In 1970, Perutz demonstrated that in deoxyhemoglobin the penultimate tyrosines (HC 2) of
both (Y and fl chains are stabilized in pockets between the F and H helices. Upon …

When the spectroscopic properties and kinetics of combination with carbon monoxide of
hemoglobin Zürich (HbZh) and its isolated abnormal chains with two sulphydryl groups …

Studies on assembly in vitro of α-globin chains with recombinant β16 Gly→ Asp, β95 Lys→
Glu, β120 Lys→ Glu and β16 Gly→ Asp, 120 Lys→ Glu human β-globin chain variants in …

Hemoglobin is one of the most widely studied proteins genetically, biochemically, and
structurally. It is an oxygen carrying tetrameric protein that imparts the characteristic red color …

In human hemoglobin (Hb) the β37 tryptophan residue (βW37), located at the hinge region
of the α1β2 interface, forms many contacts with α subunit residues of the opposite dimer, in …

Rates of in vitro synthesis of radiolabeled γ and β chains made in a cell-free transcription/
translation system were similar, but expressed globin chains were unstable. The addition of …

Abstract Hemoglobins (Hbs) Austin and Waco were detected by their electrophoretic
migration on cellulose acetate (pH 8.4) and citrate agar (pH 6.2). By these methods, both …

The linkage between the proximal histidines and the proximal polypeptide in normal adult
human hemoglobin (Hb A) has been proposed to play a major role in transmitting allosteric …

After more than a century of experimental, theoretical and computational studies, there is no
general agreement yet on the mechanisms underlying the fine regulation of hemoglobin …

Using a sol-gel encapsulation technique, we have prepared samples of CO saturated
human adult hemoglobin locked in the R or T quaternary conformation. We report time …