Thermodynamic analysis of incorporation and aggregation in a membrane: application to the pore-forming peptide alamethicin.
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What Ion Flow along Ion Channels Can Tell us about Their Functional ActivityConformation of alamethicin in oriented phospholipid bilayers determined by (15)N solid-state nuclear magnetic resonance.Elucidation of the interaction mechanism with liposomes of gH625-peptide functionalized dendrimersMembrane-dependent oligomeric structure and pore formation of a beta-hairpin antimicrobial peptide in lipid bilayers from solid-state NMR.A host-guest system to study structure-function relationships of membrane fusion peptides.Voltage-dependent conductance for alamethicin in phospholipid vesicles. A test for the mechanism of gating.Dynamics and aggregation of the peptide ion channel alamethicin. Measurements using spin-labeled peptidesContinuum solvent model calculations of alamethicin-membrane interactions: thermodynamic aspects.Effect of protein aggregation in the aqueous phase on the binding of membrane proteins to membranes.Structural features that modulate the transmembrane migration of a hydrophobic peptide in lipid vesiclesPore formation kinetics in membranes, determined from the release of marker molecules out of liposomes or cells.Membrane lysis by the antibacterial peptides cecropins B1 and B3: A spin-label electron spin resonance study on phospholipid bilayersBiophysical characterization and membrane interaction of the two fusion loops of glycoprotein B from herpes simplex type I virus.Incorporation kinetics in a membrane, studied with the pore-forming peptide alamethicinAlamethicin adsorption to a planar lipid bilayerA Coiled-Coil Peptide Shaping Lipid Bilayers upon Fusion.Template-assembled melittin: structural and functional characterization of a designed, synthetic channel-forming protein.The structure and organization within the membrane of the helices composing the pore-forming domain of Bacillus thuringiensis delta-endotoxin are consistent with an "umbrella-like" structure of the poreInteraction of a synthetic mitochondrial presequence with isolated yeast mitochondria: mechanism of binding and kinetics of importHydrogen bond stabilities in membrane-reconstituted alamethicin from amide-resolved hydrogen-exchange measurementsComputational studies of peptide-induced membrane pore formation.Antimicrobial peptide magainin I from Xenopus skin forms anion-permeable channels in planar lipid bilayersMembrane partitioning of the cleavage peptide in flock house virus.Calculations suggest a pathway for the transverse diffusion of a hydrophobic peptide across a lipid bilayer.The presence of a single N-terminal histidine residue enhances the fusogenic properties of a Membranotropic peptide derived from herpes simplex virus type 1 glycoprotein H.Peptide models for membrane channels.Dimerization in tailoring uptake efficacy of the HSV-1 derived membranotropic peptide gH625.Artificial Lipid Membranes: Past, Present, and Future.A thermodynamic approach to alamethicin pore formationLipid-alamethicin interactions influence alamethicin orientationThe structure and organization of synthetic putative membranous segments of ROMK1 channel in phospholipid membranes.Pore formation in a lipid bilayer under a tension ramp: modeling the distribution of rupture tensions.Androctonin, a hydrophilic disulphide-bridged non-haemolytic anti-microbial peptide: a plausible mode of action.Reversible surface aggregation in pore formation by pardaxin.Solution structure and interaction of the antimicrobial polyphemusins with lipid membranes.A peptide analogue to a fusion domain within photoreceptor peripherin/rds promotes membrane adhesion and depolarization.Analysis of a membrane interacting region of herpes simplex virus type 1 glycoprotein H.A synthetic S6 segment derived from KvAP channel self-assembles, permeabilizes lipid vesicles, and exhibits ion channel activity in bilayer lipid membrane.Secondary structure, membrane localization, and coassembly within phospholipid membranes of synthetic segments derived from the N- and C-termini regions of the ROMK1 K+ channelEffects of electric field on alamethicin bound at the lipid-water interface: a molecular mechanics study.
P2860
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P2860
Thermodynamic analysis of incorporation and aggregation in a membrane: application to the pore-forming peptide alamethicin.
description
1986 nî lūn-bûn
@nan
1986年の論文
@ja
1986年学术文章
@wuu
1986年学术文章
@zh
1986年学术文章
@zh-cn
1986年学术文章
@zh-hans
1986年学术文章
@zh-my
1986年学术文章
@zh-sg
1986年學術文章
@yue
1986年學術文章
@zh-hant
name
Thermodynamic analysis of inco ...... e-forming peptide alamethicin.
@en
Thermodynamic analysis of inco ...... e-forming peptide alamethicin.
@nl
type
label
Thermodynamic analysis of inco ...... e-forming peptide alamethicin.
@en
Thermodynamic analysis of inco ...... e-forming peptide alamethicin.
@nl
prefLabel
Thermodynamic analysis of inco ...... e-forming peptide alamethicin.
@en
Thermodynamic analysis of inco ...... e-forming peptide alamethicin.
@nl
P2093
P1476
Thermodynamic analysis of inco ...... e-forming peptide alamethicin.
@en
P2093
P304
P356
10.1016/0005-2736(86)90573-0
P577
1986-09-01T00:00:00Z