Application of linear free energy relations to protein conformational changes: the quaternary structural change of hemoglobin. - Wikidata - awgldk - TriplyDB

Application of linear free energy relations to protein conformational changes: the quaternary structural change of hemoglobin.

Application of linear free energy relations to protein conformational changes: the quaternary structural change of hemoglobin.

http://www.wikidata.org/entity/Q37516292

about

Scalable rule-based modelling of allosteric proteins and biochemical networks Changes in dynamics upon oligomerization regulate substrate binding and allostery in amino acid kinase family members The crystal structure of a tetrameric hemoglobin in a partial hemichrome state Application of linear free energy relationships to the serpin-proteinase inhibition mechanism Time Evolution of the Quaternary Structure of Escherichia coli Aspartate Transcarbamoylase upon Reaction with the Natural Substrates and a Slow, Tight-Binding Inhibitor Nonlinear elasticity, proteinquakes, and the energy landscapes of functional transitions in proteins.Tracking the structural dynamics of proteins in solution using time-resolved wide-angle X-ray scattering.Relationships between structural dynamics and functional kinetics in oligomeric membrane receptors Both protein dynamics and ligand concentration can shift the binding mechanism between conformational selection and induced fit Quaternary structure dynamics and carbon monoxide binding kinetics of hemoglobin valency hybrids.Photoselection in polarized photolysis experiments on heme proteins The effect of water on the rate of conformational change in protein allostery.New insights into the allosteric mechanism of human hemoglobin from molecular dynamics simulations Plasticity of acetylcholine receptor gating motions via rate-energy relationships.Phi value analysis of heterogeneity in pathways of allosteric transitions: Evidence for parallel pathways of ATP-induced conformational changes in a GroEL ring.Free-energy landscapes of ion-channel gating are malleable: changes in the number of bound ligands are accompanied by changes in the location of the transition state in acetylcholine-receptor channels Ligand migration through hemeprotein cavities: insights from laser flash photolysis and molecular dynamics simulations.Coupling between voltage sensor activation, Ca2+ binding and channel opening in large conductance (BK) potassium channels.The extracellular linker of muscle acetylcholine receptor channels is a gating control element.Structure of the transition state for the binding of c-Myb and KIX highlights an unexpected order for a disordered system.New insights into allosteric mechanisms from trapping unstable protein conformations in silica gels.Universality of supersaturation in protein-fiber formation.Mapping the conformational wave of acetylcholine receptor channel gating.Raman dispersion spectroscopy probes heme distortions in deoxyHb-trout IV involved in its T-state Bohr effect.Allosteric kinetics and equilibria of triligated, cross-linked hemoglobin

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P2860

Application of linear free energy relations to protein conformational changes: the quaternary structural change of hemoglobin.

http://www.wikidata.org/entity/Q37516292

description

article científic

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article scientifique

@fr

articolo scientifico

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artigo científico

@pt

bilimsel makale

@tr

scientific article published on May 1991

@en

vedecký článok

@sk

vetenskaplig artikel

@sv

videnskabelig artikel

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vědecký článek

@cs

name

Application of linear free ene ...... ructural change of hemoglobin.

@en

Application of linear free ene ...... ructural change of hemoglobin.

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type

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Application of linear free ene ...... ructural change of hemoglobin.

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Application of linear free ene ...... ructural change of hemoglobin.

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Application of linear free ene ...... ructural change of hemoglobin.

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Application of linear free ene ...... ructural change of hemoglobin.

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PNAS.88.10.4472

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Proceedings of the National Academy of Sciences of the United States of America

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Application of linear free ene ...... ructural change of hemoglobin.

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P2093

Eaton WA

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Henry ER

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Hofrichter J

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P2860

ON THE NATURE OF ALLOSTERIC TRANSITIONS: A PLAUSIBLE MODEL

The effect of quaternary structure on the kinetics of conformational changes and nanosecond geminate rebinding of carbon monoxide to hemoglobin.

Rate of allosteric change in hemoglobin measured by modulated excitation using fluorescence detection

Allosteric kinetics and equilibria differ for carbon monoxide and oxygen binding to hemoglobin.

Energetics of subunit assembly and ligand binding in human hemoglobin

Conformational kinetics of triligated hemoglobin

Cooperative interactions of hemoglobin.

Quaternary conformational changes in human hemoglobin studied by laser photolysis of carboxyhemoglobin.

Nanosecond optical spectra of iron-cobalt hybrid hemoglobins: geminate recombination, conformational changes, and intersubunit communication.

Spin equilibrium and quaternary structure change in hemoglobin A. Experiments on a quantitative probe of the stereochemical mechanism of hemoglobin cooperativity.

P304

4472-4475

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scholarly article

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10.1073/PNAS.88.10.4472

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10

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88

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1991-05-01T00:00:00Z

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21120696

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2034685

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51682

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