X-ray diffraction study of binding of 2,3-diphosphoglycerate to human deoxyhaemoglobin
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Insights into the solution structure of human deoxyhemoglobin in the absence and presence of an allosteric effectorReverse engineering the cooperative machinery of human hemoglobinHigh-resolution crystal structure of deoxy hemoglobin complexed with a potent allosteric effectorThe X-ray structure determination of bovine carbonmonoxy hemoglobin at 2.1 Å resoultion and its relationship to the quaternary structures of other hemoglobin crystal formsCrystal structure of horse carbonmonoxyhemoglobin-bezafibrate complex at 1.55-A resolution. A novel allosteric binding site in R-state hemoglobinUnliganded structure of human bisphosphoglycerate mutase reveals side-chain movements induced by ligand bindingATP regulation of the ligand-binding properties in temperate and cold-adapted haemoglobins. X-ray structure and ligand-binding kinetics in the sub-Antarctic fish Eleginops maclovinusStructures of haemoglobin from woolly mammoth in liganded and unliganded statesIdentification of a Small Molecule that Increases Hemoglobin Oxygen Affinity and Reduces SS Erythrocyte SicklingThe structure of apo ArnA features an unexpected central binding pocket and provides an explanation for enzymatic cooperativityHemoglobin variants: biochemical properties and clinical correlatesSpecies differences in the binding of compounds designed to fit a site of known structure in adult human haemoglobinRed cell 2,3-diphosphoglycerate and oxygen affinity.Protein structure change studied by hydrogen-deuterium exchange, functional labeling, and mass spectrometry.Quantitative theory of hydrophobic effect as a driving force of protein structureInositol monophosphatase is a highly conserved enzyme having localized structural similarity to both glycerol 3-phosphate dehydrogenase and haemoglobin.Allosteric effectors influence the tetramer stability of both R- and T-states of hemoglobin A.Fetal and embryonic haemoglobins.Myoglobin in primary muscular disease. I. Duchenne muscular dystrophy. II. Muscular dystrophy of distal typeAn 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 SubstitutesHemoglobin affinity for 2,3-bisphosphoglycerate in solutions and intact erythrocytes: studies using pulsed-field gradient nuclear magnetic resonance and Monte Carlo simulations.Allosteric effects of the antipsychotic drug trifluoperazine on the energetics of calcium binding by calmodulinRate of allosteric change in hemoglobin measured by modulated excitation using fluorescence detectionDynamics of oxygen unloading from sickle erythrocytesTherapeutic strategies to alter the oxygen affinity of sickle hemoglobin.Quaternary structures of intermediately ligated human hemoglobin a and influences from strong allosteric effectors: resonance Raman investigation.Hemoglobin Syracuse (alpha2beta2-143(H21)His leads to Pro), a new high-affinity variant detected by special electrophoretic methods. Observations on the auto-oxidation of normal and variant hemoglobinsErythrocyte Hb-S concentration. An important factor in the low oxygen affinity of blood in sickle cell anemia.Pyridoxal compounds as specific reagents for the alpha and beta N-termini of hemoglobinGlycosylation of hemoglobin in vitro: affinity labeling of hemoglobin by glucose-6-phosphateInteraction of hemoglobin with three ligans: organic phosphates and the Bohr effect.Acetylation of sickle cell hemoglobin by aspirinSites of acetylation of sickle cell hemoglobin by aspirin.Recent studies on transport of respiratory gases by the red blood cell.New look at hemoglobin allostery.Genetically based low oxygen affinities of felid hemoglobins: lack of biochemical adaptation to high-altitude hypoxia in the snow leopard.Searching sequence space: two different approaches to dihydrofolate reductase catalysis.Practicing biochemistry without a licenseStudies of pyruvate-water isotope exchange catalysed by erythrocytes and proteins.
P2860
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P2860
X-ray diffraction study of binding of 2,3-diphosphoglycerate to human deoxyhaemoglobin
description
1972 թուականի Մայիսին հրատարակուած գիտական յօդուած
@hyw
1972 թվականի մայիսին հրատարակված գիտական հոդված
@hy
article publié dans la revue scientifique Nature
@fr
artículu científicu espublizáu en 1972
@ast
scientific journal article
@en
vedecký článok (publikovaný 1972/05/19)
@sk
vědecký článek publikovaný v roce 1972
@cs
wetenschappelijk artikel (gepubliceerd op 1972/05/19)
@nl
наукова стаття, опублікована в травні 1972
@uk
مقالة علمية (نشرت في 19-5-1972)
@ar
name
X-ray diffraction study of binding of 2,3-diphosphoglycerate to human deoxyhaemoglobin
@ast
X-ray diffraction study of binding of 2,3-diphosphoglycerate to human deoxyhaemoglobin
@en
X-ray diffraction study of binding of 2,3-diphosphoglycerate to human deoxyhaemoglobin
@nl
type
label
X-ray diffraction study of binding of 2,3-diphosphoglycerate to human deoxyhaemoglobin
@ast
X-ray diffraction study of binding of 2,3-diphosphoglycerate to human deoxyhaemoglobin
@en
X-ray diffraction study of binding of 2,3-diphosphoglycerate to human deoxyhaemoglobin
@nl
prefLabel
X-ray diffraction study of binding of 2,3-diphosphoglycerate to human deoxyhaemoglobin
@ast
X-ray diffraction study of binding of 2,3-diphosphoglycerate to human deoxyhaemoglobin
@en
X-ray diffraction study of binding of 2,3-diphosphoglycerate to human deoxyhaemoglobin
@nl
P356
P1433
P1476
X-ray diffraction study of binding of 2,3-diphosphoglycerate to human deoxyhaemoglobin
@en
P2093
P2888
P304
P356
10.1038/237146A0
P407
P577
1972-05-19T00:00:00Z
P6179
1049744005