Search results for "proteïnes"

showing 10 items of 89 documents

Role of HDL function and LDL atherogenicity on cardiovascular risk: a comprehensive examination

2019

[Background] High-density lipoprotein (HDL) functionality and low-density lipoprotein (LDL) atherogenic traits can describe the role of both particles on cardiovascular diseases more accurately than HDL- or LDL-cholesterol levels. However, it is unclear how these lipoprotein properties are particularly affected by different cardiovascular risk factors.

MalePhysiologyhumanosLipoproteïnesBlood PressureCardiovascular Medicine030204 cardiovascular system & hematologyOxidacióBiochemistryVascular Medicinelipoproteínas616.1 - Patologia del sistema circulatori dels vasos sanguinis. Trastorns cardiovasculars:Ciencias de la Salud::Cardiología [Materias Investigacion]Endocrinology0302 clinical medicineRisk FactorsSex factorsSistema cardiovascular--MalaltiesMedicine and Health SciencesMedicine030212 general & internal medicinemediana edadancianoMultidisciplinaryQChemical ReactionsAge FactorsRMiddle AgedadultoLipidsBody FluidsLipoproteins LDLLipoproteïnes de densitat baixaChemistryBloodCholesterolCardiovascular DiseasesPhysical SciencesHypertensiondiabetes mellitusMedicineFemalelipids (amino acids peptides and proteins)AnatomyLipoproteins HDLColesterolResearch ArticleAdultEndocrine DisordersScienceLipoproteinsdislipidemiasenfermedades cardiovascularesBlood Plasma03 medical and health sciencesSex FactorsOxidationHumansfactores de riesgoAgedDyslipidemiasbusiness.industryCholesterol HDLBiology and Life SciencesProteinsCholesterol LDLAtherosclerosisSistema cardiovascular -- Malalties -- Factors de riscCross-Sectional StudiesLipoproteïnes de densitat altaDyslipidemiaDiabetes Mellitus Type 2Metabolic DisordersaterosclerosisbusinessHumanitiesestudios transversales
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Peptides corresponding to helices 5 and 6 of Bax can independently form large lipid pores

2006

Proteins of the B-cell lymphoma protein 2 (Bcl2) family are key regulators of the apoptotic cascade, controlling the release of apoptotic factors from the mitochondrial intermembrane space. A helical hairpin found in the core of water-soluble folds of these proteins has been reported to be the pore- forming domain. Here we show that peptides including any of the two a-helix fragments of the hairpin of Bcl2 associated protein X (Bax) can independently induce release of large labelled dextrans from synthetic lipid vesicles. The permeability promoted by these peptides is influenced by intrinsic monolayer curvature and accompanied by fast transbilayer redis- tribution of lipids, supporting a to…

Mitochondrial intermembrane spaceLipid BilayersMolecular Sequence DataIn Vitro TechniquesBiologyBiochemistryPermeabilityProtein Structure SecondaryMiceMonolayerAnimalsAmino Acid SequenceMolecular Biologybcl-2-Associated X ProteinCircular DichroismProtein xProteïnes de membranaCell BiologyPeptide FragmentsMitochondriaCell biologyMembrane proteinApoptosisLiposomesLipid vesiclePèptids
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Molecular architecture and activation of the insecticidal protein Vip3Aa from Bacillus thuringiensis

2020

9 p.-5 fig.

Models Molecular0301 basic medicineProteasesBiologiaMolecular biologymedicine.medical_treatmentScienceAmino Acid MotifsBacillus thuringiensisGeneral Physics and Astronomy02 engineering and technologyGenetically modified cropsBiotecnologiaArticleProtein Structure SecondaryGeneral Biochemistry Genetics and Molecular Biology03 medical and health sciencesBacterial ProteinsProtein DomainsTetramerBacillus thuringiensisElectron microscopymedicineTrypsinlcsh:ScienceMultidisciplinaryProteasebiologyChemistryQfungifood and beveragesMidgutGeneral Chemistry021001 nanoscience & nanotechnologybiology.organism_classification030104 developmental biologyStructural biologyBiochemistrylcsh:QStructural biology0210 nano-technologyProteïnesFunction (biology)
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Changes in the hydrogen-bonding strength of internal water molecules and cysteine residues in the conductive state of channelrhodopsin-1

2014

Water plays an essential role in the structure and function of proteins, particularly in the less understood class of membrane proteins. As the first of its kind, channelrhodopsin is a light-gated cation channel and paved the way for the new and vibrant field of optogenetics, where nerve cells are activated by light. Still, the molecular mechanism of channelrhodopsin is not understood. Here, we applied time-resolved FT-IR difference spectroscopy to channelrhodopsin-1 from Chlamydomonas augustae. It is shown that the (conductive) P2(380) intermediate decays with τ ≈ 40 ms and 200 ms after pulsed excitation. The vibrational changes between the closed and the conductive states were analyzed in…

Models Molecular570StereochemistryGeneral Physics and AstronomyInfrared spectroscopy530Ion Channelschemistry.chemical_compoundAmideRhodopsins MicrobialSpectroscopy Fourier Transform InfraredSide chainMoleculePeptide bondCysteinePhysical and Theoretical ChemistryPlant Proteinschemistry.chemical_classificationHydrogen bondChlamydomonasWaterFísicaHydrogen BondingQuímicaCrystallographychemistryThiolProteïnesCysteineThe Journal of Chemical Physics
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Synthetic Pulmonary Surfactant Preparations: New developments and future trends

2008

Pulmonary surfactant is a lipid-protein complex that coats the interior of the alveoli and enables the lungs to function properly. Upon its synthesis, lung surfactant adsorbs at the interface between the air and the hypophase, a capillary aqueous layer covering the alveoli. By lowering and modulating surface tension during breathing, lung surfactant reduces respiratory work of expansion, and stabilises alveoli against collapse during expiration. Pulmonary surfactant deficiency, or dysfunction, contributes to several respiratory pathologies, such as infant respiratory distress syndrome (IRDS) in premature neonates, and acute respiratory distress syndrome (ARDS) in children and adults. The ma…

Models MolecularARDSmedicine.medical_specialtyMolecular Sequence DataAcute respiratory distressPharmacologyBiochemistryStructure-Activity RelationshipPulmonary surfactantDrug DiscoveryAnimalsHumansMedicineAmino Acid SequenceRespiratory systemPharmacologyRespiratory distressbusiness.industryOrganic ChemistryRespiratory diseasePulmonary Surfactantsmedicine.diseaseLipidsSurgeryDuring expirationBreathingMolecular MedicinebusinessProteïnesPulmons Malalties
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Distant downstream sequence determinants can control N-tail translocation during protein insertion into the endoplasmic reticulum membrane.

2000

We have studied the membrane insertion of ProW, an Escherichia coli inner membrane protein with seven transmembrane segments and a large periplasmic N-terminal tail, into endoplasmic reticulum (ER)-derived dog pancreas microsomes. Strikingly, significant levels of N-tail translocation is seen only when a minimum of four of the transmembrane segments are present; for constructs with fewer transmembrane segments, the N-tail remains mostly nontranslocated and the majority of the molecules adopt an 'inverted' topology where normally nontranslocated parts are translocated and vice versa. N-tail translocation can also be promoted by shortening of the N-tail and by the addition of positively charg…

Models MolecularBioquímicaGlycosylationChromosomal translocationBiologyEndoplasmic ReticulumBiochemistryBacterial ProteinsMembranes (Biologia)MicrosomesEscherichia coliAnimalsInner membranePancreasMolecular BiologyEscherichia coli ProteinsEndoplasmic reticulumMembrane ProteinsSTIM1Periplasmic spaceCell BiologyMolecular biologyTransmembrane proteinCell biologyMembrane proteinMutationCatsMicrosomeATP-Binding Cassette TransportersProteïnesJournal of Biological Chemistry
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Charge Pair Interactions in Transmembrane Helices and Turn Propensity of the Connecting Sequence Promote Helical Hairpin Insertion

2013

alpha-Helical hairpins, consisting of a pair of closely spaced transmembrane (TM) helices that are connected by a short interfacial turn, are the simplest structural motifs found in multi-spanning membrane proteins. In naturally occurring hairpins, the presence of polar residues is common and predicted to complicate membrane insertion. We postulate that the pre-packing process offsets any energetic cost of allocating polar and charged residues within the hydrophobic environment of biological membranes. Consistent with this idea, we provide here experimental evidence demonstrating that helical hairpin insertion into biological membranes can be driven by electrostatic interactions between clo…

Models MolecularBioquímicaProtein FoldingGlycosylationMolecular Sequence Datamembrane integrationEndoplasmic Reticulumsalt bridgeProtein Structure SecondaryTurn (biochemistry)Viral Proteins03 medical and health sciencesProtein structureStructural BiologyComputer SimulationAmino Acid SequenceAmino AcidsStructural motifMolecular Biologytranslocon030304 developmental biology0303 health sciencesBinding SitesChemistry030302 biochemistry & molecular biologyProteïnes de membranaBiochemistry and Molecular BiologyMembrane ProteinsBiological membraneTransloconelectrostatic interactionsTransmembrane proteinProtein Structure TertiaryPoliovirusProtein TransportCrystallographyTransmembrane domainhelical hairpinMembrane proteinMutationBiophysicsElectrophoresis Polyacrylamide GelHydrophobic and Hydrophilic InteractionsBiokemi och molekylärbiologi
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Peptides Derived from Apoptotic Bax and Bid Reproduce the Poration Activity of the Parent Full-Length Proteins

2005

Bax and Bid are proapoptotic proteins of the Bcl-2 family that regulate the release of apoptogenic factors from mitochondria. Although they localize constitutively in the cytoplasm, their apoptotic function is exerted at the mitochondrial outer membrane, and is related to their ability to form transbilayer pores. Here we report the poration activity of fragments from these two proteins, containing the first alpha-helix of a colicinlike hydrophobic hairpin (alpha-helix 5 of Bax and alpha-helix 6 of Bid). Both peptides readily bind to synthetic lipid vesicles, where they adopt predominantly alpha-helical structures and induce the release of entrapped calcein. In planar lipid membranes they fo…

Models MolecularMolecular Sequence DataBiophysicsApoptosisPeptideIn Vitro TechniquesBiophysical PhenomenaIon ChannelsPermeabilityProtein Structure Secondarychemistry.chemical_compoundBcl-2-associated X proteinSpectroscopy Fourier Transform InfraredHumansChannels Receptors and Electrical SignalingAmino Acid SequencePeptide sequenceIon channelbcl-2-Associated X Proteinchemistry.chemical_classificationbiologyChemistryCircular DichroismPeptide FragmentsCell biologyCalceinMembraneProto-Oncogene Proteins c-bcl-2CytoplasmMultiprotein ComplexesLiposomesbiology.proteinPèptidsCarrier ProteinsBacterial outer membraneProteïnesBH3 Interacting Domain Death Agonist ProteinBiophysical Journal
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Membrane insertion and topology of the TRanslocating chain-Associating Membrane protein (TRAM)

2011

The translocating chain-associating membrane protein (TRAM) is a glycoprotein involved in the translocation of secreted proteins into the endoplasmic reticulum (ER) lumen and in the insertion of integral membrane proteins into the lipid bilayer. As a major step toward elucidating the structure of the functional ER translocation/insertion machinery, we have characterized the membrane integration mechanism and the transmembrane topology of TRAM using two approaches: photocross-linking and truncated C-terminal reporter tag fusions. Our data indicate that TRAM is recognized by the signal recognition particle and translocon components, and suggest a membrane topology with eight transmembrane seg…

Models MolecularProtein ConformationEndoplasmic ReticulumModels BiologicalProtein Structure SecondaryMiceMembranes (Biologia)Structural BiologyAnimalsMolecular BiologyIntegral membrane proteinSignal recognition particleMembrane GlycoproteinsbiologyMembrane transport proteinPeripheral membrane proteinProteïnes de membranaIntracellular MembranesTransloconTransmembrane proteinProtein Structure TertiaryMembrane proteinBiochemistryMembrane topologybiology.proteinBiophysics
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Influence of proline residues in transmembrane helix packing

2003

Integral membrane proteins often contain proline residues in their alpha-helical transmembrane (TM) fragments, which may strongly influence their folding and association. Pro-scanning mutagenesis of the helical domain of glycophorin A (GpA) showed that replacement of the residues located at the center abrogates helix packing while substitution of the residues forming the ending helical turns allows dimer formation. Synthetic TM peptides revealed that a point mutation of one of the residues of the dimerization motif (L75P) located at the N-terminal helical turn of the GpA TM fragment, adopts a secondary structure and oligomeric state similar to the wild-type sequence in detergents. In additi…

Models MolecularProtein FoldingGlycosylationProlineStereochemistryProtein ConformationCollagen helixRecombinant Fusion ProteinsMolecular Sequence DataEndoplasmic ReticulumProtein Structure SecondaryComputers MolecularProtein structureStructural BiologyAmino Acid SequenceGlycophorinsMolecular BiologyIntegral membrane proteinProtein secondary structureChemistryCell MembraneProteïnes de membranaWaterLipidsTransmembrane proteinPeptide FragmentsCrystallographyTransmembrane domainMembrane proteinHelixMutagenesis Site-DirectedDimerization
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