1. The X-ray structure of Hb Rainier (Tyr145β è Cys) indicates that the mutant Cys residue forms a disulfide bond with Cys 93β of the same subunit. This holds the β subunits's C-terminal residue in a quite different orientation than it assumes in HbA. How would the following quantities for Hb Rainier compare with those of HbA? Explain. (a) The oxygen affinity, (b) the Bohr effect of HbA, (c) the Hill constant, and (d) the BPG affinity.

2. Myoglobin contains eight α helices, on of which has the following sequence: -Gln-Gly-Ala-Met-Asn-Lys-Ala-Leu-Glu-His-Phe-Arg-Lys-Asp-Ile-Ala-AlaWhich side chains are likely to be on the side of the helix that faces the interior of the protein? Which are likely to be facing the aqueous solvent? Account for the spacing of the residues facing the interior.