Search results for "bilayers"

showing 10 items of 140 documents

Calorimetric Behavior of Phosphatidylcholine/Phosphatidylethanolamine Bilayers is Compatible with the Superlattice Model

2012

Differential scanning calorimetry was used to study the phase behavior of binary lipid bilayers consisting of phosphatidylcholine (PC) and phosphatidylethanolamine (PE) of varying acyl chain length. A two-state transition model was used to resolve the individual transition components, and the two-state transition enthalpy, the relative enthalpy, and the transition temperature of each component were plotted as a function of composition. Intriguingly, abrupt changes in these thermodynamic parameters were observed at or close to many "critical" X(PE) values predicted by the superlattice model proposing that phospholipids with different headgroups tend to adopt regular rather than random latera…

Models MolecularSuperlatticeLipid BilayersEnthalpyAnalytical chemistryThermodynamics02 engineering and technologyCalorimetryArticle03 medical and health scienceschemistry.chemical_compoundDifferential scanning calorimetryPhase (matter)PhosphatidylcholineMaterials ChemistryTransition TemperaturePhysical and Theoretical ChemistryLipid bilayer030304 developmental biologyPhysics::Biological Physics0303 health sciencesCalorimetry Differential ScanningChemistryPhosphatidylethanolaminesTransition temperature021001 nanoscience & nanotechnologySurfaces Coatings and FilmsPhosphatidylcholinesThermodynamics0210 nano-technologyThe Journal of Physical Chemistry B
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Functional competition within a membrane: Lipid recognition vs. transmembrane helix oligomerization

2015

Abstract Binding of specific lipids to large, polytopic membrane proteins is well described, and it is clear that such lipids are crucial for protein stability and activity. In contrast, binding of defined lipid species to individual transmembrane helices and regulation of transmembrane helix monomer–oligomer equilibria by binding of distinct lipids is a concept, which has emerged only lately. Lipids bind to single-span membrane proteins, both in the juxta-membrane region as well as in the hydrophobic membrane core. While some interactions counteract transmembrane helix oligomerization, in other cases lipid binding appears to enhance oligomerization. As reversible oligomerization is involve…

Models MolecularSyntaxin 1AMembrane lipidsLipid BilayersBiophysicsBiologyBinding CompetitiveBiochemistryProtein Structure SecondaryMembrane LipidsLipid bindingOligomerizationIntegral membrane proteinC99Transmembrane channelsMolecular StructureMembrane transport proteinCell MembranePeripheral membrane proteinMembrane ProteinsCell Biologyp24Transmembrane proteinProtein Structure TertiaryCell biologyTransmembrane domainMembrane proteinMembrane proteinbiology.proteinlipids (amino acids peptides and proteins)Protein BindingBiochimica et Biophysica Acta (BBA) - Biomembranes
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Cluster organization and pore structure of ion channels formed by beticolin 3, a nonpeptidic fungal toxin

1999

Beticolin 3 (B3) belongs to a family of nonpeptidic phytotoxins produced by the fungus Cercospora beticola, which present a broad spectrum of cytotoxic effects. We report here that, at cytotoxic concentration (10 microM), B3 formed voltage-independent, weakly selective ion channels with multiple conductance levels in planar lipid bilayers. In symmetrical standard solutions, conductance values of the first levels were, respectively, 16 +/- 1 pS, 32 +/- 2 pS, and 57 +/- 2 pS (n = 4) and so on, any conductance level being roughly twice the lower one. Whether a cluster organization of elementary channels or different channel structures underlies this particular property was addressed by investi…

Models Molecular[SDV]Life Sciences [q-bio]Lipid BilayersMolecular ConformationBiophysicsIn Vitro Techniques010402 general chemistryHeterocyclic Compounds 4 or More Rings01 natural sciencesBiophysical PhenomenaIon ChannelsMembrane Potentials03 medical and health sciencesElectrical resistivity and conductivityCluster (physics)Lipid bilayerIon channelComputingMilieux_MISCELLANEOUS030304 developmental biologyMembrane potential0303 health sciencesChemistryElectric ConductivityConductanceBiological activityMycotoxins0104 chemical sciencesCrystallographySelectivityResearch Article
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Formation of irreversibly bound annexin A1 protein domains on POPC/POPS solid supported membranes

2008

AbstractThe specific interaction of annexin A1 with phospholipid bilayers is scrutinized by means of scanning force and fluorescence microscopy, quartz crystal microbalance, ellipsometry, and modeled by dynamic Monte Carlo simulations. It was found that POPC/POPS bilayers exhibit phase separation in POPC- and POPS-enriched domains as a function of Ca2+ concentration. Annexin A1 interacts with POPC/POPS bilayers by forming irreversibly bound protein domains with monolayer thickness on POPS-enriched nanodomains, while the attachment of proteins to the POPC-enriched regions is fully reversible. A thorough kinetic analysis of the process reveals that both, the binding constant of annexin A1 at …

Models Moleculargenetic structuresLipid BilayersBiophysicsPhospholipidAnalytical chemistryPhosphatidylserines02 engineering and technologyMicroscopy Atomic ForceBiochemistryBiophysical PhenomenaMembrane Lipids03 medical and health scienceschemistry.chemical_compoundProtein structureSFMMonolayerMicropatterned membranesAnimalsHumansPOPCMonte Carlo simulationAnnexin A1030304 developmental biologyFluorescence microscopy0303 health sciencesEllipsometrytechnology industry and agricultureCell BiologyQuartz crystal microbalanceSurface Plasmon Resonance021001 nanoscience & nanotechnologyBinding constantProtein Structure TertiaryMembraneMicroscopy FluorescencechemistryQCMPhosphatidylcholinesBiophysicsCalciumlipids (amino acids peptides and proteins)Adsorption0210 nano-technologyMonte Carlo MethodProtein BindingAnnexin A1Biochimica et Biophysica Acta (BBA) - Biomembranes
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Phospholipid and phospholipid-protein monolayers at the air/water interface.

1990

Molecular StructureAir water interfaceChemistryAirLipid BilayersPhospholipidProteinsWaterchemistry.chemical_compoundChemical engineeringMonolayerPressurePhysical and Theoretical ChemistryPhospholipidsAnnual review of physical chemistry
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Force Measurements on Myelin Basic Protein Adsorbed to Mica and Lipid Bilayer Surfaces Done with the Atomic Force Microscope

1999

The mechanical and adhesion properties of myelin basic protein (MBP) are important for its function, namely the compaction of the myelin sheath. To get more information about these properties we used atomic force microscopy to study tip-sample interaction of mica and mixed dioleoylphosphatidylserine (DOPS) (20%)/egg phosphatidylcholine (EPC) (80%) lipid bilayer surfaces in the absence and presence of bovine MBP. On mica or DOPS/EPC bilayers a short-range repulsive force (decay length 1.0-1.3 nm) was observed during the approach. The presence of MBP always led to an attractive force between tip and sample. When retracting the tip again, force curves on mica and on lipid layers were different…

Persistence lengthbiologyProtein ConformationChemistryBilayerLipid BilayersBiophysicsMyelin Basic ProteinPhosphatidylserinesAdhesionMicroscopy Atomic ForceMyelin basic proteinCrystallographyMicroscopyPhosphatidylcholinesbiology.proteinAnimalsAluminum SilicatesCattleAdsorptionLipid bilayer phase behaviorMicaLipid bilayerResearch ArticleBiophysical Journal
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No Label Required: Protein Binding at Membrane Interfaces Visualized through Colloid Phase Transitions

2004

Phase transitionChemistryBilayerCell MembraneLipid BilayersSurface plasmonAnalytical chemistryMembrane ProteinsPlasma protein bindingLigandsSilicon DioxidePhase TransitionAtomic and Molecular Physics and OpticsKineticsColloidMembraneBiophysicsColloidsPhysical and Theoretical ChemistrySurface plasmon resonanceLipid bilayerProtein BindingChemPhysChem
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Phase Transition of Individually Addressable Microstructured Membranes Visualized by Imaging Ellipsometry

2007

The phase transition of individually addressable microstructured lipid bilayers was investigated by means of imaging ellipsometry. Microstructured bilayers were created on silicon substrates by micromolding in capillaries, and the thermotropic behavior of various saturated diacyl phosphatidylcholine (1,2-dipalmitoyl-sn-glycero-3-phosphocholine, 1,2-dipentadecoyl-sn-glycero-3-phosphocholine, and 1,2-dimyristoyl-sn-glycero-3-phosphocholine (DMPC)) bilayers as well as DMPC/cholesterol membranes was determined by measuring the area expansion and thickness of the bilayer as a function of temperature. We found an increase in the main phase transition temperature T(M) of 2-6 degrees C and a substa…

Phase transitionMaterials scienceBilayerVesicleLipid BilayersTemperatureAnalytical chemistryMicroscopy Atomic ForceThermotropic crystalPhase TransitionSurfaces Coatings and FilmsDiffusionchemistry.chemical_compoundMembranechemistryEllipsometryPhosphatidylcholineMaterials ChemistryPhysical and Theoretical ChemistryLipid bilayerThe Journal of Physical Chemistry B
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Thermal Expansion of Microstructured DMPC Bilayers Quantified by Temperature-Controlled Atomic Force Microscopy

2006

Phase transitionMembrane FluiditySurface PropertiesLipid BilayersBiophysicsAnalytical chemistryPhospholipidMicroscopy Atomic ForcePhase TransitionThermal expansionchemistry.chemical_compoundAdsorptionMembrane fluidityPhysical and Theoretical ChemistryLipid bilayerAtomic force microscopyBilayerTemperatureProteinsLipidsAtomic and Molecular Physics and OpticsModels ChemicalchemistryChemical physicsAdsorptionDimyristoylphosphatidylcholinePeptidesChemPhysChem
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Unusual triskelion patterns and dye-labelled GUVs: consequences of the interaction of cholesterol-containing linear-hyperbranched block copolymers wi…

2015

Cholesterol (Ch) linked to a linear-hyperbranched block copolymer composed of poly(ethylene glycol) (PEG) and poly(glycerol) (hbPG) was investigated for its membrane anchoring properties. Two polyether-based linear-hyperbranched block copolymers with and without a covalently attached rhodamine fluorescence label (Rho) were employed (Ch-PEG30-b-hbPG23 and Ch-PEG30-b-hbPG17-Rho). Compression isotherms of co-spread 1,2-dipalmitoyl-sn-glycero-3-phosphocholine (DPPC) or 1-palmitoyl-2-oleoyl-sn-glycero-3-phosphocholine (POPC) with the respective polymers were measured on the Langmuir trough and the morphology development of the liquid-condensed (LC) domains was studied by epi-fluorescence microsc…

PolymersPolyestersLipid BilayersPolyethylene GlycolsRhodaminechemistry.chemical_compoundMonolayerLactic AcidPOPCPhospholipidsUnilamellar Liposomeschemistry.chemical_classificationAqueous solutionChromatographyRhodaminesVesicletechnology industry and agricultureGeneral ChemistryPolymerCondensed Matter PhysicsGlycerylphosphorylcholineCrystallographyCholesterolMembraneMicroscopy FluorescencechemistryPhosphatidylcholineslipids (amino acids peptides and proteins)Ethylene glycolSoft Matter
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