a mutation in the sequence of the subunit of hemoglobin was identified the mutation site is not

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A mutation in the sequence of the α subunit of hemoglobin was identified. The mutation site is not at the ligand (O2) binding site, but causes the protein to favor the “T” state over the “R” state. Compared to normal hemoglobin, what consequences do you suppose this will have on hemoglobin function? Less O2 will be released in tissues. The central cavity in the middle of the hemoglobin proteins will, on average, be smaller. There will be higher fractional saturation for the mutant protein at a given partial O2 pressure. All of the above will take place. None of the above will take place.

          A mutation in the sequence of the α subunit of hemoglobin was identified. The mutation site is not at the ligand (O2) binding site, but causes the protein to favor the “T” state over the “R” state. Compared to normal hemoglobin, what consequences do you suppose this will have on hemoglobin function?

Less O2 will be released in tissues.
The central cavity in the middle of the hemoglobin proteins will, on average, be smaller.
There will be higher fractional saturation for the mutant protein at a given partial O2 pressure.
All of the above will take place.
None of the above will take place.

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