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Bacterial Outer Membrane ProteinsCell MembraneTransferrin-Binding Protein AMembrane ProteinsEscherichia coli ProteinsEscherichia coliProtein Structure, TertiaryIntracellular MembranesMembranesPorinsMembrane LipidsMolecular Sequence DataMembrane PotentialsBacterial ProteinsMembranes, ArtificialAmino Acid SequenceErythrocyte MembraneMembrane Transport ProteinsCell Membrane PermeabilityMembrane FluidityElectrophoresis, Polyacrylamide GelMolecular WeightProtein TransportLipid BilayersDetergentsMitochondrial MembranesMutationBase SequenceAntibodies, BacterialBasement MembraneProtein BindingAntigens, BacterialCarrier ProteinsMicroscopy, ElectronCloning, MolecularMembrane GlycoproteinsGenes, BacterialCell LineRecombinant Fusion ProteinsProtein Structure, SecondaryCell FractionationNeisseria meningitidisProtein ConformationSequence Homology, Amino AcidModels, MolecularModels, BiologicalEndoplasmic ReticulumPeriplasmProtein Sorting SignalsLiposomesSolubilityChlamydia trachomatisMitochondriaPlasmidsRecombinant ProteinsGolgi ApparatusImmunoblottingRabbitsHaemophilus influenzaeBlotting, WesternNeisseria gonorrhoeaeGene Expression Regulation, BacterialBacterial VaccinesTemperatureMicroscopy, FluorescenceBinding SitesMicroscopy, ImmunoelectronKineticsCells, CulturedMitochondrial Membrane Transport ProteinsHydrogen-Ion ConcentrationAntibodies, MonoclonalBiological TransportViral Matrix ProteinsSubcellular FractionsSynaptic MembranesEpitopesCytoplasmSequence AlignmentFreeze FracturingPeptidesCalciumDNA, BacterialLipopolysaccharidesFluorescent Antibody TechniqueProtein FoldingReceptors, Cell SurfaceSaccharomyces cerevisiae ProteinsIon ChannelsPseudomonas aeruginosaLipoproteinsChlamydophila psittaciCattleBiological Transport, ActivePeriplasmic ProteinsSpecies SpecificityMicellesBacterial AdhesionProtein Processing, Post-TranslationalPhosphatidylcholines
Lipid bilayerAnalysesInteractionsGenesPurificationRole
Lipid bilayer3
  • Peripheral membrane proteins are temporarily attached either to the lipid bilayer or to integral proteins by a combination of hydrophobic, electrostatic, and other non-covalent interactions. (wikipedia.org)
  • citation needed] Integral and peripheral proteins may be post-translationally modified, with added fatty acid, diacylglycerol or prenyl chains, or GPI (glycosylphosphatidylinositol), which may be anchored in the lipid bilayer. (wikipedia.org)
  • These proteins are water-soluble but can aggregate and associate irreversibly with the lipid bilayer and become reversibly or irreversibly membrane-associated. (wikipedia.org)
Analyses1
  • For example, proteins involved in immune response The localization of proteins in membranes can be predicted reliably using hydrophobicity analyses of protein sequences, i.e. the localization of hydrophobic amino acid sequences. (wikipedia.org)
Interactions2
  • The combination of such self-organizational phenomena with canonical intermolecular interactions is most likely to control the release of membrane proteins from the ER into the secretory pathway. (biologists.com)
  • This process depends on the general physico-chemical features of the cargo membrane protein and on the interactions of these features with the collective properties of the bilayer, instead of the one-to-one intermolecular interactions that exist between discrete signals and their receptors. (biologists.com)
Genes1
Purification1
  • Although membrane proteins play an important role in all organisms, their purification has historically, and continues to be, a huge challenge for protein scientists. (wikipedia.org)
Role1
  • In this Commentary, I review evidence in favor of the idea that partitioning of TMDs into bilayer domains that are endowed with distinct physico-chemical properties plays a pivotal role in the transport of membrane proteins within the early secretory pathway. (biologists.com)