Fourier transform infrared and hydrogen/deuterium exchange reveal an exchange-resistant core of alpha-helical peptide hydrogens in the nicotinic acetylcholine receptor.
about
Tryptophan substitutions at lipid-exposed positions of the gamma M3 transmembrane domain increase the macroscopic ionic current response of the Torpedo californica nicotinic acetylcholine receptorExpression, purification, and structural characterization of CfrA, a putative iron transporter from Campylobacter jejuniPhysicochemical and immunological studies of the N-terminal domain of the Torpedo acetylcholine receptor alpha-subunit expressed in Escherichia coli.Gamma-aminobutyric acid increases the water accessibility of M3 membrane-spanning segment residues in gamma-aminobutyric acid type A receptorsFolding and assembly of large macromolecular complexes monitored by hydrogen-deuterium exchange and mass spectrometry.Structural sensitivity of a prokaryotic pentameric ligand-gated ion channel to its membrane environment.Tryptophan scanning of the acetylcholine receptor's betaM4 transmembrane domain: decoding allosteric linkage at the lipid-protein interface with ion-channel gating.Uncovering the lipidic basis for the preparation of functional nicotinic acetylcholine receptor detergent complexes for structural studiesThe structural basis of function in Cys-loop receptors.Fourier transform coupled tryptophan scanning mutagenesis identifies a bending point on the lipid-exposed δM3 transmembrane domain of the Torpedo californica nicotinic acetylcholine receptor.Kinked-helices model of the nicotinic acetylcholine receptor ion channel and its complexes with blockers: simulation by the Monte Carlo minimization method.Synthetic melanin bound to subunit vaccine antigens significantly enhances CD8+ T-cell responses.The net orientation of nicotinic receptor transmembrane alpha-helices in the resting and desensitized statesIntramembrane aromatic interactions influence the lipid sensitivities of pentameric ligand-gated ion channels.Tryptophan scanning mutagenesis reveals distortions in the helical structure of the δM4 transmembrane domain of the Torpedo californica nicotinic acetylcholine receptor.Structure of the pore-forming transmembrane domain of a ligand-gated ion channel.A distinct mechanism for activating uncoupled nicotinic acetylcholine receptors.Lipid-protein interactions at the nicotinic acetylcholine receptor. A functional coupling between nicotinic receptors and phosphatidic acid-containing lipid bilayers.Phosphatidic acid and phosphatidylserine have distinct structural and functional interactions with the nicotinic acetylcholine receptor.The chain length dependence of helix formation of the second transmembrane domain of a G protein-coupled receptor of Saccharomyces cerevisiae.Proton detection for signal enhancement in solid-state NMR experiments on mobile species in membrane proteins.Analysis of 1H/2H exchange kinetics using model infrared spectra.
P2860
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P2860
Fourier transform infrared and hydrogen/deuterium exchange reveal an exchange-resistant core of alpha-helical peptide hydrogens in the nicotinic acetylcholine receptor.
description
1995 nî lūn-bûn
@nan
1995年の論文
@ja
1995年学术文章
@wuu
1995年学术文章
@zh-cn
1995年学术文章
@zh-hans
1995年学术文章
@zh-my
1995年学术文章
@zh-sg
1995年學術文章
@yue
1995年學術文章
@zh
1995年學術文章
@zh-hant
name
Fourier transform infrared and ...... otinic acetylcholine receptor.
@en
Fourier transform infrared and ...... otinic acetylcholine receptor.
@nl
type
label
Fourier transform infrared and ...... otinic acetylcholine receptor.
@en
Fourier transform infrared and ...... otinic acetylcholine receptor.
@nl
prefLabel
Fourier transform infrared and ...... otinic acetylcholine receptor.
@en
Fourier transform infrared and ...... otinic acetylcholine receptor.
@nl
P2860
P356
P1476
Fourier transform infrared and ...... cotinic acetylcholine receptor
@en
P2093
P2860
P304
29129-29137
P356
10.1074/JBC.270.49.29129
P407
P577
1995-12-01T00:00:00Z