Search results for "Lipid Bilayers"

showing 5 items of 135 documents

The dynamic orientation of membrane-bound peptides: bridging simulations and experiments.

2007

AbstractThe structural organization in a peptide/membrane supramolecular complex is best described by knowledge of the peptide orientation plus its time-dependent and spatial fluctuations. The static orientation, defined by the peptide tilt and a rotation about its molecular axis, is accessible through a number of spectroscopic methods. However, peptide dynamics, although relevant to understand the functionality of these systems, remains largely unexplored. Here, we describe the orientation and dynamics of Trp-flanked and Lys-flanked hydrophobic peptides in a lipid bilayer from molecular dynamics simulations. A novel view is revealed, where collective nontrivial distributions of time-evolvi…

chemistry.chemical_classificationModels MolecularMembranesProtein ConformationLipid BilayersBiophysicsSupramolecular chemistryAnchoringMembrane ProteinsPeptideOrientation (graph theory)CrystallographyMolecular dynamicsMembraneProtein structurechemistryModels ChemicalChemical physicsComputer SimulationLipid bilayerDimyristoylphosphatidylcholinePeptidesBiophysical journal
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Self-Assembling of Peptide/Membrane Complexes by Atomistic Molecular Dynamics Simulations

2007

Abstract Model biological membranes consisting of peptide/lipid-bilayer complexes can nowadays be studied by classical molecular dynamics (MD) simulations at atomic detail. In most cases, the simulation starts with an assumed state of a peptide in a preformed bilayer, from which equilibrium configurations are difficult to obtain due to a relatively slow molecular diffusion. As an alternative, we propose an extension of reported work on the self-organization of unordered lipids into bilayers, consisting of including a peptide molecule in the initial random configuration to obtain a membrane-bound peptide simultaneous to the formation of the lipid bilayer. This strategy takes advantage of the…

chemistry.chemical_classificationModels MolecularMolecular diffusionMembranesChemistryMacromolecular SubstancesMembrane FluidityBilayerLipid BilayersMolecular ConformationBiophysicsPeptideBiological membraneTransmembrane proteinMolecular dynamicsCrystallographyMembraneModels ChemicalQuantum TheoryComputer SimulationLipid bilayerPeptidesPhospholipidsBiophysical Journal
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Studies on the interaction of C1q,a subcomponent of the first component of complement, with porins fromSalmonella minnesotaincorporated into artifici…

1990

AbstractPurified outer membrane proteins (OMP) of Salmonella minnesota, Re-form, were incorporated into liposomes. These induced in macrophages a chemiluminescence signal identical to that of the intact Re-form. This signal was abolished by preincubation of porin-containing liposomes with purified C1q. Incorporation of isolated OMP into black lipid membranes (BLM) resulted in channel-formation which could not be inhibited by isolated C1q. Additionally, incubation of OMP-containing liposomes with BLM resulted in pore-formation within the BLM. This was amplified when lipid A was present within the liposomes. Preincubation of OMP-containing liposomes with purified C1q abolished pore-formation …

congenital hereditary and neonatal diseases and abnormalitiesLuminescenceMacrophageLipid BilayersBiophysicsSynthetic membranePorinschemical and pharmacologic phenomenaBiochemistryIon ChannelsMembrane PotentialsLipid AMiceSalmonellaStructural BiologyGeneticsAnimalsHumansBlack lipid membraneLipid bilayerMolecular BiologyC1qCells CulturedMice Inbred BALB CLiposomeurogenital systemChemistryComplement C1qMacrophagesElectric Conductivitynutritional and metabolic diseasesMembranes ArtificialCell BiologyLiposomeKineticsCholesterolMembraneMembrane proteinBiochemistryOuter membrane proteinPorinPhosphatidylcholinesbacteriaBacterial outer membraneBacterial Outer Membrane ProteinsFEBS Letters
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Lipid Binding Controls Dimerization of the Coat Protein p24 Transmembrane Helix

2019

Abstract Coat protein (COP) I and COP II complexes are involved in the transport of proteins between the endoplasmic reticulum and the Golgi apparatus in eukaryotic cells. The formation of COP I/II complexes at membrane surfaces is an early step in vesicle formation and is mastered by p24, a type I transmembrane protein. Oligomerization of p24 monomers was suggested to be mediated and/or stabilized via interactions within the transmembrane domain, and the p24 transmembrane helix appears to selectively bind a single sphingomyelin C18:0 molecule. Furthermore, a potential cholesterol-binding sequence has also been predicted in the p24 transmembrane domain. Thus, sphingomyelin and/or cholestero…

virusesLipid BilayersBiophysicsProtein Structure Secondary03 medical and health sciencessymbols.namesake0302 clinical medicineimmune system diseasesAmino Acid Sequence030304 developmental biology0303 health sciencesChemistryEndoplasmic reticulumVesicleCholesterol bindingvirus diseasesArticlesCOPIGolgi apparatusLipidsTransmembrane proteinSphingomyelinsTransmembrane domainCholesterolsymbolsBiophysicsCapsid Proteinslipids (amino acids peptides and proteins)SphingomyelinDimerization030217 neurology & neurosurgeryBiophysical Journal
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An experimental model for mimicking biological systems: the Belousov-Zhabotinsky reaction in Lipid membranes

2006

{LIPID} {BILAYERS}Belousov-Zhabotinsky reaction; Biomimetic systems; Cell membranes; Lipid bilayers; Morphogenesis; Self-organizing systemsEcologyLipid bilayersChemistryExperimental modelBelousov-Zhabotinsky reaction{BELOUSOV-ZHABOTINSKY} {REACTION}; Biomimetic systems; Cell membranes; {LIPID} {BILAYERS}; morphogenesis; Self-organizing systemsSelf-organizing systemsBiomimetic systemsCell membranesMembraneBelousov–Zhabotinsky reactionBiophysicsMorphogenesis{BELOUSOV-ZHABOTINSKY} {REACTION}Lipid bilayerEcology Evolution Behavior and Systematics
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