Extensive conformational transitions are required to turn on ATP hydrolysis in myosin.
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Allosteric activation transitions in enzymes and biomolecular motors: insights from atomistic and coarse-grained simulationsEffects of protonation on the hydrolysis of triphosphate in vacuum and the implications for catalysis by nucleotide hydrolyzing enzymesComputational modeling of allosteric communication reveals organizing principles of mutation-induced signaling in ABL and EGFR kinases.Myosin-catalyzed ATP hydrolysis elucidated by 31P NMR kinetic studies and 1H PFG-diffusion measurementsSimulating Protein Mediated Hydrolysis of ATP and Other Nucleoside Triphosphates by Combining QM/MM Molecular Dynamics with Advances in Metadynamics.Atomically detailed simulation of the recovery stroke in myosin by MilestoningQM/MM analysis suggests that Alkaline Phosphatase (AP) and nucleotide pyrophosphatase/phosphodiesterase slightly tighten the transition state for phosphate diester hydrolysis relative to solution: implication for catalytic promiscuity in the AP supeMolecular simulation of water and hydration effects in different environments: challenges and developments for DFTB based modelsApplication of the SCC-DFTB method to neutral and protonated water clusters and bulk water.Parametrization of DFTB3/3OB for magnesium and zinc for chemical and biological applicationsThe mechanism of the converter domain rotation in the recovery stroke of myosin motor protein.A modified QM/MM Hamiltonian with the Self-Consistent-Charge Density-Functional-Tight-Binding Theory for highly charged QM regions.Stabilization of different types of transition states in a single enzyme active site: QM/MM analysis of enzymes in the alkaline phosphatase superfamily.Description of phosphate hydrolysis reactions with the Self-Consistent-Charge Density-Functional-Tight-Binding (SCC-DFTB) theory. 1. Parameterization.QM/MM free energy simulations: recent progress and challengesEffects of ATP and actin-filament binding on the dynamics of the myosin II S1 domain.The hydrolysis activity of adenosine triphosphate in myosin: a theoretical analysis of anomeric effects and the nature of the transition stateParameterization of DFTB3/3OB for Sulfur and Phosphorus for Chemical and Biological Applications.Stabilization of the ADP/metaphosphate intermediate during ATP hydrolysis in pre-power stroke myosin: quantitative anatomy of an enzymeDFTB3: Extension of the self-consistent-charge density-functional tight-binding method (SCC-DFTB).Early stages of the recovery stroke in myosin II studied by molecular dynamics simulations.Free energy simulations of a GTPase: GTP and GDP binding to archaeal initiation factor 2.H-loop histidine catalyzes ATP hydrolysis in the E. coli ABC-transporter HlyB.Regulation and Plasticity of Catalysis in Enzymes: Insights from Analysis of Mechanochemical Coupling in Myosin.Metadynamics combined with auxiliary density functional and density functional tight-binding methods: alanine dipeptide as a case study.Comparing the catalytic strategy of ATP hydrolysis in biomolecular motors.QM/MM Description of Newly Selected Catalytic Bioscavengers Against Organophosphorus Compounds Revealed Reactivation Stimulus Mediated by Histidine Residue in the Acyl-Binding Loop
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P2860
Extensive conformational transitions are required to turn on ATP hydrolysis in myosin.
description
article científic
@ca
article scientifique
@fr
articolo scientifico
@it
artigo científico
@pt
bilimsel makale
@tr
scientific article published on July 2008
@en
vedecký článok
@sk
vetenskaplig artikel
@sv
videnskabelig artikel
@da
vědecký článek
@cs
name
Extensive conformational transitions are required to turn on ATP hydrolysis in myosin.
@en
Extensive conformational transitions are required to turn on ATP hydrolysis in myosin.
@nl
type
label
Extensive conformational transitions are required to turn on ATP hydrolysis in myosin.
@en
Extensive conformational transitions are required to turn on ATP hydrolysis in myosin.
@nl
prefLabel
Extensive conformational transitions are required to turn on ATP hydrolysis in myosin.
@en
Extensive conformational transitions are required to turn on ATP hydrolysis in myosin.
@nl
P2860
P1476
Extensive conformational transitions are required to turn on ATP hydrolysis in myosin
@en
P2093
P2860
P304
P356
10.1016/J.JMB.2008.06.071
P407
P50
P577
2008-07-01T00:00:00Z