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