Nuclear magnetic resonance study of heme-heme interaction in hemoglobin M Milwaukee: implications concerning the mechanism of cooperative ligand binding in normal hemoglobin.
about
A new mode for heme-heme interactions in hemoglobin associated with distal perturbations.Proton nuclear magnetic resonance investigation of structural changes associated with cooperative oxygenation of human adult hemoglobin.Identification of the intermediate allosteric species in human hemoglobin reveals a molecular code for cooperative switching.Hb Evans or alpha 262(E11)Val----Met beta 2; an unstable hemoglobin causing a mild hemolytic anemia.An Origin of Cooperative Oxygen Binding of Human Adult Hemoglobin: Different Roles of the α and β Subunits in the α2β2 TetramerInteractions of haemoglobin with the Neisseria meningitidis receptor HpuAB: the role of TonB and an intact proton motive force.
P2860
Nuclear magnetic resonance study of heme-heme interaction in hemoglobin M Milwaukee: implications concerning the mechanism of cooperative ligand binding in normal hemoglobin.
description
1976 nî lūn-bûn
@nan
1976 թուականի Մայիսին հրատարակուած գիտական յօդուած
@hyw
1976 թվականի մայիսին հրատարակված գիտական հոդված
@hy
1976年の論文
@ja
1976年論文
@yue
1976年論文
@zh-hant
1976年論文
@zh-hk
1976年論文
@zh-mo
1976年論文
@zh-tw
1976年论文
@wuu
name
Nuclear magnetic resonance stu ...... binding in normal hemoglobin.
@ast
Nuclear magnetic resonance stu ...... binding in normal hemoglobin.
@en
type
label
Nuclear magnetic resonance stu ...... binding in normal hemoglobin.
@ast
Nuclear magnetic resonance stu ...... binding in normal hemoglobin.
@en
prefLabel
Nuclear magnetic resonance stu ...... binding in normal hemoglobin.
@ast
Nuclear magnetic resonance stu ...... binding in normal hemoglobin.
@en
P2093
P2860
P356
P1476
Nuclear magnetic resonance stu ...... binding in normal hemoglobin.
@en
P2093
P2860
P304
P356
10.1073/PNAS.73.5.1581
P407
P577
1976-05-01T00:00:00Z