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.
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- 2,3-Bisphosphoglycerate lies in a central cavity within the hemoglobin tetramer, stabilizing the T state. What would be the effect of mutations that placed the BPG-binding site on the surface of hemoglobin?The distal Histidine (His 64) in myoglobin is subjected to three different mutations, this is one of them: H64N. (Histidine to Aparagine) For the mutation, draw a theoretical binding curve and CO relative to the O2 and CO binding curves for wild-type Mb (see example below). Provide a clear rationale for the binding curve.In a molecular disease of hemoglobin, Hemoglobin Rainier, Tyr 145β is replaced by Cys, which forms a disulfide bond with another Cysresidue in the same subunit. This prevents the formation of ion pairs that normally stabilize the T state. How does hemoglobin Rainier differ from normal hemoglobin with respect to the Hillcoefficient? Explain your answers.
- Using the quarternary structure of hemoglobin shown inFigure 9-3(d), explain in structural terms how a mutation in the β subunit protein could be suppressed by amutation in the a subunit gene.Sickle cell anemia is caused by a point mutation in the β-globin chain of hemoglobin. Glutamic acid is replaced by Valine. HBB sequence in normal adult hemoglobin (Hb A): Leu-Thr-Pro-Glu-Glu-Lys-Ser HBB sequence in mutant adult hemoglobin (Hb S): Leu-Thr-Pro-Val-Glu-Lys-Ser What effect does this mutation have on the structure and function of the protein? Predict what would happen to the RBC if the glutamic acid was replaced with asparagine instead of valine.You are studying how your Lys-Val-Thr tripep de interacts with another pep de, which places an Asp in close proximity to the Lys on your pep de. How would the presence of an Asp side chain affect the pKa of the Lys side chain? Briefly explain your reasoning. (remember pKas are rela ve, pKa=log([H+][A-]/[HA])
- A binding curve for the binding of the amino acid tryptophan to the protein called TxtE is shown below. Estimate the association equilibrium constant (Ka; in units of M-1) for Trp binding to TxtE.There was a study done (Isabel, et al.) on structural analysis of SARS-CoV-2 spike protein. The researchers hypothesized that a mutation in Asp 614 to Gly 614 will result in a loss of four inter-chain destabilizing (i.e., hydrophobic-hydrophilic) contacts. I attached an image that illustrates this (C). My question is: how does this classify as a repelling effect when Asp 614 should be hydrogen bonding with Thr 859? If Asp 614 is mutated to Gly 614, then wouldn't this hydrogen bonding no longer occur? Just not too sure what this hydrophobic-hydrophilic repelling effect is referring to exactly.In oxygenated hemoglobin, pKa 5 6.6 forthe histidines at position 146 on the -chain. In deoxygenated hemoglobin, the pKa of these residues is 8.2. How can this piece ofinformation be correlated with the Bohr effect?
- The SARS-CoV-2 spike (S) protein and its sugars have been the subject of much scientific investigation. S protein, the main focus of SARS-CoV-2 vaccine development, is heavily glycosylated. In fact, it contains 22 N-linked, and at least two O-linked, glycosylation sites. Which of the following statements is most likely to describe this glycosylation process? a.) The SARS-CoV-2 spike protein is probably glycosylated in both the lysosomes and Golgi apparatus of cells in the respiratory tract of an infected subject. b.) The SARS-CoV-2 spike protein is probably glycosylated in both the endoplasmic reticulum and proteasomes of cells in the respiratory tract of an infected subject. c.) The SARS-CoV-2 spike protein is probably glycosylated in both the endoplasmic reticulum and Golgi apparatus of cells in the respiratory tract of an infected subject.Amino acids at the interaction site ( F,I and L) and its G protein partner (P, L, Y) are very conserved.If the amino acids are swapped between the protein and GPCR is binding expected to be as tight?While each G-protein subunit has a distinctly characteristic C-terminal sequence that binds certain GPCRs better than others, the GPCRs that prefer the same G-protein subunit do not share a conserved sequence motif, even in the regions that form the binding pocket for the C-terminal domain of the G-protein a subunit. Given this fact, what must be similar about the binding pockets of these GPCRs in order to achieve specificity?