Nuclear magnetic resonance studies of hemoglobins. VII. Tertiary structure around ligand binding site in carbonmonoxyhemoglobin

Abstract

can be assigned to the /3E11 valine methyls. The spectra of isolated a and ß chains indicate the a-and /3-chain con-

Sickle Cell Hemoglobin with Mutation at αHis-50 Has Improved Solubility

“…The ␥ 2 -CH 3 groups of ␣Val-62 and ␤Val-67 of the distal heme pocket give resonances at Ϫ1.75 and Ϫ1.82 ppm relative to 2,2-dimethyl-2-silapentanesulfonic acid, respectively (41,42). The signals at Ϫ1.75 ppm are similar among all six proteins studied.…”

Autoxidation and Oxygen Binding Properties of Recombinant Hemoglobins with Substitutions at the αVal-62 or βVal-67 Position of the Distal Heme Pocket

“…The signals at Ϫ1.75 and Ϫ1.82 ppm relative to DSS have been assigned to the ␥ 2 -CH 3 group of ␣Val-62 and ␤Val-67, respectively (46,47). For the ␣-subunit E11 mutations, the resonance corresponding to ␣Val-62 is absent from the spectra.…”

Substitution of the Heme Binding Module in Hemoglobin α- and β-Subunits

“…Association Properties-Before analyzing the heme environmental structure of the ␤␣(HBM)-subunit, we investigated its association property with native hemoglobin subunits, since the heme environmental structure of globin proteins is very sensitive to the subunit assembly (33,34). Fig.…”