Search results for "hydrophilic"

showing 10 items of 276 documents

Methodological approaches for the analysis of transmembrane domain interactions: A systematic review

2021

The study of protein-protein interactions (PPI) has proven fundamental for the understanding of the most relevant cell processes. Any protein domain can participate in PPI, including transmembrane (TM) segments that can establish interactions with other TM domains (TMDs). However, the hydrophobic nature of TMDs and the environment they occupy complicates the study of intramembrane PPI, which demands the use of specific approaches and techniques. In this review, we will explore some of the strategies available to study intramembrane PPI in vitro, in vivo, and, in silico, focusing on those techniques that could be carried out in a standard molecular biology laboratory regarding its previous e…

Protein FoldingBacteriaChemistryIn silicoProtein domainBiophysicsMembrane ProteinsCell CommunicationCell BiologyComputational biologyBiochemistryTransmembrane proteinIn vitroProtein–protein interactionTransmembrane domainProtein DomainsMembrane proteinProtein foldingProtein Interaction MapsHydrophobic and Hydrophilic InteractionsBiochimica et Biophysica Acta (BBA) - Biomembranes
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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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Influence of hydrophobic matching on association of model transmembrane fragments containing a minimised glycophorin A dimerisation motif

2005

AbstractThe principles that govern the folding and packing of membrane proteins are still not completely understood. In the present work, we have revisited the glycophorin A (GpA) dimerisation motif that mediates transmembrane (TM) helix association, one of the best-suited models of membrane protein oligomerisation. By using artificial polyleucine TM segments we have demonstrated in this study that a pattern of only five amino acids (GVxxGVxxT) promotes specific dimerisation. Further, we have used this minimised GpA motif to assess the influence of hydrophobic matching on the TM helix packing process in detergent micelles and found that this factor modulates helix–helix association and/or d…

Protein FoldingRecombinant Fusion ProteinsAmino Acid MotifsMolecular Sequence DataBiophysicsBiochemistryMicelleHydrophobic mismatchHydrophobic mismatchStructural BiologyLeucineHelix packingGeneticsGlycophorinAnimalsHumansAmino Acid SequenceGlycophorinsMolecular BiologyPolyacrylamide gel electrophoresischemistry.chemical_classificationbiologyChemistryGlycophorin AProteïnes de membranaMembrane ProteinsMembrane protein associationCell BiologyTransmembrane proteinAmino acidTransmembrane domainBiochemistryMembrane proteinMutationTransmembrane helixBiophysicsbiology.proteinPeptidesDimerizationHydrophobic and Hydrophilic Interactions
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Transmembrane but not soluble helices fold inside the ribosome tunnel

2018

Integral membrane proteins are assembled into the ER membrane via a continuous ribosome-translocon channel. The hydrophobicity and thickness of the core of the membrane bilayer leads to the expectation that transmembrane (TM) segments minimize the cost of harbouring polar polypeptide backbones by adopting a regular pattern of hydrogen bonds to form α-helices before integration. Co-translational folding of nascent chains into an α-helical conformation in the ribosomal tunnel has been demonstrated previously, but the features governing this folding are not well understood. In particular, little is known about what features influence the propensity to acquire α-helical structure in the ribosom…

Protein FoldingSequence Homology Amino AcidScienceQProteïnes de membranaMembrane ProteinsMolecular Dynamics SimulationEndoplasmic ReticulumArticleProtein Structure SecondaryAnimalslcsh:QAmino Acid Sequencelcsh:ScienceHydrophobic and Hydrophilic InteractionsSignal Recognition ParticleRibosomes
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Solvent-induced free energy landscape and solute-solvent dynamic coupling in a multielement solute

1999

AbstractMolecular dynamics simulations using a simple multielement model solute with internal degrees of freedom and accounting for solvent-induced interactions to all orders in explicit water are reported. The potential energy landscape of the solute is flat in vacuo. However, the sole untruncated solvent-induced interactions between apolar (hydrophobic) and charged elements generate a rich landscape of potential of mean force exhibiting typical features of protein landscapes. Despite the simplicity of our solute, the depth of minima in this landscape is not far in size from free energies that stabilize protein conformations. Dynamical coupling between configurational switching of the syst…

Quantitative Biology::BiomoleculesProtein ConformationChemistryBiophysicsDegrees of freedom (physics and chemistry)ProteinsEnergy landscapeMolecular Dynamics SimulationSolventMolecular dynamicsCoupling (computer programming)Chemical physicsComputational chemistrySolventsThermodynamicsProtein foldingPotential of mean forceHydrophobic and Hydrophilic InteractionsOrder of magnitudeResearch Article
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Determination of the hydrophobicity of organic compounds measured as logPo/w through a new chromatographic method

2009

A new chromatographic method to determine the octanol-water partition coefficient (logP(o/w)) of organic substances is proposed in this paper. This method is based on a previously reported model that relates the retention factor in reversed-phase liquid chromatography with solute (p), mobile phase (P(m)(N)) and stationary phase (P(s)(N)) polarity parameters: logk=(logk)(0)+p(P(m)(N)-P(s)(N)). P(m)(N) values are calculated through expressions that depend only on the organic solvent fraction in the mobile phase. (logk)(0) and P(s)(N) parameters are characteristic of the chromatographic system and are determined from the retention of a selected set of 12 compounds. Then, the p value of a solut…

Quantitative structure–activity relationshipChromatographyChemistryChemical structureOrganic ChemistryAnalytical chemistryQuantitative Structure-Activity RelationshipGeneral MedicineReversed-phase chromatographyHydrogen-Ion ConcentrationBiochemistryHigh-performance liquid chromatographyAnalytical ChemistryPartition coefficientchemistry.chemical_compoundPhase (matter)LipophilicityOrganic ChemicalsAcetonitrileHydrophobic and Hydrophilic InteractionsChromatography LiquidJournal of Chromatography A
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Event-based criteria in GT-STAF information indices: theory, exploratory diversity analysis and QSPR applications

2012

Versatile event-based approaches for the definition of novel information theory-based indices (IFIs) are presented. An event in this context is the criterion followed in the "discovery" of molecular substructures, which in turn serve as basis for the construction of the generalized incidence and relations frequency matrices, Q and F, respectively. From the resultant F, Shannon's, mutual, conditional and joint entropy-based IFIs are computed. In previous reports, an event named connected subgraphs was presented. The present study is an extension of this notion, in which we introduce other events, namely: terminal paths, vertex path incidence, quantum subgraphs, walks of length k, Sach's subg…

Quantitative structure–activity relationshipEntropyChemistry OrganicInformation TheoryQuantitative Structure-Activity RelationshipBioengineeringInformation theoryJoint entropyMolecular descriptorDrug DiscoveryComputer GraphicsCluster AnalysisEntropy (information theory)QuantumMathematicsDiscrete mathematicsMolecular StructureLinear modelComputational BiologyGeneral MedicineEthylenesModels TheoreticalLinear ModelsMolecular MedicineSubstructureHydrophobic and Hydrophilic InteractionsAlgorithmsSoftwareSAR and QSAR in Environmental Research
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Improvement of the wettability and dissolution of fenofibrate compacts by plasma treatment

2011

Abstract The goal of this study was to investigate the effect of plasma treatment on the wettability and dissolution of fenofibrate compacts. Contact angle measurements and intrinsic dissolution rate studies of untreated and plasma-treated fenofibrate compacts were conducted. The contact angle data clearly show that the wettability of the tablet surface increased with the duration of plasma treatment. Analyses of stability revealed that the surfaces which were plasma-treated for more than 1 min regained some degree of hydrophobicity after storage in air. Since their hydrophobic recovery finally reached the level observed with 1 min plasma-treated fenofibrate compacts it was deduced that per…

Radiation NonionizingMaterials sciencePlasma irradiationFenofibrateChromatographyDrug CompoundingPharmaceutical SciencePlasma treatmentOxygenContact angleFenofibrateSolubilityChemical engineeringWettabilitymedicineWettingSolubilitySaturation (chemistry)Hydrophobic and Hydrophilic InteractionsDissolutionTabletsmedicine.drugInternational Journal of Pharmaceutics
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The Tobacco mosaic virus movement protein associates with but does not integrate into biological membranes

2014

Plant positive-strand RNA viruses require association with plant cell endomembranes for viral translation and replication, as well as for intra- and intercellular movement of the viral progeny. The membrane association and RNA binding of the Tobacco mosaic virus (TMV) movement protein (MP) are vital for orchestrating the macromolecular network required for virus movement. A previously proposed topological model suggests that TMV MP is an integral membrane protein with two putative -helical transmembrane (TM) segments. Here we tested this model using an experimental system that measured the efficiency with which natural polypeptide segments were inserted into the ER membrane under conditions…

Recombinant Fusion ProteinsvirusesMolecular Sequence DataImmunologyGene ExpressionMicrobiologiaBiologyEndoplasmic ReticulumMicrobiologyCell membraneGenes ReporterPlant CellsVirologymedicineTobacco mosaic virusAmino Acid SequenceMovement proteinIntegral membrane proteinStructure and AssemblyCell MembraneViral translationfungifood and beveragesBiological membraneVirologyTransmembrane proteinTransport proteinCell biologyVirusPlant Viral Movement ProteinsTobacco Mosaic VirusProtein Transportmedicine.anatomical_structureInsect ScienceHydrophobic and Hydrophilic InteractionsProtein Binding
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Influence of PVP/VA copolymer composition on drug–polymer solubility

2015

In this study, the influence of copolymer composition on drug-polymer solubility was investigated. The solubility of the model drug celecoxib (CCX) in various polyvinylpyrrolidone/vinyl acetate (PVP/VA) copolymer compositions (70/30, 60/40, 50/50 and 30/70 w/w) and the pure homopolymers polyvinylpyrrolidone (PVP) and polyvinyl acetate (PVA) was predicted at 25 °C using a thermal analysis method based on the recrystallization of a supersaturated amorphous dispersion (recrystallization method). These solubilities were compared with a prediction based on the solubility of CCX in the liquid monomeric precursors of PVP/VA, N-vinylpyrrolidone (NVP) and vinyl acetate (VA), using the Flory-Huggins …

Recrystallization (geology)PolymersChemistry PharmaceuticalPharmaceutical Science02 engineering and technologyFlory–Huggins solution theory030226 pharmacology & pharmacy03 medical and health scienceschemistry.chemical_compound0302 clinical medicineDrug StabilityPolymer chemistrymedicineVinyl acetateCopolymerSolubilityPolyvinyl acetatePolyvinylpyrrolidonePovidone021001 nanoscience & nanotechnologyMonomerSolubilitychemistryCelecoxibThermodynamicsPolyvinylsCrystallization0210 nano-technologyHydrophobic and Hydrophilic Interactionsmedicine.drugEuropean Journal of Pharmaceutical Sciences
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