The conducting form of gramicidin A is a right-handed double-stranded double helix
about
Membrane Protein Crystallization in Lipidic Mesophases. Hosting Lipid Effects on the Crystallization and Structure of a Transmembrane PeptideUse of europium ions for SAD phasing of lysozyme at the Cu Kα wavelengthCovalently linked gramicidin channels: effects of linker hydrophobicity and alkaline metals on different stereoisomers.The preference of tryptophan for membrane interfaces: insights from N-methylation of tryptophans in gramicidin channelsCoarse-grained molecular dynamics provides insight into the interactions of lipids and cholesterol with rhodopsin.Common structural features in gramicidin and other ion channels.Gramicidin D conformation, dynamics and membrane ion transport.Functional interrelationships between cell membrane and cell wall in antimicrobial peptide-mediated killing of Staphylococcus aureus.Diversity in antistaphylococcal mechanisms among membrane-targeting antimicrobial peptidesSimulation study of a gramicidin/lipid bilayer system in excess water and lipid. I. Structure of the molecular complex.Structural restraints and heterogeneous orientation of the gramicidin A channel closed state in lipid bilayers.Spin-labeled gramicidin a: channel formation and dissociation.Channel and nonchannel forms of spin-labeled gramicidin in membranes and their equilibria.Validation of the single-stranded channel conformation of gramicidin A by solid-state NMR.Failures in clinical treatment of Staphylococcus aureus Infection with daptomycin are associated with alterations in surface charge, membrane phospholipid asymmetry, and drug binding.Gramicidin-perforated patch recording revealed the oscillatory nature of secretory Cl- movements in salivary acinar cellsRattusin structure reveals a novel defensin scaffold formed by intermolecular disulfide exchanges.Water permeation through gramicidin A: desformylation and the double helix: a molecular dynamics study.Aggregation of gramicidin A in phospholipid Langmuir-Blodgett monolayers.Gramicidin A disassembles large conductive clusters of its lysine-substituted derivatives in lipid membranes.Dynamic combinatorial enrichment of polyconformational D-/L-peptide dimers.The membrane interface dictates different anchor roles for "inner pair" and "outer pair" tryptophan indole rings in gramicidin A channels.The pH-dependent induction of lipid membrane ionic permeability by N-terminally lysine-substituted analogs of gramicidin A.Modeling the membrane environment for membrane proteins.Alanine scan of the peptide antibiotic feglymycin: assessment of amino acid side chains contributing to antimicrobial activity.A unimolecular channel formed by dual helical peptide modified pillar[5]arene: correlating transmembrane transport properties with antimicrobial activity and haemolytic toxicity.Sequence Engineering to Control the Helix Handedness of Peptide Foldamers.Limiting Assumptions in the Design of Peptidomimetics.Protein displacements under external forces: An atomistic Langevin dynamics approach.Stability of the gramicidin-A channel structure in view of nanofiltration: a computational and experimental study
P2860
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P2860
The conducting form of gramicidin A is a right-handed double-stranded double helix
description
1998 nî lūn-bûn
@nan
1998 թուականի Հոկտեմբերին հրատարակուած գիտական յօդուած
@hyw
1998 թվականի հոտեմբերին հրատարակված գիտական հոդված
@hy
1998年の論文
@ja
1998年論文
@yue
1998年論文
@zh-hant
1998年論文
@zh-hk
1998年論文
@zh-mo
1998年論文
@zh-tw
1998年论文
@wuu
name
The conducting form of gramicidin A is a right-handed double-stranded double helix
@ast
The conducting form of gramicidin A is a right-handed double-stranded double helix
@en
The conducting form of gramicidin A is a right-handed double-stranded double helix
@nl
type
label
The conducting form of gramicidin A is a right-handed double-stranded double helix
@ast
The conducting form of gramicidin A is a right-handed double-stranded double helix
@en
The conducting form of gramicidin A is a right-handed double-stranded double helix
@nl
prefLabel
The conducting form of gramicidin A is a right-handed double-stranded double helix
@ast
The conducting form of gramicidin A is a right-handed double-stranded double helix
@en
The conducting form of gramicidin A is a right-handed double-stranded double helix
@nl
P2093
P2860
P356
P1476
The conducting form of gramicidin A is a right-handed double-stranded double helix
@en
P2093
P2860
P304
P356
10.1073/PNAS.95.22.12950
P407
P577
1998-10-27T00:00:00Z