Search results for "layer"

showing 10 items of 2667 documents

Solid state NMR analysis of peptides in membranes: Influence of dynamics and labeling scheme.

2010

The functional state of a membrane-active peptide is often defined by its conformation, molecular orientation, and its oligomeric state in the lipid bilayer. These "static" structural properties can be routinely studied by solid state NMR using isotope-labeled peptides. In the highly dynamic environment of a liquid crystalline biomembrane, however, the whole-body fluctuations of a peptide are also of paramount importance, although difficult to address and most often ignored. Yet it turns out that disregarding such motional averaging in calculating the molecular alignment from orientational NMR-constraints may give a misleading, if not false picture of the system. Here, we demonstrate that t…

Models MolecularLipid BilayersBiophysicsPeptideWhole body fluctuationBiochemistryProtein Structure SecondaryOrientation (geometry)Side chainLipid bilayerNuclear Magnetic Resonance BiomolecularNMR tensor orientationchemistry.chemical_classificationChemistrySolid-state 2H- 19F- 15N-NMRPeptide orientationMembrane ProteinsBiological membraneCell BiologyGALAMembrane-bound peptidePISEMACrystallographyMembraneSolid-state nuclear magnetic resonanceChemical physicsIsotope LabelingHelixIsotope labeling schemeα-helicesPeptide dynamicPeptidesBiochimica et biophysica acta
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Modulation of lipid-induced ER stress by fatty acid shape.

2011

IF : 5,709; International audience; Exposure of pancreatic β cells to long-chain saturated fatty acids (SFA) induces a so-called endoplasmic reticulum (ER) stress that can ultimately lead to cell death. This process is believed to participate in insulin deficiency associated with type 2 diabetes, via a decrease in β-cell mass. By contrast, some unsaturated fatty acid species appear less toxic to the cells and can even alleviate SFA-induced ER stress. In the present study, we took advantage of a simple yeast-based model, which brings together most of the trademarks of lipotoxicity in human cells, to screen fatty acids of various structures for their capacity to counter ER stress. Here we dem…

Models MolecularLipid Bilayers[SDV.BC.BC]Life Sciences [q-bio]/Cellular Biology/Subcellular Processes [q-bio.SC]Endoplasmic ReticulumBiochemistry03 medical and health sciences0302 clinical medicine[ SDV.BBM.BC ] Life Sciences [q-bio]/Biochemistry Molecular Biology/Biomolecules [q-bio.BM]Structural BiologyStress PhysiologicalGeneticsHumansadipocyte protein 2[SDV.BBM.BC]Life Sciences [q-bio]/Biochemistry Molecular Biology/Biochemistry [q-bio.BM]Molecular BiologyUnsaturated fatty acidCells CulturedPhospholipids030304 developmental biologychemistry.chemical_classification0303 health sciencesbiologyEndoplasmic reticulumFatty Acids[ SDV.BC.BC ] Life Sciences [q-bio]/Cellular Biology/Subcellular Processes [q-bio.SC]food and beveragesFatty acidCell BiologyLipidsCell biologychemistryLipotoxicityFree fatty acid receptorUnfolded protein responsebiology.proteinFatty Acids Unsaturated030217 neurology & neurosurgeryPolyunsaturated fatty acid
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Influence of Whole-Body Dynamics on 15N PISEMA NMR Spectra of Membrane Proteins: A Theoretical Analysis

2009

AbstractMembrane proteins and peptides exhibit a preferred orientation in the lipid bilayer while fluctuating in an anisotropic manner. Both the orientation and the dynamics have direct functional implications, but motions are usually not accessible, and structural descriptions are generally static. Using simulated data, we analyze systematically the impact of whole-body motions on the peptide orientations calculated from two-dimensional polarization inversion spin exchange at the magic angle (PISEMA) NMR. Fluctuations are found to have a significant effect on the observed spectra. Nevertheless, wheel-like patterns are still preserved, and it is possible to determine the average peptide til…

Models MolecularMagic angleRotationGaussianLipid BilayersNormal DistributionBiophysicsMolecular physicsProtein Structure SecondarySpectral lineQuantitative Biology::Subcellular ProcessesMolecular dynamicssymbols.namesakeNuclear magnetic resonanceOrientationComputer SimulationLipid bilayerAnisotropyNuclear Magnetic Resonance BiomolecularQuantitative Biology::BiomoleculesChemistryMembranePolarization (waves)AmplitudesymbolsDimyristoylphosphatidylcholinePeptidesBiophysical Journal
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The synthesis, structure and properties of N-acetylated derivatives of ethyl 3-amino-1H-pyrazole-4-carboxylate.

2007

Ethyl 3-amino-1H-pyrazole-4-carboxylate (1) was yielded through total synthesis and reacted with acetic anhydride to give the acetylated products 2-6. Compounds 1-6 were studied with HPLC, X-ray, FT-IR, (1)H-NMR, (13)C-NMR and MS. Acetylation was carried out in solvents of various polarity, namely; chloroform; dioxane; DMF; acetic anhydride, at room temperature and at boiling points; and in the presence and absence of DMAP. The acetylated products are mainly nitrogen atoms in the ring. The position of the ring proton in the solution was based on NOESY; multinuclear HMBC, HSQC spectra and calculations. For equivalent amounts (1-1.5 mol) of acetic anhydride at room temperature two products of…

Models MolecularMagnetic Resonance Spectroscopy13C-NMR spectraAcetic AnhydridesRing (chemistry)Crystallography X-RayCatalysisCatalysischemistry.chemical_compoundDrug DiscoverySpectroscopy Fourier Transform InfraredOrganic chemistry4-AminopyridineFT-IR spectraChromatography High Pressure Liquidhetareneamino acidChloroformTemperatureTotal synthesisAcetylationGeneral ChemistryGeneral MedicineNuclear magnetic resonance spectroscopyhydrogen bondingSolventAcetic anhydridechemistry1H-NMR spectraDimethylformamidePyrazolesIndicators and ReagentsChromatography Thin LayerChemicalpharmaceutical bulletin
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New antitumoral acetogenin ‘Guanacone type’ derivatives: Isolation and bioactivity. Molecular dynamics simulation of diacetyl-guanacone

2007

We describe herein the isolation and semisynthesis of four acetogenin derivatives (1-4) as well as their ability to inhibit the mitochondrial respiratory chain and several tumor cell lines. In addition, four nanoseconds (ns) of MD simulation of compound 4, in a fully hydrated POPC bilayer, is reported.

Models MolecularMagnetic Resonance SpectroscopyAcetogeninsStereochemistryLipid BilayersClinical BiochemistryMolecular ConformationRespiratory chainPharmaceutical ScienceBiochemistryChemical synthesisAnnonaElectron TransportLactoneschemistry.chemical_compoundPolyketideCell Line TumorDrug DiscoveryHumansComputer SimulationFuransMolecular BiologyPOPCBilayerOrganic ChemistryHydrogen BondingAntineoplastic Agents PhytogenicSemisynthesisMitochondrial respiratory chainchemistrySeedsAcetogeninPhosphatidylcholinesMolecular MedicineIndicators and ReagentsFatty AlcoholsBioorganic & Medicinal Chemistry
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Orientational landscapes of peptides in membranes: prediction of (2)H NMR couplings in a dynamic context.

2009

Unlike soluble proteins, membrane polypeptides face an anisotropic milieu. This imposes restraints on their orientation and provides a reference that makes structure prediction tractable by minimalistic thermodynamic models. Here we use this framework to build orientational distributions of monomeric membrane-bound peptides and to predict their expected solid-state (2)H NMR quadrupolar couplings when labeled at specific side chain positions. Using a complete rigid-body sampling of configurations relative to an implicit lipid membrane, peptide free energy landscapes are calculated. This allows us to obtain probability distributions of the peptide tilt, azimuthal rotation, and depth of membra…

Models MolecularMagnetic Resonance SpectroscopyMembrane FluidityPopulationDegrees of freedom (physics and chemistry)Context (language use)BiochemistryQuantitative Biology::Subcellular ProcessesComputational chemistryOrientation (geometry)Computer SimulationLipid bilayereducationAnisotropyPhysics::Biological PhysicsQuantitative Biology::Biomoleculeseducation.field_of_studyChemistryCell MembraneMaxima and minimaMembraneSolubilityChemical physicsThermodynamicsPeptidesAlgorithmsBiochemistry
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Mechanical Properties of Pore-Spanning Lipid Bilayers Probed by Atomic Force Microscopy

2006

AbstractWe measure the elastic response of a free-standing lipid membrane to a local indentation by using an atomic force microscope. Starting point is a planar gold-coated alumina substrate with a chemisorbed 3-mercaptopropionic acid monolayer displaying circular pores of very well defined and tunable size, over which bilayers composed of N,N,-dimethyl-N,N,-dioctadecylammonium bromide or 1,2-dioleoyl-3-trimethylammonium-propane chloride were spread. Centrally indenting these “nanodrums” with an atomic force microscope tip yields force-indentation curves, which we quantitatively analyze by solving the corresponding shape equations of continuum curvature elasticity. Since the measured respon…

Models MolecularMaterials scienceMembrane FluidityLipid BilayersBiophysicsAnalytical chemistryFOS: Physical sciencesMechanicsMicroscopy Atomic ForceCurvatureIndentation hardnessHardnessIndentationMonolayerComputer SimulationHardness TestsParticle SizeComposite materialElasticity (economics)Lipid bilayerPhysics::Biological PhysicsMembranesFlexural modulus20399 Classical Physics not elsewhere classifiedElasticityMembraneModels ChemicalStress MechanicalPorosityBiophysical Journal
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Field theoretic study of bilayer membrane fusion: I. Hemifusion mechanism

2003

Self-consistent field theory is used to determine structural and energetic properties of metastable intermediates and unstable transition states involved in the standard stalk mechanism of bilayer membrane fusion. A microscopic model of flexible amphiphilic chains dissolved in hydrophilic solvent is employed to describe these self-assembled structures. We find that the barrier to formation of the initial stalk is much smaller than previously estimated by phenomenological theories. Therefore its creation it is not the rate limiting process. The barrier which is relevant is associated with the rather limited radial expansion of the stalk into a hemifusion diaphragm. It is strongly affected by…

Models MolecularMembrane FluidityLipid BilayersStatic ElectricityBiophysicsFOS: Physical sciencesCondensed Matter - Soft Condensed Matter010402 general chemistryCurvatureQuantitative Biology - Quantitative MethodsMembrane Fusion01 natural sciencesQuantitative Biology::Subcellular Processes03 medical and health sciencesElectromagnetic FieldsMetastabilityPhase (matter)Computer SimulationLipid bilayerQuantitative Methods (q-bio.QM)030304 developmental biology0303 health sciencesFusionMembranesChemistryBilayerLipid bilayer fusionMembranes Artificial0104 chemical sciencesCrystallographyMembraneModels ChemicalChemical physicsFOS: Biological sciencesSoft Condensed Matter (cond-mat.soft)Porosity
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Pore Formation by a Bax-Derived Peptide: Effect on the Line Tension of the Membrane Probed by AFM

2007

AbstractBax is a critical regulator of physiological cell death that increases the permeability of the outer mitochondrial membrane and facilitates the release of the so-called apoptotic factors during apoptosis. The molecular mechanism of action is unknown, but it probably involves the formation of partially lipidic pores induced by Bax. To investigate the interaction of Bax with lipid membranes and the physical changes underlying the formation of Bax pores, we used an active peptide derived from helix 5 of this protein (Bax-α5) that is able to induce Bax-like pores in lipid bilayers. We report the decrease of line tension due to peptide binding both at the domain interface in phase-separa…

Models MolecularMembrane FluidityProtein ConformationLipid BilayersBiophysicsPeptide bindingPeptideMicroscopy Atomic ForceProtein structureBcl-2-associated X proteinMembrane fluiditySurface TensionComputer SimulationLipid bilayerbcl-2-Associated X Proteinchemistry.chemical_classificationLiposomeMembranesbiologyChemistryCell biologyMembraneModels ChemicalLiposomesbiology.proteinPorosityBiophysical Journal
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Metalloporphyrin intercalation in liposome membranes: ESR study

2010

Liposomes characterized by membranes featuring diverse fluidity (liquid-crystalline and/or gel phase), prepared from egg yolk lecithin (EYL) and dipalmitoylphosphatidylcholine (DPPC), were doped with selected metalloporphyrins and the time-related structural and dynamic changes within the lipid double layer were investigated. Porphyrin complexes of Mg(II), Mn(III), Fe(III), Co(II), Ni(II), Cu(II), Zn(II), and the metal-free base were embedded into the particular liposome systems and tested for 350 h at 24°C using the electron spin resonance (ESR) spin probe technique. 5-DOXYL, 12-DOXYL, and 16-DOXYL stearic acid methyl ester spin labels were applied to explore the interior of the lipid bila…

Models MolecularOriginal PaperLiposomeMolecular StructureMetalloporphyrinsIntercalation (chemistry)Electron Spin Resonance SpectroscopyPorphyrinBiochemistryLipid bilayerSpin probeInorganic Chemistrychemistry.chemical_compoundCrystallographyMembranechemistryElectron spin resonanceDipalmitoylphosphatidylcholineLiposomesDensity functional theory calculationsOrganic chemistrylipids (amino acids peptides and proteins)Lipid bilayer phase behaviorLipid bilayerJBIC Journal of Biological Inorganic Chemistry
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