(a) Because the mutation destabilizes the T conformation of hemoglobin Rainier, the R (oxy) conformation is more stable. Therefore, the oxygen affi nity of hemoglobin Rainier is greater than normal. (b) The ion pairs that normally form in deoxyhemoglobin absorb protons. The absence of the ion pairs in hemoglobin Rainier decreases the Bohr eff ect (in fact, the Bohr eff ect in hemoglobin Rainier is about half that of normal hemoglobin). (c) Because the R conformation of hemoglobin Rainier is more stable than the T conformation, even when the molecule is not oxygenated, O2-binding cooperativity is reduced. The Hill constant of hemoglobin Rainier is therefore less than that for normal hemoglobin.