Nanosecond absorption spectroscopy of hemoglobin: elementary processes in kinetic cooperativity.
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Spontaneous quaternary and tertiary T-R transitions of human hemoglobin in molecular dynamics simulationStructural dynamics of ligand diffusion in the protein matrix: A study on a new myoglobin mutant Y(B10) Q(E7) R(E10)Picosecond study of the near infrared absorption band of hemoglobin after photolysis of carbonmonoxyhemoglobin.Myoglobin strikes back.Allosteric action in real time: time-resolved crystallographic studies of a cooperative dimeric hemoglobinMultiple geminate ligand recombinations in human hemoglobinTracking the structural dynamics of proteins in solution using time-resolved wide-angle X-ray scattering.Protein structural dynamics in solution unveiled via 100-ps time-resolved x-ray scattering.The effect of quaternary structure on the kinetics of conformational changes and nanosecond geminate rebinding of carbon monoxide to hemoglobin.Real-time tracking of CO migration and binding in the α and β subunits of human hemoglobin via 150-ps time-resolved Laue crystallographyDeriving reaction mechanisms from kinetic spectroscopy. Application to late rhodopsin intermediates.Quaternary structure dynamics and carbon monoxide binding kinetics of hemoglobin valency hybrids.Metastable CO binding sites in the photoproduct of a novel cooperative dimeric hemoglobin.Nanosecond time-resolved absorption studies of human oxyhemoglobin photolysis intermediatesTime-resolved magnetic circular dichroism spectroscopy of photolyzed carbonmonoxy cytochrome c oxidase (cytochrome aa3)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 detectionNanosecond optical rotatory dispersion spectroscopy: application to photolyzed hemoglobin-CO kinetics.Heme reactivity is uncoupled from quaternary structure in gel-encapsulated hemoglobin: a resonance Raman spectroscopic study.Experimental basis for a new allosteric model for multisubunit proteins.The effect of water on the rate of conformational change in protein allostery.The use of principal component analysis to resolve the spectra and kinetics of cytochrome c oxidase reduction by 5,10-dihydro-5-methyl phenazineConformational kinetics of triligated hemoglobinTime-resolved circular dichroism and absorption studies of the photolysis reaction of (carbonmonoxy)myoglobin.Picosecond transient absorption study of photodissociated carboxy hemoglobin and myoglobin.Direct observations of ligand dynamics in hemoglobin by subpicosecond infrared spectroscopyWater and ligand entry in myoglobin: assessing the speed and extent of heme pocket hydration after CO photodissociation.The Monod-Wyman-Changeux allosteric model accounts for the quaternary transition dynamics in wild type and a recombinant mutant human hemoglobin.Ligand migration through hemeprotein cavities: insights from laser flash photolysis and molecular dynamics simulations.Motion of proximal histidine and structural allosteric transition in soluble guanylate cyclase.Linkage between ligand binding and the dimer-tetramer equilibrium in the Monod-Wyman-Changeux model of hemoglobin.Applications of ultrafast laser spectroscopy for the study of biological systems.Experiments on Hemoglobin in Single Crystals and Silica Gels Distinguish among Allosteric Models.Conformational diversity of acid-denatured cytochrome c studied by a matrix analysis of far-UV CD spectra.Molecular dynamics simulation of photodissociation of carbon monoxide from hemoglobinFast events in protein folding initiated by nanosecond laser photolysis.Application of linear free energy relations to protein conformational changes: the quaternary structural change of hemoglobin.Five-coordinate H64Q neuroglobin as a ligand-trap antidote for carbon monoxide poisoning.New insights into allosteric mechanisms from trapping unstable protein conformations in silica gels.
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P2860
Nanosecond absorption spectroscopy of hemoglobin: elementary processes in kinetic cooperativity.
description
article científic
@ca
article scientifique
@fr
articolo scientifico
@it
artigo científico
@pt
bilimsel makale
@tr
scientific article published on April 1983
@en
vedecký článok
@sk
vetenskaplig artikel
@sv
videnskabelig artikel
@da
vědecký článek
@cs
name
Nanosecond absorption spectros ...... sses in kinetic cooperativity.
@en
Nanosecond absorption spectros ...... sses in kinetic cooperativity.
@nl
type
label
Nanosecond absorption spectros ...... sses in kinetic cooperativity.
@en
Nanosecond absorption spectros ...... sses in kinetic cooperativity.
@nl
prefLabel
Nanosecond absorption spectros ...... sses in kinetic cooperativity.
@en
Nanosecond absorption spectros ...... sses in kinetic cooperativity.
@nl
P2093
P2860
P356
P1476
Nanosecond absorption spectros ...... sses in kinetic cooperativity.
@en
P2093
P2860
P304
P356
10.1073/PNAS.80.8.2235
P407
P577
1983-04-01T00:00:00Z