Conformational changes of an ion channel detected through water-protein interactions using solid-state NMR spectroscopy.
about
Cationic membrane peptides: atomic-level insight of structure-activity relationships from solid-state NMRStructural basis for the function and inhibition of an influenza virus proton channelSupramolecular Structure of Membrane-Associated Polypeptides by Combining Solid-State NMR and Molecular Dynamics SimulationsHigh-resolution structures of the M2 channel from influenza A virus reveal dynamic pathways for proton stabilization and transductionThe 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 ChannelNon-equilibrium hydrogen exchange for determination of H-bond strength and water accessibility in solid proteins.Cryoprotection of lipid membranes for high-resolution solid-state NMR studies of membrane peptides and proteins at low temperature.Probing membrane protein structure using water polarization transfer solid-state NMR.Membrane protein structure and dynamics from NMR spectroscopy.Paramagnetic Cu(II) for probing membrane protein structure and function: inhibition mechanism of the influenza M2 proton channel.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.Membrane-dependent conformation, dynamics, and lipid interactions of the fusion peptide of the paramyxovirus PIV5 from solid-state NMRMagic-angle-spinning NMR techniques for measuring long-range distances in biological macromolecules.Drug-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.Quantitative analysis of the water occupancy around the selectivity filter of a K+ channel in different gating modes.Protein-ice interaction of an antifreeze protein observed with solid-state NMR.Mechanisms of proton conduction and gating in influenza M2 proton channels from solid-state NMRProton Transport Mechanism of M2 Proton Channel Studied by Laser-Induced pH JumpNMR detection of pH-dependent histidine-water proton exchange reveals the conduction mechanism of a transmembrane proton channel.Proton and cation transport activity of the M2 proton channel from influenza A virus.Proton association constants of His 37 in the Influenza-A M218-60 dimer-of-dimers.Structures of β-hairpin antimicrobial protegrin peptides in lipopolysaccharide membranes: mechanism of gram selectivity obtained from solid-state nuclear magnetic resonance.Tidal surge in the M2 proton channel, sensed by 2D IR spectroscopy.Water Distribution, Dynamics, and Interactions with Alzheimer's β-Amyloid Fibrils Investigated by Solid-State NMR.Transmembrane communication: general principles and lessons from the structure and function of the M2 proton channel, K⁺ channels, and integrin receptors.Structural and dynamic mechanisms for the function and inhibition of the M2 proton channel from influenza A virus.Affinity of Rimantadine Enantiomers against Influenza A/M2 Protein Revisited.Conformational disorder of membrane peptides investigated from solid-state NMR line widths and line shapes.Structural Basis for Asymmetric Conductance of the Influenza M2 Proton Channel Investigated by Solid-State NMR Spectroscopy.Infrared and fluorescence assessment of the hydration status of the tryptophan gate in the influenza A M2 proton channel.Conformational plasticity of the influenza A M2 transmembrane helix in lipid bilayers under varying pH, drug binding, and membrane thickness.Structural characterization of the caveolin scaffolding domain in association with cholesterol-rich membranes.Specific binding of adamantane drugs and direction of their polar amines in the pore of the influenza M2 transmembrane domain in lipid bilayers and dodecylphosphocholine micelles determined by NMR spectroscopy.Characterization of a cyclic nucleotide-activated K(+) channel and its lipid environment by using solid-state NMR spectroscopy.Interplay between membrane curvature and protein conformational equilibrium investigated by solid-state NMR.
P2860
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P2860
Conformational changes of an ion channel detected through water-protein interactions using solid-state NMR spectroscopy.
description
2010 nî lūn-bûn
@nan
2010 թուականի Փետրուարին հրատարակուած գիտական յօդուած
@hyw
2010 թվականի փետրվարին հրատարակված գիտական հոդված
@hy
2010年の論文
@ja
2010年論文
@yue
2010年論文
@zh-hant
2010年論文
@zh-hk
2010年論文
@zh-mo
2010年論文
@zh-tw
2010年论文
@wuu
name
Conformational changes of an i ...... solid-state NMR spectroscopy.
@ast
Conformational changes of an i ...... solid-state NMR spectroscopy.
@en
Conformational changes of an i ...... solid-state NMR spectroscopy.
@nl
type
label
Conformational changes of an i ...... solid-state NMR spectroscopy.
@ast
Conformational changes of an i ...... solid-state NMR spectroscopy.
@en
Conformational changes of an i ...... solid-state NMR spectroscopy.
@nl
prefLabel
Conformational changes of an i ...... solid-state NMR spectroscopy.
@ast
Conformational changes of an i ...... solid-state NMR spectroscopy.
@en
Conformational changes of an i ...... solid-state NMR spectroscopy.
@nl
P2860
P356
P1476
Conformational changes of an i ...... solid-state NMR spectroscopy.
@en
P2093
P2860
P304
P356
10.1021/JA9096219
P407
P577
2010-02-01T00:00:00Z