TY - JOUR
T1 - Oxygen binding to α-subunits in high-salt crystals of T-state hemoglobin
AU - Vásquez, Gregory B.
AU - Ji, Xinhua
AU - Pechik, Igor
AU - Fronticelli, Clara
AU - Gilliland, Gary L.
N1 - Copyright:
Copyright 2004 Elsevier Science B.V., Amsterdam. All rights reserved.
PY - 1999
Y1 - 1999
N2 - The crystal structures of a partially-oxygenated, human, T-state hemoglobin variant, βC112G, and a deoxy structure of a related hemoglobin construct, β(C93A+C112G), have been determined at 2.0 Å and 1.8 Å resolution, respectively. Oxygen molecules fully occupy the α1-heme and partially occupy the α2-heme binding sites of the βC112G mutant hemoglobin. Comparisons of these structures with deoxy-, oxy-, and carboxyhemoglobin provide insight into hemoglobin's allosteric transition.
AB - The crystal structures of a partially-oxygenated, human, T-state hemoglobin variant, βC112G, and a deoxy structure of a related hemoglobin construct, β(C93A+C112G), have been determined at 2.0 Å and 1.8 Å resolution, respectively. Oxygen molecules fully occupy the α1-heme and partially occupy the α2-heme binding sites of the βC112G mutant hemoglobin. Comparisons of these structures with deoxy-, oxy-, and carboxyhemoglobin provide insight into hemoglobin's allosteric transition.
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M3 - Article
AN - SCOPUS:0346491823
SN - 0929-8665
VL - 6
SP - 59
EP - 66
JO - Protein and Peptide Letters
JF - Protein and Peptide Letters
IS - 2
ER -