Search results for "BILAYER"

showing 10 items of 391 documents

The membrane environment modulates self-association of the human GpA TM domain--implications for membrane protein folding and transmembrane signaling.

2010

Abstract The influence of lipid bilayer properties on a defined and sequence-specific transmembrane helix–helix interaction is not well characterized yet. To study the potential impact of changing bilayer properties on a sequence-specific transmembrane helix–helix interaction, we have traced the association of fluorescent-labeled glycophorin A transmembrane peptides by fluorescence spectroscopy in model membranes with varying lipid compositions. The observed changes of the glycophorin A dimerization propensities in different lipid bilayers suggest that the lipid bilayer thickness severely influences the monomer–dimer equilibrium of this transmembrane domain, and dimerization was most effici…

Protein FoldingLipid BilayersMolecular Sequence DataBiophysicsGpABiochemistryFluorescenceMembrane LipidsOrientations of Proteins in Membranes databaseMembrane fluidityFluorescence Resonance Energy TransferHumansAmino Acid SequenceGlycophorinsBilayerLipid bilayerIntegral membrane proteinBinding SitesChemistryBilayerPeripheral membrane proteinTemperatureMembrane ProteinsCell BiologyTransmembrane proteinCell biologyTransmembrane domainCholesterolSpectrometry FluorescenceFRETPhosphatidylcholineslipids (amino acids peptides and proteins)Transmembrane helix–helix interactionProtein MultimerizationPeptidesHydrophobic and Hydrophilic InteractionsSignal TransductionBiochimica et biophysica acta
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Linked Analysis of Large Cooperative, Allosteric Systems: The Case of the Giant HBL Hemoglobins

2008

Homotropic and heterotropic allosteric interactions are important mechanisms that regulate protein function. These mechanisms depend on the ability of oligomeric protein complexes to adopt different conformations and to transmit conformation-linked signals from one subunit of the complex to the neighboring ones. An important step in understanding the regulation of protein function is to identify and characterize the conformations available to the protein complex. This task becomes increasingly challenging with increasing numbers of interacting binding sites. However, a large number of interacting binding sites allows for high homotropic interactions (cooperativity) and thus represents the m…

Protein functionOrder (biology)BiochemistryHexagonal crystal systemBilayerProtein subunitAllosteric regulationBiophysicsCooperativityBiologyBinding site
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Generation of proteoliposomes from subcellular fractions.

1998

Intracellular membranes are highly dynamic, yet they retain their identity and functional characteristics. Integral membrane proteins, which must confer this specific membrane identity, remain poorly characterized at the biochemical level, largely because detergent-mediated solubilization is required for purification and analysis, and several properties of integral membrane proteins can only be investigated when the molecule is properly embedded in a lipid bilayer. We present a method for the efficient reconstitution into proteoliposomes of integral membrane proteins from subcellular fractions. Integral membrane proteins were identified on high-resolution two-dimensional gels after selectiv…

ProteolipidsClinical BiochemistryPeripheral membrane proteinMembrane ProteinsBiological membraneIntracellular MembranesBiologyBiochemistryTransmembrane proteinAnalytical ChemistryCell LineMembrane proteinBiochemistryCricetinaeLiposomesMembrane fluidityAnimalsProtein–lipid interactionLipid bilayerIntegral membrane proteinSubcellular FractionsElectrophoresis
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Exchange coupling in an electrodeposited magnetic bilayer of Prussian blue analogues

2015

Bilayers of Prussian blue analogues (PBA) constituted of hard and soft magnets have been fabricated by means of electrochemical deposition. This method affords a good contact between two PBA thin films of nanometer thickness. Complete characterization of the resulting system has been performed, which has allowed the determination of the preservation of the chemical identity of both materials during the electrodeposition and the establishment of a clear interface between them. The magnetic behavior of the bilayer can be explained in terms of an exchange-spring magnet.

Prussian blueMaterials scienceBilayerNanotechnologyGeneral ChemistryElectrochemistryCharacterization (materials science)chemistry.chemical_compoundchemistryChemical engineeringMagnetMaterials ChemistryNanometreThin filmDeposition (law)Journal of Materials Chemistry C
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Factors affecting the amount and the mode of merocyanine 540 binding to the membrane of human erythrocytes. A comparison with the binding to leukemia…

1995

Abstract In the presence of albumin Merocyanine 540 (MC540) exhibits a very limited binding to the outer surface of the membrane of normal erythrocytes, whereas pronounced binding is observed to leukemia cells. To find out whether this difference is due to differences in the composition or structural organization of the cell membrane we analyzed effects of a number of covalent and non-covalent perturbations of the red cell membrane on the binding and fluorescence characteristics of membrane-bound MC540. It is shown that exposure of the cells to cationic chlorpromazine, neuraminidase or photodynamic treatment with AlPcS 4 as sensitizer caused a limited increase (30–50%) of MC540 binding, tog…

Radiation-Sensitizing AgentsTMA-DPHHot TemperatureIndolesBSALightChlorpromazineLipid BilayersBiophysicsPhospholipidNeuraminidaseQuantum yieldPyrimidinonesBiochemistryCell membranechemistry.chemical_compoundt-BuOOHOrganometallic CompoundsTumor Cells CulturedmedicineMerocyanine 540HumansPBSCell MembraneErythrocyte MembraneMembrane structureCell Biologymedicine.diseasePEGFluorescenceDIDSLeukemiaLeukemia cellAlPcS4CholesterolSpectrometry FluorescenceMembranemedicine.anatomical_structureBNML cellsBiochemistrychemistryLeukemia MyeloidCovalent bondBiophysicsMC540Biochimica et Biophysica Acta (BBA) - Biomembranes
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Vesicle transport and photoreceptor death: fishing for molecular links.

2013

Intracellular vesicle transport defects can induce retinal degeneration and photoreceptor cell death, but the molecular connections between these processes remains poorly understood. Reporting in Developmental Cell, Nishiwaki et al. (2013) suggest that a vesicle fusion cis-SNARE complex component translates vesicular transport defects into photoreceptor cell apoptosis.

Retinal degenerationVesicle fusionLipid bilayer fusionIntracellular vesicleApoptosisCell BiologyBiologymedicine.diseaseMembrane FusionGeneral Biochemistry Genetics and Molecular BiologyPhotoreceptor cellCell biologyVesicular transport proteinSoluble N-Ethylmaleimide-Sensitive Factor Attachment Proteinsmedicine.anatomical_structureProto-Oncogene Proteins c-bcl-2ApoptosismedicineRetinal Cone Photoreceptor CellsAnimalsMolecular BiologyDevelopmental BiologyDevelopmental cell
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Poly(sarcosine) surface modification imparts stealth-like properties to liposomes

2019

Circulation lifetime is a crucial parameter for a successful therapy with nanoparticles. Reduction and alteration of opsonization profiles by surface modification of nanoparticles is the main strategy to achieve this objective. In clinical settings, PEGylation is the most relevant strategy to enhance blood circulation, yet it has drawbacks, including hypersensitivity reactions in some patients treated with PEGylated nanoparticles, which fuel the search for alternative strategies. In this work, lipopolysarcosine derivatives (BA-pSar, bisalkyl polysarcosine) with precise chain lengths and low polydispersity indices are synthesized, characterized, and incorporated into the bilayer of preformed…

SarcosineSurface PropertiesProton Magnetic Resonance SpectroscopyDispersityStatic ElectricityNanoparticle02 engineering and technology010402 general chemistry01 natural sciencesBiomaterialsAnimals Genetically Modifiedchemistry.chemical_compoundAnimalsGeneral Materials ScienceSurface chargeComplement ActivationZebrafishLiposomeChemistryBilayerSarcosineGeneral Chemistry021001 nanoscience & nanotechnology0104 chemical sciencesMolecular WeightLiposomesBiophysicsPEGylationSurface modification0210 nano-technologyPeptidesBiotechnology
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Specific binding of VegT mRNA localization signal to membranes in Xenopus oocytes

2021

Abstract We have studied the interaction of a VegT mRNA localization signal sequence with the membranes of the mitochondrial cloud in Xenopus oocytes, and the binding of the VegT mRNA signal sequence to the lipid raft regions of the vesicles bounded by ordered and disordered phospholipid bilayers. RNA preference for the membranes of the mitochondrial cloud was confirmed using microscopy of a fluorescence resonance energy transfer from RNA molecules to membranes. Our studies show that VegT mRNA has a higher affinity for ordered regions of lipid bilayers. This conclusion is supported by the dissociation constant measurements for RNA-liposome complex and the visualization of the FRET signal be…

Signal peptideXenopusLipid vesiclesMitochondrial cloudProtein Sorting SignalsXenopus ProteinsXenopus laevis03 medical and health sciencesMembrane MicrodomainsRafts0302 clinical medicineFluorescence Resonance Energy TransferAnimalsLipid bilayerMolecular BiologyLipid raftXenopus oocytes030304 developmental biology0303 health sciencesMessenger RNABinding SitesbiologyChemistryVegT mRNARNACell BiologyMembrane RNAbiology.organism_classificationFörster resonance energy transferLiposomesOocytesFRETBiophysicsFemaleT-Box Domain Proteins030217 neurology & neurosurgeryBiochimica et Biophysica Acta (BBA) - Molecular Cell Research
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Efficient DNA Packaging of Bacteriophage PRD1 Requires the Unique Vertex Protein P6

2007

ABSTRACT The assembly of bacteriophage PRD1 proceeds via formation of empty procapsids containing an internal lipid membrane, into which the linear double-stranded DNA genome is subsequently packaged. The packaging ATPase P9 and other putative packaging proteins have been shown to be located at a unique vertex of the PRD1 capsid. Here, we describe the isolation and characterization of a suppressor-sensitive PRD1 mutant deficient in the unique vertex protein P6. Protein P6 was found to be an essential part of the PRD1 packaging machinery; its absence leads to greatly reduced packaging efficiency. Lack of P6 was not found to affect particle assembly, because in the P6-deficient mutant infecti…

Specificity factorImmunologyMutantBiologymedicine.disease_causeMicrobiologyBacteriophageViral Proteins03 medical and health scienceschemistry.chemical_compoundVirologyDNA PackagingmedicineBacteriophage PRD1Lipid bilayer030304 developmental biology0303 health sciencesMutationStructure and AssemblyVirus Assembly030302 biochemistry & molecular biologyVirionTectivirusSalmonella entericabiology.organism_classificationMolecular biologychemistryCapsidInsect ScienceMutationBiophysicsDNAJournal of Virology
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Alpha-toxin of Staphylococcus aureus

1991

Alpha-toxin, the major cytotoxic agent elaborated by Staphylococcus aureus, was the first bacterial exotoxin to be identified as a pore former. The protein is secreted as a single-chain, water-soluble molecule of Mr 33,000. At low concentrations (less than 100 nM), the toxin binds to as yet unidentified, high-affinity acceptor sites that have been detected on a variety of cells including rabbit erythrocytes, human platelets, monocytes and endothelial cells. At high concentrations, the toxin additionally binds via nonspecific absorption to lipid bilayers; it can thus damage both cells lacking significant numbers of the acceptor and protein-free artificial lipid bilayers. Membrane damage occu…

Staphylococcus aureusCell Membrane PermeabilityToxinBacterial ToxinsCell MembraneBiologymedicine.disease_causeHemolysin ProteinsApplied Microbiology and BiotechnologyTransmembrane proteinExocytosisCell membraneHemolysin ProteinsStructure-Activity Relationshipmedicine.anatomical_structureBiochemistrymedicineBiophysicsAnimalsHumansLipid bilayerStaphylococcus aureus alpha toxinExotoxinResearch ArticleMicrobiological Reviews
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