Search results for "Orientations of Proteins in Membranes database"

showing 4 items of 4 documents

Biological insertion of computationally designed short transmembrane segments

2016

The great majority of helical membrane proteins are inserted co-translationally into the ER membrane through a continuous ribosome-translocon channel. The efficiency of membrane insertion depends on transmembrane (TM) helix amino acid composition, the helix length and the position of the amino acids within the helix. In this work, we conducted a computational analysis of the composition and location of amino acids in transmembrane helices found in membrane proteins of known structure to obtain an extensive set of designed polypeptide segments with naturally occurring amino acid distributions. Then, using an in vitro translation system in the presence of biological membranes, we experimental…

0301 basic medicineModels MolecularBiologyEndoplasmic ReticulumArticleProtein Structure Secondary03 medical and health sciencesOrientations of Proteins in Membranes databaseMembranes (Biologia)Amino Acid SequenceIntegral membrane proteinMultidisciplinary030102 biochemistry & molecular biologyPeripheral membrane proteinCell MembraneProteïnes de membranaComputational BiologyMembrane ProteinsBiological membraneBiofísicaTransmembrane proteinTransmembrane domain030104 developmental biologyBiochemistryMembrane proteinHelixBiophysicsPeptidesScientific Reports
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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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Chemically driven phase separation in black lipid membranes and its coupling to membrane functions

1992

Abstract We analysed the single-channel current fluctuations of gramicidin in bimolecular lipid membranes in order to demonstrate (i) the influence of protein binding to the lateral organisation of a mixed membrane, and (ii) how this couples to the function of the ionophore. Examples of phase separations induced by synthetic polyelectrolytes, as models for peripheral membrane proteins, and specific ligand-receptor interactions are presented and discussed in view of the important lateral order-function relationship in biomembranes.

StereochemistryChemistryPeripheral membrane proteinLipid microdomainMetals and AlloysSynthetic membraneBiological membraneSurfaces and InterfacesPolar membraneSurfaces Coatings and FilmsElectronic Optical and Magnetic MaterialsOrientations of Proteins in Membranes databaseMembraneMaterials ChemistryBiophysicsMembrane biophysicsThin Solid Films
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Binding, Interaction, and Organization of Proteins with Lipid Model Membranes

1991

Model membrane systems are used to investigate protein recognition and binding at interfaces. Fluorescence microscopy results are presented for interactions of the proteins, phospholipase A2 and antifluorescyl IgG, at lipid monolayer interfaces. Total internal reflection fluorescence measurements are used to quantify albumin and IgG adsorption to supported lipid monolayers.

Total internal reflection fluorescence microscopeOrientations of Proteins in Membranes databaseMembraneMembrane proteinChemistryMonolayerBiophysicsFluorescence microscopeBiological membranePlant lipid transfer proteins
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