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Plasticity of acetylcholine receptor gating motions via rate-energy relationships.

Plasticity of acetylcholine receptor gating motions via rate-energy relationships.

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Toolbox for analyzing finite two-state trajectories Solid-state NMR characterization of conformational plasticity within the transmembrane domain of the influenza A M2 proton channel.Molecular determinants of coupling between the domain III voltage sensor and pore of a sodium channel Temperature dependence of acetylcholine receptor channels activated by different agonists Structural answers and persistent questions about how nicotinic receptors work.Functional anatomy of an allosteric protein.Conformational dynamics of the alphaM3 transmembrane helix during acetylcholine receptor channel gating.Phenylalanine-508 mediates a cytoplasmic-membrane domain contact in the CFTR 3D structure crucial to assembly and channel function A residue at the cytoplasmic entrance of BK-type channels regulating single-channel opening by its hydrophobicity.Unliganded gating of acetylcholine receptor channels Application of rate-equilibrium free energy relationship analysis to nonequilibrium ion channel gating mechanisms The energy and work of a ligand-gated ion channel.Highly conserved tyrosine 37 stabilizes desensitized states and restricts calcium permeability of ATP-gated P2X3 receptor.Conformational plasticity of the influenza A M2 transmembrane helix in lipid bilayers under varying pH, drug binding, and membrane thickness.Universal properties of mechanisms from two-state trajectories.Properties of the generalized master equation: Green's functions and probability density functions in the path representation.

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P2860

Plasticity of acetylcholine receptor gating motions via rate-energy relationships.

http://www.wikidata.org/entity/Q34351674

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2005 nî lūn-bûn

@nan

2005 թուականի Օգոստոսին հրատարակուած գիտական յօդուած

@hyw

2005 թվականի օգոստոսին հրատարակված գիտական հոդված

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2005年の論文

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2005年学术文章

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2005年学术文章

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2005年学术文章

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2005年学术文章

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2005年学术文章

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2005年學術文章

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name

Plasticity of acetylcholine receptor gating motions via rate-energy relationships.

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Plasticity of acetylcholine receptor gating motions via rate-energy relationships.

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Plasticity of acetylcholine receptor gating motions via rate-energy relationships.

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type

label

Plasticity of acetylcholine receptor gating motions via rate-energy relationships.

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Plasticity of acetylcholine receptor gating motions via rate-energy relationships.

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Plasticity of acetylcholine receptor gating motions via rate-energy relationships.

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prefLabel

Plasticity of acetylcholine receptor gating motions via rate-energy relationships.

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Plasticity of acetylcholine receptor gating motions via rate-energy relationships.

@en

Plasticity of acetylcholine receptor gating motions via rate-energy relationships.

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BIOPHYSJ.105.068783

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Biophysical Journal

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Plasticity of acetylcholine receptor gating motions via rate-energy relationships.

@en

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Ananya Mitra

http://www.w3.org/2001/XMLSchema#string

Anthony Auerbach

http://www.w3.org/2001/XMLSchema#string

Richard Tascione

http://www.w3.org/2001/XMLSchema#string

Stuart Licht

http://www.w3.org/2001/XMLSchema#string

P2860

X-ray structure of a voltage-dependent K+ channel

Structure of the KcsA channel intracellular gate in the open state

Structure and gating mechanism of the acetylcholine receptor pore

Congenital myasthenic syndrome caused by decreased agonist binding affinity due to a mutation in the acetylcholine receptor epsilon subunit

Refined structure of the nicotinic acetylcholine receptor at 4A resolution

Structural rearrangements underlying K+-channel activation gating.

Nonlinear elasticity, proteinquakes, and the energy landscapes of functional transitions in proteins.

Gating of acetylcholine receptor channels: brownian motion across a broad transition state.

Femtochemistry: Atomic-Scale Dynamics of the Chemical Bond Using Ultrafast Lasers (Nobel Lecture) Copyright((c)) The Nobel Foundation 2000. We thank the Nobel Foundation, Stockholm, for permission to print this lecture.

Characterizing transition states in protein folding: an essential step in the puzzle.

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10.1529/BIOPHYSJ.105.068783

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