The energetic cost of domain reorientation in maltose-binding protein as studied by NMR and fluorescence spectroscopy
about
Structure, function, and evolution of bacterial ATP-binding cassette systemsCrystal structures of the choline/acetylcholine substrate-binding protein ChoX from Sinorhizobium meliloti in the liganded and unliganded-closed statesComputational design of ligand binding is not a solved problemEvidence for an allosteric mechanism of substrate release from membrane-transporter accessory binding proteinsMolecular details of ligand selectivity determinants in a promiscuous β-glucan periplasmic binding proteinIn vitro recombination of non-homologous genes can result in gene fusions that confer a switching phenotype to cellsStructural dissimilarity sampling with dynamically self-guiding selection.Discovery of an auto-regulation mechanism for the maltose ABC transporter MalFGK2Crystallization, data collection and data processing of maltose-binding protein (MalE) from the phytopathogen Xanthomonas axonopodis pv. citri.Visualizing lowly-populated regions of the free energy landscape of macromolecular complexes by paramagnetic relaxation enhancementStimulation of the maltose transporter ATPase by unliganded maltose binding proteinTheory, practice, and applications of paramagnetic relaxation enhancement for the characterization of transient low-population states of biological macromolecules and their complexes.Accessing a hidden conformation of the maltose binding protein using accelerated molecular dynamicsSolution NMR studies of periplasmic binding proteins and their interaction partnersBoth protein dynamics and ligand concentration can shift the binding mechanism between conformational selection and induced fitExploration of multi-state conformational dynamics and underlying global functional landscape of maltose binding protein.Computational design of receptors for an organophosphate surrogate of the nerve agent soman.Exploring sparsely populated states of macromolecules by diamagnetic and paramagnetic NMR relaxation.Rational design of a fusion protein to exhibit disulfide-mediated logic gate behavior.Mapping the Free Energy Landscape of PKA Inhibition and Activation: A Double-Conformational Selection Model for the Tandem cAMP-Binding Domains of PKA RIα.Structure-based model of allostery predicts coupling between distant sitesProtein Conformational Changes Are Detected and Resolved Site Specifically by Second-Harmonic Generation.Conformational Dynamics of apo-GlnBP Revealed by Experimental and Computational Analysis.Probing the binding entropy of ligand-protein interactions by NMR.Development of a Reagentless Biosensor for Inorganic Phosphate, Applicable over a Wide Concentration RangeThe 70-kDa heat shock protein chaperone nucleotide-binding domain in solution unveiled as a molecular machine that can reorient its functional subdomains.The energetics of structural change in maltose-binding proteinCompetitive interactions of ligands and macromolecular crowders with maltose binding protein.Interplay between conformational selection and induced fit in multidomain protein-ligand binding probed by paramagnetic relaxation enhancement.Carbohydrate-protein interactions: a 3D view by NMR.A salt-bridge motif involved in ligand binding and large-scale domain motions of the maltose-binding protein.How maltose influences structural changes to bind to maltose-binding protein: results from umbrella sampling simulation.Induced fit or conformational selection? The role of the semi-closed state in the maltose binding proteinLigand-modulated parallel mechanical unfolding pathways of maltose-binding proteins.Aptameric sensors based on structural change for diagnosis.Non-allosteric enzyme switches possess larger effector-induced changes in thermodynamic stability than their non-switch analogs.A master switch couples Mg²⁺-assisted catalysis to domain motion in B. stearothermophilus tryptophanyl-tRNA SynthetaseModeling of glycerol-3-phosphate transporter suggests a potential 'tilt' mechanism involved in its function.Molecular dynamics simulations of NAD+-induced domain closure in horse liver alcohol dehydrogenase.Local encoding of computationally designed enzyme activity.
P2860
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P2860
The energetic cost of domain reorientation in maltose-binding protein as studied by NMR and fluorescence spectroscopy
description
2003 nî lūn-bûn
@nan
2003年の論文
@ja
2003年論文
@yue
2003年論文
@zh-hant
2003年論文
@zh-hk
2003年論文
@zh-mo
2003年論文
@zh-tw
2003年论文
@wuu
2003年论文
@zh
2003年论文
@zh-cn
name
The energetic cost of domain r ...... and fluorescence spectroscopy
@ast
The energetic cost of domain r ...... and fluorescence spectroscopy
@en
type
label
The energetic cost of domain r ...... and fluorescence spectroscopy
@ast
The energetic cost of domain r ...... and fluorescence spectroscopy
@en
prefLabel
The energetic cost of domain r ...... and fluorescence spectroscopy
@ast
The energetic cost of domain r ...... and fluorescence spectroscopy
@en
P2860
P356
P1476
The energetic cost of domain r ...... and fluorescence spectroscopy
@en
P2093
Rhea P Hudson
P2860
P304
12700-12705
P356
10.1073/PNAS.2134311100
P407
P577
2003-10-06T00:00:00Z