(b) The hemoglobin subunits expressed in a growing fetus and adult mother are different from each other. Thefetal y variant of the adult ß subunit substitutes a Ser for one of the His residues that interacts with BPG in thecentral cavity between the ß subunits, reducing affinity for BPG.(i) Draw in oxygen binding curves below for the wild-type adult hemoglobin and the fetal hemoglobincontaining the y variant. Make sure to label each curve.Fractional occupancy (f)1.0₁0.5-tissuesT50po₂ (torr)2lungs100(ii) Given how the mutation influences BPG binding, why do you think its advantageous for the fetus tocarry this amino acid substitution? Provide a mechanistic explanation for your answer. The image below depicts 2,3-bisphosphoglyceratedepicted in dark gray, and ß subunits are depicted in light gray.(BPG) bound to hemoglobin. The a subunits areBPG

Hemoglobin is a globular protein, ie it is roughly spherical. It is a tetramer of two types of…

Answered: (b) The hemoglobin subunits expressed…

Biochemistry

9th Edition

ISBN:9781319114671

Author:Lubert Stryer, Jeremy M. Berg, John L. Tymoczko, Gregory J. Gatto Jr.

Publisher:Lubert Stryer, Jeremy M. Berg, John L. Tymoczko, Gregory J. Gatto Jr.

Chapter1: Biochemistry: An Evolving Science

Section: Chapter Questions

Problem 1P

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Based on the following data, is the p50 higher or lower than normal in (a) hemoglobin Yakima and (b) hemoglobin Kansas? Explain. Name Yakima Kansas Mutation Asp G1 (99) ẞ → His Asn G4 (102) ß → Thr Effect Disrupts a hydrogen bond that stabilizes the T conformation Disrupts a hydrogen bond that stabilizes the R conformation
5. (a) Hexokinase IV is known as glucokinase (GCK) and is a central metabolic enzyme that participates in glucose homeostatic maintenance by governing the rates of glucose catabolism in pan- creatic B-cells and glycogen storage in hepatocytes (liver cells). In contrast to the regulatory mecha- nisms of hexokinase I or Il in other tissues, GCk is regulated by binding to the Glucokinase Regulatory Protein (GRP) located in the cell nucleus. When glucose in hepatocytes is low, GCK is sequestered in the nucleus by binding to the GRP. High glucose, for instance, after ingestion of a meal, disrupts the GRP-GCK complex, allowing the GCK to diffuse into the cytoplasm to convert glucose into glucose-6- phosphate. Contrast the properties of hexokinases I and IV with respect to oligomeric structure, mech- anism of regulation of their activity, KM value, and dependence of catalytic activity on cellular location. Hexokinase l is found in, for instance, muscle tissue. Property subunit structutre…
. What physiological effect would you predict from a mutation that replaced with serine the cysteine in the constant part of the immunoglobulin light chain that is involved in disulfide-bond for- mation with the heavy chain? ,
Of all the genes in the human genome, the ones withthe most characterized Alu insertions are those thatcause hemophilia, including several insertions in thefactor VIII and factor IX genes. Based on this fact, yourcolleague hypothesizes that the Alu element prefers toinsert into these genes. Do you agree? What other reason can you provide that also explains these data?
The activity provides you with a version of the NGF pathway, an example of a RTK. All of the proteins involved can be in ON/OFF states. Using this cell signaling pathway you will be asked a variety of questions to determine how the molecules are regulated, but also how a cell would respond if this cell signaling party steps were interrupted or activated. Neural Growth Factir (NGF) Ras- Ras- GDP GTP Trk-A Ras-GEF braf braf МЕК МЕК ERK ERK ERK ERK STAT STAT Spiouty DNA Nucleus Cytosol
The hemoglobin in the fetus (HbF) is a structural variant of the hemoglobin in the mother (HbA). HbA is a tetrameric protein complex consisting of two α-globin and two β-globin subunits. HbF is made up of two αglobin and two γ-globin subunits, where the γ-globins are similar to the β-globins but γglobins have lower affinity for 2,3- bisphosphoglycerate or BPG. Studies of oxygen transport in pregnant mammals show that the oxygen-saturation curves between the red blood cells of the fetus and the mother are markedly different. 1. The shape of hemoglobin binding curves is: hyperbolic or sigmoidal 2. a) Based on the binding curves, determine the dissociation constant (Kd) for each hemoglobin complex. (Show correct units.) Kd of HbF + BPG: ________________ Kd of HbA + BPG: _____________________ b) Which has a higher affinity for oxygen? HbF+BPG HbA+BPG 3. a) How many BPG molecule(s) is/are expected to bind one hemoglobin complex? 1 2 3 4 b) BPG binding preferentially stabilizes which state…
1) The plot to the right shows the Oxygen Saturation of Hemoglobin (Hb) versus O2 concentration. a) The Kd between HBa and HBB chains is 100 nM. When L35S mutation (Leucine 35 → Serine) is introduced into the Hba chain the Kd changes to 300 mm. \^^^^^A^A Draw a dashed curve on the figure to the right that represents how this mutation would likely change the curve. Note: that I am asking for how a change in affinity between HBa and HBB chains will impact HB binding to O2 1.00 0.75- HB Y 0.50 HBa L35S HBa L35S D101P 0.25 0.00 0 2 4 po₂ (kPa) 6 b) How might this specific mutation alter the interaction between HBa and HBB chains? I am asking you to predict what Leu specifically might be doing here. 8 c) Now imagine that a second mutation is added to the HB¤ L35S mutant to generate an HBa L35S D101P double mutant. A measure of the double mutant shows that it has a Kg = 2 kPa, but does not change the binding of HBa and HBB. Draw a dotted line on the figure above that shows the resulting…
Mutations in the ribosomal protein gene RPS19 have been found to be associated with Diamond-Blackfan anemia (DBA), a rare syndrome that disrupts erythropoiesis, the process by which new red blood cells are produced. Which of the following provides the most likely explanation for the connection between a mutation in RPS19 and a disruption in erythropoiesis? A B с D The ribosomes in the cell are unable to package and transfer the components that are required for erythropoiesis. The ribosomes in the cell are unable to facilitate the movement of nutrients that are re- quired for erythropoiesis across the cell membrane. The ribosomes in the cell are unable to correctly synthesize the proteins that are re- sponsible for erythropoiesis. The ribosomes in the cell are unable to effectively produce the ATP that is required for erythropoiesis.
Normal Hgb is referred to as HbA and contains 4 subunits, 2 a-globin chains and 2 B-globin chains, arranged as two dimers of aß. In Sickle Cell Disease, both B-globin chains are altered in the dimers (aßS/aßS). Q3: Which level of structure does the aß/aß and aßS/aßS in HbA and HbS describe?
The mutation in hemoglobin at B82 Lys → Asp results in lowered O,-binding affinity compared to normal hemoglobin. B82 is one of the residues that lines the 2,3-BPG binding site (see Figure 7.29; B82 is adjacent to His143). Based on the location of this residue and the differences between Lys and Asp, sug- gest a rationale for the observed reduction in Oz-binding affinity.
How can a single nucleotide insertion in the beta globin gene generate a phenotypic change in the ability of the red blood cell to transport oxygen?
4)

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