Proton nuclear magnetic resonance investigation of structural changes associated with cooperative oxygenation of human adult hemoglobin.
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A quantitative model for the cooperative mechanism of human hemoglobin.An investigation of the distal histidyl hydrogen bonds in oxyhemoglobin: effects of temperature, pH, and inositol hexaphosphate.Phthalide Derivatives from Angelica Sinensis Decrease Hemoglobin Oxygen Affinity: A New Allosteric-Modulating Mechanism and Potential Use as 2,3-BPG Functional Substitutes1H-NMR investigation of the oxygenation of hemoglobin in intact human red blood cellsA proton nuclear magnetic resonance investigation of proximal histidyl residues in human normal and abnormal hemoglobins. A probe for the heme pocket.Structure-specific model of hemoglobin cooperativity.An Origin of Cooperative Oxygen Binding of Human Adult Hemoglobin: Different Roles of the α and β Subunits in the α2β2 TetramerOximetry with the NMR signals of hemoglobin Val E11 and Tyr C7
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P2860
Proton nuclear magnetic resonance investigation of structural changes associated with cooperative oxygenation of human adult hemoglobin.
description
article científic
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article scientifique
@fr
articolo scientifico
@it
artigo científico
@pt
bilimsel makale
@tr
scientific article published on August 1979
@en
vedecký článok
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vetenskaplig artikel
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videnskabelig artikel
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vědecký článek
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name
Proton nuclear magnetic resona ...... ion of human adult hemoglobin.
@en
Proton nuclear magnetic resona ...... ion of human adult hemoglobin.
@nl
type
label
Proton nuclear magnetic resona ...... ion of human adult hemoglobin.
@en
Proton nuclear magnetic resona ...... ion of human adult hemoglobin.
@nl
prefLabel
Proton nuclear magnetic resona ...... ion of human adult hemoglobin.
@en
Proton nuclear magnetic resona ...... ion of human adult hemoglobin.
@nl
P2860
P356
P1476
Proton nuclear magnetic resona ...... ion of human adult hemoglobin.
@en
P2860
P304
P356
10.1073/PNAS.76.8.3673
P407
P577
1979-08-01T00:00:00Z