Induction of nonbilayer structures in diacylphosphatidylcholine model membranes by transmembrane alpha-helical peptides: importance of hydrophobic mismatch and proposed role of tryptophans.
about
Hydrophobic mismatch between helices and lipid bilayers.Transmembrane peptides stabilize inverted cubic phases in a biphasic length-dependent manner: implications for protein-induced membrane fusion.Dual functions of a small regulatory subunit in the mitochondrial calcium uniporter complexTopology of the porin MspA in the outer membrane of Mycobacterium smegmatis.The transmembrane domain of influenza hemagglutinin exhibits a stringent length requirement to support the hemifusion to fusion transitionCharacterization of the thermotropic behavior and lateral organization of lipid-peptide mixtures by a combined experimental and theoretical approach: effects of hydrophobic mismatch and role of flanking residuesAccommodation of a central arginine in a transmembrane peptide by changing the placement of anchor residues.The effect of peptide/lipid hydrophobic mismatch on the phase behavior of model membranes mimicking the lipid composition in Escherichia coli membranes.Single tryptophan and tyrosine comparisons in the N-terminal and C-terminal interface regions of transmembrane GWALP peptidesGeometry and intrinsic tilt of a tryptophan-anchored transmembrane alpha-helix determined by (2)H NMRComparisons of interfacial Phe, Tyr, and Trp residues as determinants of orientation and dynamics for GWALP transmembrane peptides.Interaction of the water-soluble protein aprotinin with liposomes: gel-filtration, turbidity studies, and 31P NMR studies.Membrane environment modulates the pKa values of transmembrane helicesInduction of morphological changes in model lipid membranes and the mechanism of membrane disruption by a large scorpion-derived pore-forming peptide.Water accessibility in a membrane-inserting peptide comparing Overhauser DNP and pulse EPR methods.Helical distortion in tryptophan- and lysine-anchored membrane-spanning alpha-helices as a function of hydrophobic mismatch: a solid-state deuterium NMR investigation using the geometric analysis of labeled alanines methodMolecular ordering of interfacially localized tryptophan analogs in ester- and ether-lipid bilayers studied by 2H-NMR.Influence of membrane-spanning alpha-helical peptides on the phase behavior of the dioleoylphosphatidylcholine/water system.Orientation and dynamics of peptides in membranes calculated from 2H-NMR dataSmall scale membrane mechanicsPeptide structural analysis by solid-state NMR spectroscopy.Order parameters of a transmembrane helix in a fluid bilayer: case study of a WALP peptideChemical shift tensor - the heart of NMR: Insights into biological aspects of proteinsInfluence of hydrophobic mismatch and amino acid composition on the lateral diffusion of transmembrane peptides.Charged or aromatic anchor residue dependence of transmembrane peptide tilt.Structural restraints and heterogeneous orientation of the gramicidin A channel closed state in lipid bilayers.Tilt angles of transmembrane model peptides in oriented and non-oriented lipid bilayers as determined by 2H solid-state NMR.Transmembrane peptide-induced lipid sorting and mechanism of Lalpha-to-inverted phase transition using coarse-grain molecular dynamics.Interfacial tryptophan residues: a role for the cation-pi effect?Insights on the interactions of synthetic amphipathic peptides with model membranes as revealed by 31P and 2H solid-state NMR and infrared spectroscopiesSite-directed mutations in the lanthipeptide mutacin 1140.Differential repositioning of the second transmembrane helices from E. coli Tar and EnvZ upon moving the flanking aromatic residues.Solid-state NMR ensemble dynamics as a mediator between experiment and simulationAromaticity at the water-hydrocarbon core interface of the membrane: consequences on the nicotinic acetylcholine receptor.Electrospray ionization mass spectrometry as a tool to analyze hydrogen/deuterium exchange kinetics of transmembrane peptides in lipid bilayers.Structural plasticity in self-assembling transmembrane β-sheets.Synthetic peptides as models for intrinsic membrane proteins.Activation of the bacterial thermosensor DesK involves a serine zipper dimerization motif that is modulated by bilayer thicknessRobust driving forces for transmembrane helix packing.Genome wide analysis of the antimicrobial peptides in Python bivittatus and characterization of cathelicidins with potent antimicrobial activity and low cytotoxicity.
P2860
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P2860
Induction of nonbilayer structures in diacylphosphatidylcholine model membranes by transmembrane alpha-helical peptides: importance of hydrophobic mismatch and proposed role of tryptophans.
description
1996 nî lūn-bûn
@nan
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
1996年论文
@zh
1996年论文
@zh-cn
name
Induction of nonbilayer struct ...... proposed role of tryptophans.
@en
type
label
Induction of nonbilayer struct ...... proposed role of tryptophans.
@en
prefLabel
Induction of nonbilayer struct ...... proposed role of tryptophans.
@en
P2093
P356
P1433
P1476
Induction of nonbilayer struct ...... proposed role of tryptophans.
@en
P2093
Greathouse DV
Killian JA
Koeppe RE 2nd
Lindblom G
Salemink I
de Planque MR
P304
P356
10.1021/BI9519258
P407
P577
1996-01-01T00:00:00Z