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- The figure below shows amino acid interactions between the a /B2 subunit interface of hemoglobin. These interactions stabilize the T state of the protein. Based on the figure below, which amino acid in the picture below, if replaced with glutamate, would decrease the Ka of hemoglobin for O2 the most? Include both the residue and the residue number in your response (For example, V1 or K127). to B, V34 8- a, R141 D126 K127 Noncovalent2,3-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?Explain the signifi cance of the observation that peptides such as fMet-Leu-Phe “activate” the phagocytotic (particle-engulfi ng) functions of mammalian leukocytes (white blood cells).
- . In the protein adenylate kinase, the C-terminal region is a-helical, with the sequence Val-Asp-Asp-Val-Phe-Ser-Gin-Val-Cys-Thr-His-Leu-Asp- Thr-Leu-Lys- The hydrophobic residues in this sequence are presented in boldface type. Suggest a possible reason for the periodicity in their spacing.The figure below shows amino acid interactions between the a1/B2 subunit interface of hemoglobin. These interactions stabilize the T state of the protein. Based on the figure below, which amino acid in the picture below, if replaced with glutamate, would decrease the Kg of hemoglobin for O2 the most? Include both the residue and the residue number in your response (For example, V1 or K127). B, V34 8- a, R141 a2 D126 a, K127 Noncovalent InteractionsExplain the function(s) of Hsp90. Name two factors which lead to the increase of this protein in cells.
- provide examples of the levels of protein structure for mevalonate kinase (2HFU) provide the levels of protein structure (primary, secondary, tertiary, etc.) for mevalonate kinase (2HFU)The anticlotting property of heparin is partly the result of the negative charges it carries. ( Q.) Which type of heparin is a better anticoagulant, one with a high or a low degree of polymerization?In the protein adenylate kinase, the C-terminal region has the sequence Val-Asp-Asp-Val-Phe-Ser-Gln-Val-Cys-Thr-His- Leu-Asp-Thr-Leu-Lys- The hydrophobic residues in this sequence are presented in boldface type. Suggest a possible reason for the periodicity in their spacing.
- In the protein adenylate kinase, the C-terminal region has the sequence Val-Asp-Asp-Val-Phe-Ser-Gln-Val-Cys-Thr-His-Leu-Asp-Thr-Leu-Lys-The hydrophobic residues in this sequence are presented in boldface type.Suggest a possible reason for the periodicity in their spacing.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.Suggest probable consequences of the following real or possible hemoglobinmutations. [Note: as shown](a) At β146 (HC3) His → Asp(b) At β92 (F8) His → LeuIn each case, indicate whether a single-nucleotide change is sufficient forthe mutation.