Gramicidin A aggregation in supported gel state phosphatidylcholine bilayers.
about
Direct visualization of asymmetric behavior in supported lipid bilayers at the gel-fluid phase transition.NMR Studies of lipid lateral diffusion in the DMPC/gramicidin D/water system: peptide aggregation and obstruction effects.Unraveling lipid/protein interaction in model lipid bilayers by Atomic Force Microscopy.Filipin-induced lesions in planar phospholipid bilayers imaged by atomic force microscopyDynamics and ordering in mixed model membranes of dimyristoylphosphatidylcholine and dimyristoylphosphatidylserine: a 250-GHz electron spin resonance study using cholestane.Electron-spin resonance study of aggregation of gramicidin in dipalmitoylphosphatidylcholine bilayers and hydrophobic mismatch.Spin-labeled gramicidin a: channel formation and dissociation.Phase behavior and nanoscale structure of phospholipid membranes incorporated with acylated C14-peptides.Imaging domains in model membranes with atomic force microscopy.Channel and nonchannel forms of spin-labeled gramicidin in membranes and their equilibria.Facile lipid flip-flop in a phospholipid bilayer induced by gramicidin A measured by sum-frequency vibrational spectroscopy.Striated domains: self-organizing ordered assemblies of transmembrane alpha-helical peptides and lipids in bilayers.Membrane-mediated protein-protein interactions and connection to elastic models: a coarse-grained simulation analysis of gramicidin A association.Atomic force microscopy of model lipid membranes.Experimental evidence for hydrophobic matching and membrane-mediated interactions in lipid bilayers containing gramicidin.Effect of gramicidin A on the dipole potential of phospholipid membranes.Blistering of langmuir-blodgett bilayers containing anionic phospholipids as observed by atomic force microscopy.Detection of peptide-lipid interactions in mixed monolayers, using isotherms, atomic force microscopy, and fourier transform infrared analyses.Aggregation of gramicidin A in phospholipid Langmuir-Blodgett monolayers.Analyzing heat capacity profiles of peptide-containing membranes: cluster formation of gramicidin A.Natively folded HypF-N and its early amyloid aggregates interact with phospholipid monolayers and destabilize supported phospholipid bilayers.Coexistence of a two-states organization for a cell-penetrating peptide in lipid bilayer.Visualizing detergent resistant domains in model membranes with atomic force microscopy.Calcitonin-derived carrier peptide plays a major role in the membrane localization of a peptide-cargo complex.Substrate Effects on the Formation Process, Structure and Physicochemical Properties of Supported Lipid Bilayers.Stabilization of ion channels due to membrane-mediated elastic interaction
P2860
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P2860
Gramicidin A aggregation in supported gel state phosphatidylcholine bilayers.
description
1996 nî lūn-bûn
@nan
1996 թուականի Մարտին հրատարակուած գիտական յօդուած
@hyw
1996 թվականի մարտին հրատարակված գիտական հոդված
@hy
1996年の論文
@ja
1996年論文
@yue
1996年論文
@zh-hant
1996年論文
@zh-hk
1996年論文
@zh-mo
1996年論文
@zh-tw
1996年论文
@wuu
name
Gramicidin A aggregation in supported gel state phosphatidylcholine bilayers.
@ast
Gramicidin A aggregation in supported gel state phosphatidylcholine bilayers.
@en
type
label
Gramicidin A aggregation in supported gel state phosphatidylcholine bilayers.
@ast
Gramicidin A aggregation in supported gel state phosphatidylcholine bilayers.
@en
prefLabel
Gramicidin A aggregation in supported gel state phosphatidylcholine bilayers.
@ast
Gramicidin A aggregation in supported gel state phosphatidylcholine bilayers.
@en
P2093
P356
P1433
P1476
Gramicidin A aggregation in supported gel state phosphatidylcholine bilayers.
@en
P2093
P304
P356
10.1021/BI9520242
P407
P577
1996-03-01T00:00:00Z