There are almost 500 naturally occurring variants of hemoglobin. Most are the result of a single amino acid substitution in a globin polypeptide chain. Some variants produce clinical illness, though not all variants have deleterious effects. A brief sample follows.
HbS (sickle-cell Hb): substitutes a Val for a Glu on the surface
Hb Cowtown: eliminates ion pairs at N and C terminus of subunits
Hb Memphis: substitutes one uncharged polar residue for another of similar size on the surface
Hb Bibba: substitutes a Pro for a Leu involved in an a helix
Hb Milwaukee: substitutes a Glu for a Val
Hb Providence: substitutes an Asn for a Lys that normally projects into the central cavity of the tetramer
Hb Philly: substitutes a Phe for a Tyr, disrupting hydrogen bonding at the a1b1 interface
Identify and explain your choices for each of the following:
(a) The Hb variant that functions similar to Mb.
(b) The variant(s) most likely to show a larger Kd for BPG