Calculations suggest a pathway for the transverse diffusion of a hydrophobic peptide across a lipid bilayer. - Wikidata - awgldk - TriplyDB

Calculations suggest a pathway for the transverse diffusion of a hydrophobic peptide across a lipid bilayer.

Calculations suggest a pathway for the transverse diffusion of a hydrophobic peptide across a lipid bilayer.

http://www.wikidata.org/entity/Q40173072

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Implicit solvent model studies of the interactions of the influenza hemagglutinin fusion peptide with lipid bilayers.Continuum solvent model studies of the interactions of an anticonvulsant drug with a lipid bilayer.Interactions of the M2delta segment of the acetylcholine receptor with lipid bilayers: a continuum-solvent model study.Interactions of hydrophobic peptides with lipid bilayers: Monte Carlo simulations with M2delta.Structure of magainin and alamethicin in model membranes studied by x-ray reflectivity Conformation of peptides in lipid membranes studied by x-ray grazing incidence scattering.Monte Carlo simulations of peptide-membrane interactions with the MCPep web server.Analytical model and multiscale simulations of Aβ peptide aggregation in lipid membranes: towards a unifying description of conformational transitions, oligomerization and membrane damage.The Persistence-Inducing Toxin HokB Forms Dynamic Pores That Cause ATP Leakage

P2860

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P2860

Calculations suggest a pathway for the transverse diffusion of a hydrophobic peptide across a lipid bilayer.

http://www.wikidata.org/entity/Q40173072

description

2000 nî lūn-bûn

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2000年の論文

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2000年論文

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2000年論文

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2000年論文

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2000年論文

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2000年論文

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2000年论文

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2000年论文

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2000年论文

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name

Calculations suggest a pathway ...... eptide across a lipid bilayer.

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Calculations suggest a pathway ...... eptide across a lipid bilayer.

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Calculations suggest a pathway ...... eptide across a lipid bilayer.

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Biophysical Journal

P1476

Calculations suggest a pathway ...... eptide across a lipid bilayer.

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P2093

Ben-Tal N

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Kessel A

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Schulten K

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P2860

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

Free energy determinants of secondary structure formation: I. alpha-Helices

Membrane protein folding and stability: physical principles

Correlation between the free energy of a channel-forming voltage-gated peptide and the spontaneous curvature of bilayer lipids.

Continuum solvent model calculations of alamethicin-membrane interactions: thermodynamic aspects.

Structural features that modulate the transmembrane migration of a hydrophobic peptide in lipid vesicles

Membrane orientation of the N-terminal segment of alamethicin determined by solid-state 15N NMR

Collisions between helical peptides in membranes monitored using electron paramagnetic resonance: evidence that alamethicin is monomeric in the absence of a membrane potential.

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

Membrane structure of voltage-gated channel forming peptides by site-directed spin-labeling.

P304

2322-2330

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scholarly article

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10.1016/S0006-3495(00)76478-2

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