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Alamethicin aggregation in lipid membranes.

Alamethicin aggregation in lipid membranes.

http://www.wikidata.org/entity/Q33620637

about

A Rapid and Quantitative Flow Cytometry Method for the Analysis of Membrane Disruptive Antimicrobial Activity Simulations of Membrane-Disrupting Peptides II: AMP Piscidin 1 Favors Surface Defects over Pores Direct visualization of the alamethicin pore formed in a planar phospholipid matrix.Determination of mosaicity in oriented stacks of lipid bilayers.Introductory lecture: basic quantities in model biomembranes.Membrane structure correlates to function of LLP2 on the cytoplasmic tail of HIV-1 gp41 protein.Toward understanding protocell mechanosensation.New insights into the echinocandins and other fungal non-ribosomal peptides and peptaibiotics.Simulations of Membrane-Disrupting Peptides I: Alamethicin Pore Stability and Spontaneous Insertion A thermodynamic approach to alamethicin pore formation Determining Structural and Mechanical Properties from Molecular Dynamics Simulations of Lipid Vesicles.Designing foldamer-foldamer interactions in solution: the roles of helix length and terminus functionality in promoting the self-association of aminoisobutyric acid oligomers.Structure Determination of Membrane Peptides and Proteins by Solid-State NMR

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P2860

Alamethicin aggregation in lipid membranes.

http://www.wikidata.org/entity/Q33620637

description

2009 nî lūn-bûn

@nan

2009 թուականի Սեպտեմբերին հրատարակուած գիտական յօդուած

@hyw

2009 թվականի սեպտեմբերին հրատարակված գիտական հոդված

@hy

2009年の論文

@ja

2009年論文

@yue

2009年論文

@zh-hant

2009年論文

@zh-hk

2009年論文

@zh-mo

2009年論文

@zh-tw

2009年论文

@wuu

name

Alamethicin aggregation in lipid membranes.

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Alamethicin aggregation in lipid membranes.

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label

Alamethicin aggregation in lipid membranes.

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Alamethicin aggregation in lipid membranes.

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Alamethicin aggregation in lipid membranes.

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Alamethicin aggregation in lipid membranes.

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Journal of Membrane Biology

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Alamethicin aggregation in lipid membranes

@en

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Jianjun Pan

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P2860

Effect of chain length and unsaturation on elasticity of lipid bilayers.

A voltage-gated ion channel model inferred from the crystal structure of alamethicin at 1.5-A resolution

Conformation of alamethicin in oriented phospholipid bilayers determined by (15)N solid-state nuclear magnetic resonance.

Alamethicin. A rich model for channel behavior.

Analysis and evaluation of channel models: simulations of alamethicin.

Alamethicin: a peptide model for voltage gating and protein-membrane interactions.

Peptide aggregation and pore formation in a lipid bilayer: a combined coarse-grained and all atom molecular dynamics study.

Neutron scattering in the plane of membranes: structure of alamethicin pores

Probability of alamethicin conductance states varies with nonlamellar tendency of bilayer phospholipids.

X-ray scattering with momentum transfer in the plane of membrane. Application to gramicidin organization

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s00232-009-9199-8

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11-27

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