Compare the binding isotherm of normal hemoglobin (at pH 7.4, with 7.8 mM 2,3 BPG) with...

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Compare the binding isotherm of normal hemoglobin (at pH 7.4,with 7.8 mM 2,3 BPG) with that of the following variations. Foreach variant, clearly explain why or why not the binding isothermchanges the way it does.
Explain Please!
a) Hemoglobin at pH 6.9, 7.8 mM 2,3 BPG
b) Hemoglobin in which a glutamate residue (at a positionnormally exposed to the solvent) has been substituted for a valineresidue (at pH 7.4, with 7.8 mM 2,3 BPG)
c) Hemoglobin at pH 7.4 with 9.4 mM 2,3 BPG
d) Hemoglobin with a mutation in the beta chain position 94(position FG1) (at pH 7.4, with 7.8 mM 2,3 BPG). In this mutationAsp94 ->His.

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The binding of O2 tohemoglobin is affected by the concentration of H ionsand CO2 in the surrounding tissue the Bohr effecta Hemoglobin at pH 69 78mMBPGIn actively metabolizing tissue suchas muscle the concentrations of these two substances arerelatively high ie at low pH and at hydrogen ion concentrationThis effectively causes a shift of the O2 dissociationcurve for hemoglobin to the right promoting the release ofO2 This comes about because there areHbinding sites primarily His146 in the bchain whichhave a higher affinity for binding See Answer

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Compare the binding isotherm of normal hemoglobin (at pH 7.4, with 7.8 mM 2,3 BPG) with...

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Chemistry

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