Search results for "Biological membrane"

showing 10 items of 98 documents

Ultrafast structural changes within a photosynthetic reaction centre

2021

Nature <London> / Physical science 589, 310 - 314 (2021). doi:10.1038/s41586-020-3000-7

0301 basic medicinePhotosynthetic reaction centreChlorophyllModels MolecularklorofylliCytoplasmUbiquinonePhotosynthetic Reaction Center Complex ProteinsElectrons02 engineering and technologyPhotochemistrymedicine.disease_cause530yhteyttäminenbakteeritElectron Transport03 medical and health sciencesElectron transfermedicineMoleculeddc:530BacteriochlorophyllsbioenergetiikkaComputingMilieux_MISCELLANEOUSHyphomicrobiaceaeMultidisciplinaryBinding SitesCrystallography[SDV.BBM.BS]Life Sciences [q-bio]/Biochemistry Molecular Biology/Structural Biology [q-bio.BM]ChemistryBlastochloris viridisLaserskalvot (biologia)PheophytinsBiological membraneVitamin K 2021001 nanoscience & nanotechnologyAcceptor030104 developmental biologyPicosecondFemtosecondsense organsProtons0210 nano-technologyOxidation-Reductionröntgenkristallografia
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The C-terminal Domains of Apoptotic BH3-only Proteins Mediate Their Insertion into Distinct Biological Membranes

2016

Changes in the equilibrium of pro- and anti-apoptotic members of the B-cell lymphoma-2 (Bcl-2) protein family in the mitochondrial outer membrane (MOM) induce structural changes that commit cells to apoptosis. Bcl-2 homology-3 (BH3)-only proteins participate in this process by either activating pro-apoptotic effectors or inhibiting anti-apoptotic components and by promoting MOM permeabilization. The association of BH3-only proteins with MOMs is necessary for the activation and amplification of death signals; however, the nature of this association remains controversial, as these proteins lack a canonical transmembrane sequence. Here we used an in vitro expression system to study the inserti…

0301 basic medicineProtein familyCèl·lulesBiologyBiochemistryMitochondrial Proteins03 medical and health sciencesProtein DomainsMembranes (Biologia)Protein-fragment complementation assayMembrane BiologyMicrosomesProto-Oncogene ProteinsHumansMolecular BiologyAdaptor Proteins Signal TransducingGeneticsBcl-2-Like Protein 11030102 biochemistry & molecular biologyCell MembraneBcl-2 familyProteïnes de membranaMembrane ProteinsBiological membraneCell BiologyFusion proteinTransmembrane proteinCell biology030104 developmental biologyMembraneProto-Oncogene Proteins c-bcl-2Membrane proteinB-cell lymphoma 2 (Bcl-2) family BH3-only apoptosis membrane insertion membrane protein mitochondrial apoptosis transmembrane domainApoptosis Regulatory ProteinsHydrophobic and Hydrophilic InteractionsHeLa CellsJournal of Biological Chemistry
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Dynamic compartmentalization of calcium channel signalling in neurons.

2020

Calcium fluxes through the neuronal membrane are strictly limited in time due to biophysical properties of voltage-gated and ligand-activated ion channels and receptors. Being embedded into the crowded dynamic environment of biological membranes, Ca2+-permeable receptors and channels undergo perpetual spatial rearrangement, which enables their temporary association and formation of transient signalling complexes. Thus, efficient calcium-mediated signal transduction requires mechanisms to support very precise spatiotemporal alignment of the calcium source and Ca2+-binding lipids and proteins in a highly dynamic environment. The mobility of calcium channels and calcium-sensing proteins themse…

0301 basic medicinechemistry.chemical_elementCalcium03 medical and health sciencesCellular and Molecular Neuroscience0302 clinical medicineCalcium fluxAnimalsHumansCalcium SignalingIon channelCalcium signalingPharmacologyNeuronsLateral mobility ; Voltage-gated calcium channels ; Nanodomain ; Calcium signalling ; STIM/OraiNeuronal PlasticityVoltage-dependent calcium channelEndoplasmic reticulumCalcium channelCell MembraneBiological membraneDendrites030104 developmental biologychemistryBiophysicsCalcium Channels030217 neurology & neurosurgeryNeuropharmacology
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2021

The hydrophobic tails of aliphatic primary alcohols do insert into the hydrophobic core of a lipid bilayer. Thereby, they disrupt hydrophobic interactions between the lipid molecules, resulting in a decreased lipid order, i.e., an increased membrane fluidity. While aromatic alcohols, such as 2-phenylethanol, also insert into lipid bilayers and disturb the membrane organization, the impact of aromatic alcohols on the structure of biological membranes, as well as the potential physiological implication of membrane incorporation has only been studied to a limited extent. Although diverse targets are discussed to be causing the bacteriostatic and bactericidal activity of 2-phenylethanol, it is …

0303 health sciences010304 chemical physicsProcess Chemistry and TechnologyMethyl phenylacetateFiltration and SeparationBiological membranePhenylacetic acid01 natural sciencesHydrophobic effectTyrosol03 medical and health scienceschemistry.chemical_compoundMembranechemistry0103 physical sciencesBiophysicsMembrane fluidityChemical Engineering (miscellaneous)Lipid bilayer030304 developmental biologyMembranes
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Stability of Asymmetric Lipid Bilayers Assessed by Molecular Dynamics Simulations

2009

The asymmetric insertion of amphiphiles into biological membranes compromises the balance between the inner and outer monolayers. As a result, area expansion of the receiving leaflet and curvature strain may lead to membrane permeation, shape changes, or membrane fusion events. We have conducted both atomistic and coarse-grained molecular dynamics simulations of dipalmitoyl-phosphatidylcholine (DPPC) bilayers to study the effect of an asymmetric distribution of lipids between the two monolayers on membrane stability. Highly asymmetric lipid bilayers were found to be surprisingly stable within the submicrosecond time span of the simulations. Even the limiting case of a monolayer immersed in …

12-DipalmitoylphosphatidylcholineLipid BilayersBiochemistryCatalysisColloid and Surface ChemistryCOARSE-GRAINED MODELSHAPE TRANSFORMATIONSMonolayerComputer SimulationLipid bilayer phase behaviorLipid bilayerChemistryBilayerLipid bilayer fusionBiological membraneGeneral ChemistryLipid bilayer mechanicsANTIMICROBIAL PEPTIDESCrystallographyMembraneTRANSMEMBRANE DISTRIBUTIONEGG PHOSPHATIDYLCHOLINEPhosphatidylcholinesPORE FORMATIONBiophysicsPRESSURE PROFILESMECHANOSENSITIVE CHANNELlipids (amino acids peptides and proteins)OCTYL GLUCOSIDEPHOSPHOLIPID-BILAYERSJournal of the American Chemical Society
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Studies on erythrocyte acetylcholinesterase in essential hypertension.

1982

There is accumulating evidence that acetylcholinesterase (AChE might be involved in the transport of sodium across biological membranes. Consequently, because in primary hypertension abnormalities in the transport of sodium by red blood cells have been documented. AChE activities were measured in hemoglobin-free red-blood-cell membranes of patients with essential hypertension. In the absence of any effectors, the Michaelis constant of AChE for acetylcholine (Km) was 1.57 . 10(-5) mol/l, both in normotensives and in hypertensives. Sodium inhibited AChE at low substrate concentrations, whereas the enzyme was activated by sodium at moderate and high substrate levels. With increasing sodium, th…

AdultMalemedicine.medical_specialtyErythrocytesAdolescentAchéSodiumchemistry.chemical_elementEssential hypertensionchemistry.chemical_compoundInternal medicineDrug DiscoverymedicineHumansGenetics (clinical)chemistry.chemical_classificationErythrocyte MembraneSodiumSubstrate (chemistry)Biological membraneBiological TransportGeneral MedicineMiddle Agedmedicine.diseaseAcetylcholinesteraselanguage.human_languageEnzymeEndocrinologychemistryHypertensionlanguageAcetylcholinesteraseMolecular MedicineAcetylcholinemedicine.drugKlinische Wochenschrift
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The Alignment of Membrane-Active Peptides Depends on the Lipid Phase State as Viewed by solid state 19F-NMR

2009

Amphipathic membrane-active peptides (antimicrobial, hemolytic, cell-penetrating, fusogenic, etc.) achieve their functions by distinct interaction with lipid bilayers. Some typical structural modes are described in terms of models like the “barrel stave”, “toroidal pore”, “carpet” etc. These models are related to the alignment states of the peptides in the lipid bilayers (surface bound “S-state”, inserted “I-state” or tilted “T-state”), which can be readily characterized by solid state NMR. When determining such alignment, factors like peptide/lipid ratio, charge of the bilayer surface, thickness of the bilayer core, presence of cholesterol, and humidity are typically investigated. Yet, the…

AlamethicinBilayerBiophysicsMagaininLipid bilayer fusionBiological membranechemistry.chemical_compoundCrystallographychemistryBiophysicsGramicidinlipids (amino acids peptides and proteins)Lipid bilayer phase behaviorLipid bilayerBiophysical Journal
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TTAPE-Me dye is not selective to cardiolipin and binds to common anionic phospholipids nonspecifically

2021

Identification, visualization, and quantitation of cardiolipin (CL) in biological membranes is of great interest because of the important structural and physiological roles of this lipid. Selective fluorescent detection of CL using noncovalently bound fluorophore 1,1,2,2-tetrakis[4-(2-trimethylammonioethoxy)-phenylethene (TTAPE-Me) has been recently proposed. However, this dye was only tested on wild-type mitochondria or liposomes containing negligible amounts of other anionic lipids, such as phosphatidylglycerol (PG) and phosphatidylserine (PS). No clear preference of TTAPE-Me for binding to CL compared to PG and PS was found in our experiments on artificial liposomes, Escherichia coli ins…

Anions0303 health sciencesLiposomeFluorophoreCardiolipinsVesicleBiophysicsPhosphatidylglycerolsBiological membraneArticlesFluorescenceIn vitro03 medical and health scienceschemistry.chemical_compound0302 clinical medicinechemistryIn vivoLiposomesCardiolipinBiophysicsPhospholipids030217 neurology & neurosurgery030304 developmental biologyBiophysical Journal
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Anionic Lipids Modulate the Activity of the Aquaglyceroporin GlpF

2015

AbstractThe structure and composition of a biological membrane can severely influence the activity of membrane-embedded proteins. Here, we show that the E. coli aquaglyceroporin GlpF has only little activity in lipid bilayers formed from native E. coli lipids. Thus, at first glance, GlpF appears to not be optimized for its natural membrane environment. In fact, we found that GlpF activity was severely affected by negatively charged lipids regardless of the exact chemical nature of the lipid headgroup, whereas GlpF was not sensitive to changes in the lateral membrane pressure. These observations illustrate a potential mechanism by which the activity of an α-helical membrane protein is modula…

AnionsLiposomeMembranesEscherichia coli ProteinsBiophysicsAquaporinBiological membraneBiologyAquaporinsLipidsCell biologyMembraneMembrane proteinNegative chargeLiposomesEscherichia colilipids (amino acids peptides and proteins)Lipid bilayerPotential mechanismBiophysical Journal
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Intramembrane particles and filipin labelling on the membranes of autophagic vacuoles and lysosomes in mouse liver

1989

Morphologically detectable protein (intramembrane particles) and cholesterol (filipin labelling) in the membranes of autophagic vacuoles and lysosomes were studied in mouse hepatocytes using thin-section and freeze-fracture electron microscopy. Both isolated autophagic vacuoles and lysosomes, and intact tissue blocks were used due to the facts (i) that lysosomes are difficult to recognize in freeze-fracture replicas of intact hepatocytes, and (i) that filipin penetration into the tissue blocks is unsatisfactory. Intramembrane particle density was low in the membranes of early autophagic vacuoles (defined as round-shaped vacuoles in which an inner membrane parallel with the outer limiting me…

Antifungal AgentsHistologyVacuoleBiologyFilipinPathology and Forensic MedicineMice03 medical and health scienceschemistry.chemical_compoundPhagocytosisLysosomeOrganelleAutophagymedicineAnimalsFreeze FracturingFilipin030304 developmental biologyPhagosome0303 health sciencesVesicle030302 biochemistry & molecular biologyBiological membraneCell BiologyCell biologymedicine.anatomical_structureMembraneLiverchemistryVacuolesLysosomesCell and Tissue Research
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