Large-scale allosteric conformational transitions of adenylate kinase appear to involve a population-shift mechanism. - Wikidata - awgldk - TriplyDB

Large-scale allosteric conformational transitions of adenylate kinase appear to involve a population-shift mechanism.

Large-scale allosteric conformational transitions of adenylate kinase appear to involve a population-shift mechanism.

http://www.wikidata.org/entity/Q36276838

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Many local motions cooperate to produce the adenylate kinase conformational transition Coarse-grained description of protein internal dynamics: an optimal strategy for decomposing proteins in rigid subunits Rational modulation of conformational fluctuations in adenylate kinase reveals a local unfolding mechanism for allostery and functional adaptation in proteins Principles and Overview of Sampling Methods for Modeling Macromolecular Structure and Dynamics Allosteric activation transitions in enzymes and biomolecular motors: insights from atomistic and coarse-grained simulations RNA mimicry by the fap7 adenylate kinase in ribosome biogenesis Exploring the conformational transitions of biomolecular systems using a simple two-state anisotropic network model Minimum free energy path of ligand-induced transition in adenylate kinase A Coupled Equilibrium Shift Mechanism in Calmodulin-Mediated Signal Transduction Enzymes with lid-gated active sites must operate by an induced fit mechanism instead of conformational selection Structure and biochemical characterization of an adenylate kinase originating from the psychrophilic organismMarinibacillus marinus Allostery in the ferredoxin protein motif does not involve a conformational switch Structure, function, and folding of phosphoglycerate kinase are strongly perturbed by macromolecular crowding The role of oligomerization and cooperative regulation in protein function: the case of tryptophan synthase Effects of macromolecular crowding on protein conformational changes Binding leverage as a molecular basis for allosteric regulation A role for both conformational selection and induced fit in ligand binding by the LAO protein Interconversion of functional motions between mesophilic and thermophilic adenylate kinases Protein dynamics of the HIF-2α PAS-B domain upon heterodimerization and ligand binding Correlated inter-domain motions in adenylate kinase Hotspot mutations in KIT receptor differentially modulate its allosterically coupled conformational dynamics: impact on activation and drug sensitivity Quantitatively characterizing the ligand binding mechanisms of choline binding protein using Markov state model analysis Motion Tree Delineates Hierarchical Structure of Protein Dynamics Observed in Molecular Dynamics Simulation Hierarchical modeling of activation mechanisms in the ABL and EGFR kinase domains: thermodynamic and mechanistic catalysts of kinase activation by cancer mutations.Energy landscape along an enzymatic reaction trajectory: hinges or cracks?Anomalies in the vibrational dynamics of proteins are a consequence of fractal-like structure Small- and large-scale conformational changes of adenylate kinase: a molecular dynamics study of the subdomain motion and mechanics Ligand-induced global transitions in the catalytic domain of protein kinase A.Computation of conformational transitions in proteins by virtual atom molecular mechanics as validated in application to adenylate kinase.Zipping and unzipping of adenylate kinase: atomistic insights into the ensemble of open<-->closed transitions.Iterative cluster-NMA: A tool for generating conformational transitions in proteins.Frustration, specific sequence dependence, and nonlinearity in large-amplitude fluctuations of allosteric proteins.ClustENM: ENM-Based Sampling of Essential Conformational Space at Full Atomic Resolution.Computational modeling of allosteric communication reveals organizing principles of mutation-induced signaling in ABL and EGFR kinases.The energy landscape analysis of cancer mutations in protein kinases Sequence and structure signatures of cancer mutation hotspots in protein kinases Data-driven approach to decomposing complex enzyme kinetics with surrogate models.Tracing conformational changes in proteins.Multiscale coarse-graining of the protein energy landscape Substrate induced population shifts and stochastic gating in the PBCV-1 mRNA capping enzyme

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P2860

Large-scale allosteric conformational transitions of adenylate kinase appear to involve a population-shift mechanism.

http://www.wikidata.org/entity/Q36276838

description

2007 nî lūn-bûn

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Large-scale allosteric conform ...... a population-shift mechanism.

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Large-scale allosteric conform ...... a population-shift mechanism.

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Large-scale allosteric conform ...... a population-shift mechanism.

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Large-scale allosteric conform ...... a population-shift mechanism.

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Large-scale allosteric conform ...... a population-shift mechanism.

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Large-scale allosteric conform ...... a population-shift mechanism.

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

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Large-scale allosteric conform ...... a population-shift mechanism.

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Charles L Brooks

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Karunesh Arora

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P2860

Application of a Theory of Enzyme Specificity to Protein Synthesis

Conformational transitions of adenylate kinase: switching by cracking

Mechanism-based design of a protein kinase inhibitor

Crystal structures of two mutants of adenylate kinase from Escherichia coli that modify the Gly-loop

All-atom empirical potential for molecular modeling and dynamics studies of proteins

Molecular dynamics and protein function.

Structure of the complex between adenylate kinase from Escherichia coli and the inhibitor Ap5A refined at 1.9 A resolution. A model for a catalytic transition state

Movie of the structural changes during a catalytic cycle of nucleoside monophosphate kinases

Mechanochemical coupling in the myosin motor domain. II. Analysis of critical residues

Comparison of experimental binding data and theoretical models in proteins containing subunits

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