The effect of quaternary structure on the kinetics of conformational changes and nanosecond geminate rebinding of carbon monoxide to hemoglobin.
about
Crystal structure of horse carbonmonoxyhemoglobin-bezafibrate complex at 1.55-A resolution. A novel allosteric binding site in R-state hemoglobinDirect observation of photolysis-induced tertiary structural changes in hemoglobinMultiple geminate ligand recombinations in human hemoglobinReal-time tracking of CO migration and binding in the α and β subunits of human hemoglobin via 150-ps time-resolved Laue crystallographyOxygen and CO binding to triply NO and asymmetric NO/CO hemoglobin hybrids.Quaternary structure and geminate recombination in hemoglobin: flow-flash studies on alpha 2CO beta 2 and alpha 2 beta 2CO.Photoselection in polarized photolysis experiments on heme proteinsPhotocycles of bacteriorhodopsin in light- and dark-adapted purple membrane studied by time-resolved absorption spectroscopy.Rate of allosteric change in hemoglobin measured by modulated excitation using fluorescence detectionExperimental basis for a new allosteric model for multisubunit proteins.New insights into the allosteric mechanism of human hemoglobin from molecular dynamics simulationsLiganded hemoglobin structural perturbations by the allosteric effector L35.Picosecond transient absorption study of photodissociated carboxy hemoglobin and myoglobin.Ligand migration through hemeprotein cavities: insights from laser flash photolysis and molecular dynamics simulations.Simulation of the kinetics of ligand binding to a protein by molecular dynamics: geminate rebinding of nitric oxide to myoglobin.Control of the allosteric equilibrium of hemoglobin by cross-linking agents.Combining the influence of two low O2 affinity-inducing chemical modifications of the central cavity of hemoglobinInterfacial and distal-heme pocket mutations exhibit additive effects on the structure and function of hemoglobin.Application of linear free energy relations to protein conformational changes: the quaternary structural change of hemoglobin.New insights into allosteric mechanisms from trapping unstable protein conformations in silica gels.Current perspectives on the kinetics of hemoglobin S gelation.Changes in the apparent quantum efficiency for photolysis of Hb(CO)1.Ligand dynamics in the photodissociation of carboxyhemoglobin by subpicosecond transient infrared spectroscopyEffectors of hemoglobin. Separation of allosteric and affinity factors.A nanosecond ORD study of hemoglobin.Relationships of ligand binding, redox properties, and protonation in Coprinus cinereus peroxidase.Carbon monoxide religation kinetics to hemoglobin S polymers following ligand photolysis.
P2860
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P2860
The effect of quaternary structure on the kinetics of conformational changes and nanosecond geminate rebinding of carbon monoxide to hemoglobin.
description
1988 nî lūn-bûn
@nan
1988 թուականի Ապրիլին հրատարակուած գիտական յօդուած
@hyw
1988 թվականի ապրիլին հրատարակված գիտական հոդված
@hy
1988年の論文
@ja
1988年論文
@yue
1988年論文
@zh-hant
1988年論文
@zh-hk
1988年論文
@zh-mo
1988年論文
@zh-tw
1988年论文
@wuu
name
The effect of quaternary struc ...... carbon monoxide to hemoglobin.
@ast
The effect of quaternary struc ...... carbon monoxide to hemoglobin.
@en
The effect of quaternary struc ...... carbon monoxide to hemoglobin.
@nl
type
label
The effect of quaternary struc ...... carbon monoxide to hemoglobin.
@ast
The effect of quaternary struc ...... carbon monoxide to hemoglobin.
@en
The effect of quaternary struc ...... carbon monoxide to hemoglobin.
@nl
prefLabel
The effect of quaternary struc ...... carbon monoxide to hemoglobin.
@ast
The effect of quaternary struc ...... carbon monoxide to hemoglobin.
@en
The effect of quaternary struc ...... carbon monoxide to hemoglobin.
@nl
P2093
P2860
P356
P1476
The effect of quaternary struc ...... carbon monoxide to hemoglobin
@en
P2093
J Hofrichter
K Kitagishi
L P Murray
M Ikeda-Saito
T Yonetani
P2860
P304
P356
10.1073/PNAS.85.7.2151
P407
P50
P577
1988-04-01T00:00:00Z