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Ligand Binding Enhances Millisecond Conformational Exchange in Xylanase B2 from Streptomyces lividansHigh-Resolution NMR Determination of the Dynamic Structure of Membrane ProteinsA community resource of experimental data for NMR / X-ray crystal structure pairs.The Mutational Landscape of the Oncogenic MZF1 SCAN Domain in Cancer.A dynamic look backward and forward.Solution NMR Spectroscopy for the Study of Enzyme Allostery.Conformational Sub-states and Populations in Enzyme Catalysis.Sensing and signaling of oxidative stress in chloroplasts by inactivation of the SAL1 phosphoadenosine phosphataseProtein dynamics and function from solution state NMR spectroscopy.Distinct Roles for Conformational Dynamics in Protein-Ligand Interactions.Intrinsic local destabilization of the C-terminus predisposes integrin α1 I domain to a conformational switch induced by collagen binding.Thermostability of Enzymes from Molecular Dynamics SimulationsThe role of protein dynamics in allosteric effects-introduction.Effects of ligand binding on the stability of aldo-keto reductases: Implications for stabilizer or destabilizer chaperones.Defining the Structural Basis for Allosteric Product Release from E. coli Dihydrofolate Reductase Using NMR Relaxation Dispersion.3D Structure Determination of an Unstable Transient Enzyme Intermediate by Paramagnetic NMR Spectroscopy.Simultaneous determination of fast and slow dynamics in molecules using extreme CPMG relaxation dispersion experiments.The Michaelis Complex of Arginine Kinase Samples the Transition State at a Frequency That Matches the Catalytic Rate.Microsecond Dynamics in Ubiquitin Probed by Solid-State 15 N NMR Spectroscopy R1ρ Relaxation Experiments under Fast MAS (60-110 kHz).Evaluating the influence of initial magnetization conditions on extracted exchange parameters in NMR relaxation experiments: applications to CPMG and CEST.Enzymes at work are enzymes in motion.Optimization of Conformational Dynamics in an Epistatic Evolutionary Trajectory.Rescue of conformational dynamics in enzyme catalysis by directed evolution.Conformational Sampling of the Intrinsically Disordered C-Terminal Tail of DERA Is Important for Enzyme Catalysis
P2860
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P2860
description
2015 nî lūn-bûn
@nan
2015 թուականի Փետրուարին հրատարակուած գիտական յօդուած
@hyw
2015 թվականի փետրվարին հրատարակված գիտական հոդված
@hy
2015年の論文
@ja
2015年論文
@yue
2015年論文
@zh-hant
2015年論文
@zh-hk
2015年論文
@zh-mo
2015年論文
@zh-tw
2015年论文
@wuu
name
Enzyme dynamics from NMR spectroscopy
@ast
Enzyme dynamics from NMR spectroscopy
@en
Enzyme dynamics from NMR spectroscopy
@nl
type
label
Enzyme dynamics from NMR spectroscopy
@ast
Enzyme dynamics from NMR spectroscopy
@en
Enzyme dynamics from NMR spectroscopy
@nl
prefLabel
Enzyme dynamics from NMR spectroscopy
@ast
Enzyme dynamics from NMR spectroscopy
@en
Enzyme dynamics from NMR spectroscopy
@nl
P2860
P3181
P356
P1476
Enzyme dynamics from NMR spectroscopy
@en
P2093
Arthur G. Palmer
P2860
P304
P3181
P356
10.1021/AR500340A
P407
P577
2015-02-17T00:00:00Z