3. One hemoglobin variant named Kansas has a mutation of N G4 (102) to a T, repl

Question

3. One hemoglobin variant named Kansas has a mutation of N G4 (102) to a T, replacing the N amino acid with a T amino acid results in the disruption of a hydrogen bonding interaction that is one interaction which stabilizes the R-form of hemoglobin. 3a. What does this mean for the binding affinity of Kansas hemoglobin versus normal hemoglobin? Is with the hemoglobin Kansas mutation? 3ci. Would you expect this hemoglobin variant to still show the characteristics of the Bohr Effect? Explain why or why not. 3cii. How would you test to see if this Kansas hemoglobin variant still behaves in a manner that is predicted by the Bohr Effect or not?

Explanation / Answer

3a.The mutant Hemoglobin Kansas( beta 102 asparagine to threonine)Which is a neutral mutation shows very low binding affinity towards the oxygen

3b.hemoglobin Kansas react less rapidly towards carbon monoxide than hemoglobin A ,it even differs with equilibrium with oxygen and tendency to dissociate into subunits. And Kansas hemoglobin tends to dissociate into subunits upon oxygenation.so this leads to cyanosis which is caused due to poor blood oxygenation.

3ci. The factors which affect the oxygen dissociation curve are temperature, carbon dioxide, acidity and 2,3- bis phosphoglycerate

oxyhemoglobin Kansas Will have an enhanced tetramer-dimer dissociation compared with that of hemoglobin A.

Below pH 8.5 the tetramer dimer dissociation constant of Hb Kansas is about 400 times greater than that of HbA

So oxygen dissociation curve of Kansas hemoglobin will slightly deviate from Bohr effect

3cii.the test will be done by using 2,3-bis phoshoglycerate (BPG)...the ratio of binding association towards the BPG for Kansas hemoglobin is lower compared with normal hemoglobin

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