NMR detection of pH-dependent histidine-water proton exchange reveals the conduction mechanism of a transmembrane proton channel.
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Magic angle spinning NMR of virusesStructural basis for the function and inhibition of an influenza virus proton channelHigh-resolution structures of the M2 channel from influenza A virus reveal dynamic pathways for proton stabilization and transductionPhilosophy of voltage-gated proton channelsVoltage-gated proton channels: molecular biology, physiology, and pathophysiology of the H(V) familyThe Influenza M2 Ectodomain Regulates the Conformational Equilibria of the Transmembrane Proton Channel: Insights from Solid-State Nuclear Magnetic ResonanceSolid-State NMR Investigation of the Conformation, Proton Conduction, and Hydration of the Influenza B Virus M2 Transmembrane Proton ChannelProbing membrane protein structure using water polarization transfer solid-state NMR.Paramagnetic Cu(II) for probing membrane protein structure and function: inhibition mechanism of the influenza M2 proton channel.Magic angle spinning and oriented sample solid-state NMR structural restraints combine for influenza a M2 protein functional insights.Modeling the membrane environment has implications for membrane protein structure and function: influenza A M2 protein.Emerging antiviral strategies to interfere with influenza virus entry.Hydrogen-bonding partner of the proton-conducting histidine in the influenza M2 proton channel revealed from 1H chemical shiftsStructural basis for proton conduction and inhibition by the influenza M2 protein.pH-dependent conformation, dynamics, and aromatic interaction of the gating tryptophan residue of the influenza M2 proton channel from solid-state NMRDrug-induced conformational and dynamical changes of the S31N mutant of the influenza M2 proton channel investigated by solid-state NMR.Conformational analysis of the full-length M2 protein of the influenza A virus using solid-state NMR.Multivalency as a key factor for high activity of selective supported organocatalysts for the Baylis-Hillman reaction.NMR studies of active-site properties of human carbonic anhydrase II by using (15) N-labeled 4-methylimidazole as a local probe and histidine hydrogen-bond correlations.The influenza m2 cytoplasmic tail changes the proton-exchange equilibria and the backbone conformation of the transmembrane histidine residue to facilitate proton conductionIonization Properties of Histidine Residues in the Lipid Bilayer Membrane Environment.Probing Residue-Specific Water-Protein Interactions in Oriented Lipid Membranes via Solid-State NMR Spectroscopy.Probing Hydronium Ion Histidine NH Exchange Rate Constants in the M2 Channel via Indirect Observation of Dipolar-Dephased 15N Signals in Magic-Angle-Spinning NMR.Multiscale simulation reveals a multifaceted mechanism of proton permeation through the influenza A M2 proton channel.2D IR spectroscopy reveals the role of water in the binding of channel-blocking drugs to the influenza M2 channel.Proton Transport Mechanism of M2 Proton Channel Studied by Laser-Induced pH JumpProton association constants of His 37 in the Influenza-A M218-60 dimer-of-dimers.Effect of cytosolic pH on inward currents reveals structural characteristics of the proton transport cycle in the influenza A protein M2 in cell-free membrane patches of Xenopus oocytesProton affinity of the histidine-tryptophan cluster motif from the influenza A virus from ab initio molecular dynamics.Fast proton exchange in histidine: measurement of rate constants through indirect detection by NMR spectroscopyM2 proton channel structural validation from full-length protein samples in synthetic bilayers and E. coli membranes.Asymmetric protonation of EmrE.Dynamic Short Hydrogen Bonds in Histidine Tetrad of Full-Length M2 Proton Channel Reveal Tetrameric Structural Heterogeneity and Functional MechanismBeyond Structural Biology to Functional Biology: Solid-State NMR Experiments and Strategies for Understanding the M2 Proton Channel Conductance.Zinc-binding structure of a catalytic amyloid from solid-state NMR.Structure and Mechanism of the Influenza A M218-60 Dimer of Dimers.Exploring Histidine Conformations in the M2 Channel Lumen of the Influenza A Virus at Neutral pH via Molecular SimulationsActivation and proton transport mechanism in influenza A M2 channelAcid activation mechanism of the influenza A M2 proton channel.Capturing a reactive state of amyloid aggregates: NMR-based characterization of copper-bound Alzheimer disease amyloid β-fibrils in a redox cycle.
P2860
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P2860
NMR detection of pH-dependent histidine-water proton exchange reveals the conduction mechanism of a transmembrane proton channel.
description
2011 nî lūn-bûn
@nan
2011 թուականի Հոկտեմբերին հրատարակուած գիտական յօդուած
@hyw
2011 թվականի հոտեմբերին հրատարակված գիտական հոդված
@hy
2011年の論文
@ja
2011年論文
@yue
2011年論文
@zh-hant
2011年論文
@zh-hk
2011年論文
@zh-mo
2011年論文
@zh-tw
2011年论文
@wuu
name
NMR detection of pH-dependent ...... transmembrane proton channel.
@ast
NMR detection of pH-dependent ...... transmembrane proton channel.
@en
NMR detection of pH-dependent ...... transmembrane proton channel.
@nl
type
label
NMR detection of pH-dependent ...... transmembrane proton channel.
@ast
NMR detection of pH-dependent ...... transmembrane proton channel.
@en
NMR detection of pH-dependent ...... transmembrane proton channel.
@nl
prefLabel
NMR detection of pH-dependent ...... transmembrane proton channel.
@ast
NMR detection of pH-dependent ...... transmembrane proton channel.
@en
NMR detection of pH-dependent ...... transmembrane proton channel.
@nl
P2860
P356
P1476
NMR detection of pH-dependent ...... a transmembrane proton channel
@en
P2093
Fanghao Hu
Klaus Schmidt-Rohr
P2860
P304
P356
10.1021/JA2081185
P407
P50
P577
2011-10-21T00:00:00Z