes the T state. How would you identify this effector? a. Positive homotropic effector b. Negative homotropic effector c. Positive heterotropic effector d. Negative heterotropic effector
1. a) True or False - A mutation in the beta globin gene that causes conversion of His146 to Glutamate would decrease Hemoglobin’s O2 binding affinity. b) True or False - A mutation in the beta globin gene that causes conversion of His146 to Glutamate would eliminate Hemoglobin’s positive cooperativity.
The sigmoidal, cooperative binding curve commonly observed for hemoglobin is a result of: a) competition between CO2 and O2 for heme binding. B) competition between heme and distal His for O2 binding c) competition between BPG and CO2 for binding at the central cavity site d) T to R transition Hemoglobin has a tendency to release its oxygen to the tissues because: a) in this region pH is high and O2 concentrations are low b) in this region both pH and O2 concentrations are low c) in this region both pH and O2 concentrations are high d) there is much BPG in this region Which statement about fetal hemoglobin is not true? A) fetal hemoglobin has gamma chains instead of beta chains b) fetal hemoglobin binds BPG less strongly than maternal hemoglobin c) fetal hemoglobin binds oxygen less strongly than maternal hemoglobin d) fetal hemoglobin binds oxygen more strongly than maternal hemoglobin Which process is most responsible for the sickling of cells seen in sickle…
Under appropriate conditions, hemoglobin dissociates into its four subunits. The isolated α subunit binds oxygen, but the O2 -saturation curve ishyperbolic rather than sigmoid. In addition, the binding of oxygen to the isolated α subunit is not affected by the presence of H+, CO2 , or BPG. What do these observations indicate about the source of the cooperativity in hemoglobin?
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.
What is the Bohr effect? What role does BPG play in hemoglobin function?
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.

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