Is cooperative oxygen binding by hemoglobin really understood?
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Insights into the solution structure of human deoxyhemoglobin in the absence and presence of an allosteric effectorStructural and energetic basis of allosteryThe ensemble nature of allosteryAllosteric activation transitions in enzymes and biomolecular motors: insights from atomistic and coarse-grained simulationsReverse engineering the cooperative machinery of human hemoglobinOxygen binding by α(Fe2+)2β(Ni2+)2 hemoglobin crystalsThe crystal structure of a tetrameric hemoglobin in a partial hemichrome stateDirect observation of photolysis-induced tertiary structural changes in hemoglobinLigand migration and binding in the dimeric hemoglobin of Scapharca inaequivalvis.Cooperative macromolecular device revealed by meta-analysis of static and time-resolved structuresTertiary and Quaternary Allostery in Tetrameric Hemoglobin from Scapharca inaequivalvisKinetic response of a photoperturbed allosteric proteinFrom protein structure to function via single crystal optical spectroscopyHigh and low oxygen affinity conformations of T state hemoglobinTime Evolution of the Quaternary Structure of Escherichia coli Aspartate Transcarbamoylase upon Reaction with the Natural Substrates and a Slow, Tight-Binding InhibitorConfirmation of a unique intra-dimer cooperativity in the human hemoglobin alpha(1)beta(1)half-oxygenated intermediate supports the symmetry rule model of allosteric regulation.Type 1 and Type 2 scenarios in hydrogen exchange mass spectrometry studies on protein-ligand complexes.Energy transfer in molecular devices.Treating sickle cell disease by targeting HbS polymerizationAn 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 SubstitutesHaemoglobin-based oxygen carriers: research and reality towards an alternative to blood transfusions.Experimental basis for a new allosteric model for multisubunit proteins.Structural changes involved in protein binding correlate with intrinsic motions of proteins in the unbound state.Deconstructing thermodynamic parameters of a coupled system from site-specific observables.Probability fluxes and transition paths in a Markovian model describing complex subunit cooperativity in HCN2 channelsQuaternary structure of hemoglobin in solutionLigand migration through hemeprotein cavities: insights from laser flash photolysis and molecular dynamics simulations.Allostery and cooperativity revisited.The functional nitrite reductase activity of the heme-globins.Unsuspected pathway of the allosteric transition in hemoglobinPositive cooperativity without domains or subunits in a monomeric membrane channel.New look at hemoglobin allostery.Direct observation of cooperative protein structural dynamics of homodimeric hemoglobin from 100 ps to 10 ms with pump-probe X-ray solution scattering.Thermal-induced force release in oxyhemoglobin.Experiments on Hemoglobin in Single Crystals and Silica Gels Distinguish among Allosteric Models.The relationship between evolutionary and physiological variation in hemoglobin.Mechanistic Models Fit to Variable Temperature Calorimetric Data Provide Insights into Cooperativity.Modulation of reactivity and conformation within the T-quaternary state of human hemoglobin: the combined use of mutagenesis and sol-gel encapsulation.Quantitative theory for the longitudinal relaxation time of blood water.
P2860
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P2860
Is cooperative oxygen binding by hemoglobin really understood?
description
1999 nî lūn-bûn
@nan
1999 թուականի Ապրիլին հրատարակուած գիտական յօդուած
@hyw
1999 թվականի ապրիլին հրատարակված գիտական հոդված
@hy
1999年の論文
@ja
1999年論文
@yue
1999年論文
@zh-hant
1999年論文
@zh-hk
1999年論文
@zh-mo
1999年論文
@zh-tw
1999年论文
@wuu
name
Is cooperative oxygen binding by hemoglobin really understood?
@ast
Is cooperative oxygen binding by hemoglobin really understood?
@en
type
label
Is cooperative oxygen binding by hemoglobin really understood?
@ast
Is cooperative oxygen binding by hemoglobin really understood?
@en
prefLabel
Is cooperative oxygen binding by hemoglobin really understood?
@ast
Is cooperative oxygen binding by hemoglobin really understood?
@en
P356
P1476
Is cooperative oxygen binding by hemoglobin really understood?
@en
P2093
Hofrichter J
P304
P356
10.1038/7586
P577
1999-04-01T00:00:00Z