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Structural and energetic basis of allosteryAllosteric activation transitions in enzymes and biomolecular motors: insights from atomistic and coarse-grained simulationsReverse engineering the cooperative machinery of human hemoglobinSpontaneous quaternary and tertiary T-R transitions of human hemoglobin in molecular dynamics simulationStructure of fully liganded Hb ζ2β2strapped in a tense conformationA quantitative model for the cooperative mechanism of human hemoglobin.Allosteric kinetics and equilibria differ for carbon monoxide and oxygen binding to hemoglobin.Heme reactivity is uncoupled from quaternary structure in gel-encapsulated hemoglobin: a resonance Raman spectroscopic study.Conformational kinetics of triligated hemoglobinOxygen-organophosphate linkage in hemoglobin A. The double hump effect.Allostery and cooperativity revisited.Unsuspected pathway of the allosteric transition in hemoglobinNew look at hemoglobin allostery.Experiments on Hemoglobin in Single Crystals and Silica Gels Distinguish among Allosteric Models.The allosteric mechanism of the chaperonin GroEL: a dynamic analysis.Extensive conformational transitions are required to turn on ATP hydrolysis in myosin.Identification of the intermediate allosteric species in human hemoglobin reveals a molecular code for cooperative switching.Allosteric interpretation of the measurement of cooperative free energy in cyanomethemoglobin.New insights into allosteric mechanisms from trapping unstable protein conformations in silica gels.Mapping polymerization and allostery of hemoglobin S using point mutations.Tertiary and quaternary structural basis of oxygen affinity in human hemoglobin as revealed by multiscale simulations.Structure of liganded T-state haemoglobin from cat (Felis silvestris catus), a low oxygen-affinity species, in two different crystal forms.Direct observation of conformational population shifts in crystalline human hemoglobin.A theoretical study on structural, spectroscopic and energetic properties of acetamide clusters [CH3CONH2] (n=1-15).Tetrameric hemoglobin expressed in Escherichia coli. Evidence of heterogeneous subunit assembly.
P2860
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P2860
description
article científic
@ca
article scientifique
@fr
articolo scientifico
@it
artigo científico
@pt
bilimsel makale
@tr
scientific article published on December 1983
@en
vedecký článok
@sk
vetenskaplig artikel
@sv
videnskabelig artikel
@da
vědecký článek
@cs
name
Structure-specific model of hemoglobin cooperativity.
@en
Structure-specific model of hemoglobin cooperativity.
@nl
type
label
Structure-specific model of hemoglobin cooperativity.
@en
Structure-specific model of hemoglobin cooperativity.
@nl
prefLabel
Structure-specific model of hemoglobin cooperativity.
@en
Structure-specific model of hemoglobin cooperativity.
@nl
P2860
P356
P1476
Structure-specific model of hemoglobin cooperativity.
@en
P2093
P2860
P304
P356
10.1073/PNAS.80.23.7055
P407
P577
1983-12-01T00:00:00Z