Is the side chain pictured responsible for causing carbon monoxide to bind less effectively to hemoglobin?
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With the use of site-directed mutagenesis, hemoglobin has been prepared in which the proximal histidine residues in both the $\alpha$ and the $\beta$ subunits have been replaced by glycine. The imidazole ring from the histidine residue can be replaced by adding free imidazole in solution. Would you expect this modified hemoglobin to show cooperativity in oxygen binding? Why or why not? (FIGURE CANT COPY)
Hemoglobin releases protons upon oxygen binding. This phenomenon is called the Bohr effect, and an important group that participates is histidine 146 of the β subunit. In deoxyhemoglobin histidine 146 forms a salt bridge with aspartic acid 94. The salt bridge is disrupted upon oxygenation: deoxyhemoglobin oxyhemoglobin his146 asp94 asp94 his146 The pKa of the histidine side group in the deoxy form is higher than that in the free amino acid, but changes upon oxygenation of the heme Fe(II) atom. How does the pKa change (i.e., does it increase or decrease)? Why does this change occur?
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- transfer proteins to membrane from gel - treat w/ antibody that binds a protein (1° antibody) - treat w/ antibody that binds the 1st antibody (2° antibody) - the 2° antibody "glows" in some way - detect if protein (or protein variant) is present in a sample of other proteins in a given sample 6) (4 points) In the mutant hemoglobin Hb Ohio, alanine-142 of the β chain is mutated to asp, resulting in the displacement of the G helix relative to the F helix. This decreases the stability of the β146His-β94Asp ion pair. Draw the oxygen-binding curves that compare the Hb A (normal hemoglobin) to Hb Ohio. What is the effect of the decreased stability of the His-Asp ion pair on Hb Ohio?
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