In one type of hemoglobin variant, lysine EF6 is replaced by an aspartic acid residue.What would be the effects of this mutation on the affinity of the hemoglobin for 2,3BPG and oxygen?The affinity for 2,3-BPG would increase, and for oxygen would decrease.The affinity for 2,3-BPG would decrease, and for oxygen would decrease.The affinities for 2,3-BPG and for oxygen would be unaffected.The affinity for 2,3-BPG would increase, and for oxygen would increase.The affinity for 2,3-BPG would decrease, and for oxygen would increase.

The replacement of lysine (K) by aspartic acid (D) at position EF6 in hemoglobin affects the…

Answered: In one type of hemoglobin variant,…

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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Neurospora crassa can synthesize the amino acid arginine from a precursor as follows: precursor ornithine citrulline arginine George Beadle and Edward Tatum identified various mutants (arg mutants) unable to synthesize arginine from this precursor. One such class (Class I) could synthesize arginine if either ornithine or citrulline was supplied. A second mutant class (Class II) could synthesize arginine if citrulline was added, but not if ornithine was added. A third class (Class III) could not synthesize arginine from either ornithine or citrulline. Which class or classes of arg mutants will grow on complete media?
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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…
Can you check if A is correct and please help answer the following questions?
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?
Sickle cell hemoglobin DNA CACGTAGACTGAGG ACAC.. Sickle cell hemoglobin MRNA Sickle cell hemoglobin AA sequence 4. What type of mutation is this? Please explain why.
Hurler syndrome is due to a mutation in a gene that encodes aprotein called α-l-iduronidase. This protein functions withinlysosomes as an enzyme that breaks down mucopolysaccharides(a type of polysaccharide that has many acidic groups attached).When this enzyme is defective, excessive amounts of the mucopolysaccharides dermatan sulfate and heparin sulfate accumulatewithin the lysosomes, especially in liver cells and connectivetissue cells. This accumulation leads to symptoms such as anenlarged liver and spleen, bone abnormalities, corneal clouding,heart problems, and severe neurological problems. The pedigreebelow contains three members affected with Hurler syndrome,indicated with black symbols. Based on this pedigree, does thissyndrome appear to follow autosomal recessive, autosomaldominant, X-linked recessive, or X-linked dominant inheritance?Explain your reasoning.
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)
. The mutation in hemoglobin at B82 Lys → Asp results in lowered O2-binding affinity compared to normal hemoglobin. B82 is one of the residues that lines the 2,3-BPG binding site. A rationale for the observed reduction in O2-binding affinity is: A. The positive charge on the Asp side chain can form salt bridges with other negative charged side chains stabilizing R-conformer. B. The negative charge on the Asp side chain can form salt bridges with other positive charged side chains stabilizing the T-conformer. C. The Asp side chain mimics the positive charge on BPG. D. The Asp side chain mimics the negative charge on BPG. E. The Asp side chain is a nucleophile that attacks the BPG. F. BPG attacks the Asp side chain. G. Stabilization of the R-conformer favors O, release. H. Stabilization of the T-conformer favors O, release.
A very new Hemoglobin variant, called Hb simplex, has just been identified in patients with hypoxia (i.e. patients for whom the oxygenation of organs is not properly accomplished). However, this variant is able to bind dioxygen with a Kd which is significantly lower to that of Hemoglobin from normal patients. This effect has been associated with the substitution of a Lys by a Met at two distinct sites of the b subunit of Hemoglobin : one site close to the N-terminus, and the other site close to the C-terminus of the polypeptide chain. Most importantly, these 2 sites are known to be involved in the maintain of the physical interactions between the subunits a and b in Hemoglobin. 1) The aforementioned Hb simplex mutations lead to a loss of physical interactions between the subunits a and b. What type(s) of chemical bonds between the 2 subunits (i.e. covalent, electrostatic, ion-dipole, dipole-dipole, van der waals) would you hypothesize to be affected by these mutations? explain. 2)…

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