Search results for "protein structure"

showing 10 items of 757 documents

Determination of enrichment factors for modified RNA in MeRIP experiments

2019

In the growing field of RNA modification, precipitation techniques using antibodies play an important role. However, little is known about their specificities and protocols are missing to assess their effectiveness. Here we present a method to assess enrichment factors after MeRIP-type pulldown experiments, here exemplified with a commercial antibody against N6-methyladenosine (m6A). Testing different pulldown and elution conditions, we measure enrichment factors of 4-5 using m6A-containing mRNAs against an unmodified control of identical sequence. Both types of mRNA carry 32P labels at different nucleotides, allowing their relative quantification in a mixture after digestion to nucleotides…

Models MolecularAdenosineAbsolute quantificationMethylationProtein Structure SecondaryGeneral Biochemistry Genetics and Molecular BiologyViral Proteins03 medical and health sciencesAdenosine TriphosphateRNA modificationEscherichia coliHumansImmunoprecipitationProtein Interaction Domains and MotifsNucleotideRNA MessengerMolecular Biology030304 developmental biologychemistry.chemical_classification0303 health sciencesMessenger RNACell-Free SystemChemistryElution030302 biochemistry & molecular biologyRNADNA-Directed RNA PolymerasesBiochemistryImmunoglobulin GIsotope LabelingChromatography Thin LayerPhosphorus RadioisotopesProtein BindingMethods
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Fasciola spp: Mapping of the MF6 epitope and antigenic analysis of the MF6p/HDM family of heme-binding proteins

2017

MF6p/FhHDM-1 is a small cationic heme-binding protein which is recognized by the monoclonal antibody (mAb) MF6, and abundantly present in parenchymal cells and secreted antigens of Fasciola hepatica. Orthologs of this protein (MF6p/HDMs) also exist in other causal agents of important foodborne trematodiasis, such as Clonorchis sinensis, Opisthorchis viverrini and Paragonimus westermani. Considering that MF6p/FhHDM-1 is relevant for heme homeostasis in Fasciola and was reported to have immunomodulatory properties, this protein is expected to be a useful target for vaccination. Thus, in this study we mapped the epitope recognized by mAb MF6 and evaluated its antigenicity in sheep. The sequenc…

0301 basic medicineParagonimus westermaniFasciola sppPhysiologyProtein ConformationFlatwormslcsh:MedicineProtein Structure PredictionBiochemistryEpitopeAntigenicEpitopes0302 clinical medicineAnimal CellsImmune PhysiologyMedicine and Health SciencesMacromolecular Structure AnalysisMF6p/HDMEnzyme-Linked Immunoassayslcsh:ScienceMammalsNeuronsImmune System ProteinsMultidisciplinaryFasciolabiologyVaccinationEukaryotaAntibodies MonoclonalRuminantsDendritic StructureVertebratesCellular TypesAntibodyResearch ArticleHemeproteinsProtein StructureAntigenicityFascioliasisHeme bindingImmunology030231 tropical medicineAntibodies HelminthEnzyme-Linked Immunosorbent AssayHemeResearch and Analysis MethodsTrematodesAntibodiesHeme-Binding Proteins03 medical and health sciencesHelminthsparasitic diseasesParasitic DiseasesFasciola hepaticaAnimalsImmunoassaysMolecular BiologySheeplcsh:ROrganismsBiology and Life SciencesProteinsCell BiologyDendritesNeuronal DendritesFasciola hepaticabiology.organism_classificationInvertebratesMolecular biologyFasciola030104 developmental biologyEpitope mappingCellular NeuroscienceAntigens HelminthAmniotesImmunologic Techniquesbiology.proteinlcsh:QCarrier ProteinsEpitope MappingNeuroscience
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Recombinant NeutraLite Avidin: a non-glycosylated, acidic mutant of chicken avidin that exhibits high affinity for biotin and low non-specific bindin…

2000

AbstractA recombinant non-glycosylated and acidic form of avidin was designed and expressed in soluble form in baculovirus-infected insect cells. The mutations were based on the same principles that guided the design of the chemically and enzymatically modified avidin derivative, known as NeutraLite Avidin. In this novel recombinant avidin derivative, five out of the eight arginine residues were replaced with neutral amino acids, and two of the lysine residues were replaced by glutamic acid. In addition, the carbohydrate-bearing asparagine-17 residue was altered to an isoleucine, according to the known sequences of avidin-related genes. The resultant mutant protein, termed recombinant Neutr…

StreptavidinGlycosylationMolecular Sequence DataBiophysicsBiotinChick EmbryoNon-specific bindingBiochemistrylaw.inventionchemistry.chemical_compoundBiotinstomatognathic systemStructural BiologylawMutant proteinNon-glycosylated mutantGeneticsAnimalsHumansAmino Acid SequenceIsoelectric PointProtein Structure QuaternaryMolecular BiologyCells CulturedbiologyAvidin-biotin technologyDNACell BiologyProtein engineeringrespiratory systemAvidinRecombinant ProteinsKineticsAmino Acid SubstitutionchemistryBiochemistryBiotinylationMutationbiology.proteinRecombinant DNAThermodynamicsProtein engineeringEndopeptidase KIsoleucineBaculoviridaeProtein BindingAvidinFEBS Letters
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Electrostatic Tuning of the Ligand Binding Mechanism by Glu27 in Nitrophorin 7

2018

AbstractNitrophorins (NP) 1–7 are NO-carrying heme proteins found in the saliva of the blood-sucking insect Rhodnius prolixus. The isoform NP7 displays peculiar properties, such as an abnormally high isoelectric point, the ability to bind negatively charged membranes, and a strong pH sensitivity of NO affinity. A unique trait of NP7 is the presence of Glu in position 27, which is occupied by Val in other NPs. Glu27 appears to be important for tuning the heme properties, but its influence on the pH-dependent NO release mechanism, which is assisted by a conformational change in the AB loop, remains unexplored. Here, in order to gain insight into the functional role of Glu27, we examine the ef…

Models Molecular0301 basic medicineConformational changeProtein ConformationMolecular biologylcsh:MedicineSangCrystallography X-RayLigands01 natural scienceschemistry.chemical_compoundProtein structureModelsZoologiaBloodsucking insectsNitrophorinStatic electricitylcsh:ScienceHemeCell receptorschemistry.chemical_classificationCrystallographyMultidisciplinaryParasitologiaAmino acidBloodRhodniusInsect ProteinsAnimals; Crystallography X-Ray; Glutamic Acid; Heme; Hemeproteins; Insect Proteins; Ligands; Models Molecular; Molecular Dynamics Simulation; Mutation; Protein Conformation; Rhodnius; Salivary Proteins and Peptides; Static ElectricityHemeproteinsHemeproteinStatic ElectricityGlutamic AcidHemeMolecular Dynamics Simulation010402 general chemistryArticle03 medical and health sciencesAnimalsSalivary Proteins and PeptidesBiologia molecularInsectes hematòfags030102 biochemistry & molecular biologylcsh:RMolecular0104 chemical sciencesIsoelectric pointchemistryMutationX-RayBiophysicslcsh:QReceptors cel·lularsParasitologyZoologyScientific Reports
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A lipid transfer protein binds to a receptor involved in the control of plant defence responses

2001

AbstractLipid transfer proteins (LTPs) and elicitins are both able to load and transfer lipidic molecules and share some structural and functional properties. While elicitins are known as elicitors of plant defence mechanisms, the biological function of LTP is still an enigma. We show that a wheat LTP1 binds with high affinity sites. Binding and in vivo competition experiments point out that these binding sites are common to LTP1 and elicitins and confirm that they are the biological receptors of elicitins. A mathematical analysis suggests that these receptors could be represented by an allosteric model corresponding to an oligomeric structure with four identical subunits.

Models Molecular0106 biological sciencesTime FactorsProtein ConformationPlasma protein bindingLigands01 natural sciencesBiochemistryProtein structureStructural BiologyReceptorAllosteryTriticumComputingMilieux_MISCELLANEOUSPlant Proteins0303 health sciencesFungal proteinfood and beveragesCell biologyBiochemistryPlant lipid transfer proteinsAllosteric SiteProtein BindingReceptorPhytophthoraLipid transfer proteinAllosteric regulationBiophysics[SDV.BC]Life Sciences [q-bio]/Cellular BiologyBiologyBinding CompetitiveFungal Proteins03 medical and health sciencesTobaccoGeneticsBinding site[SDV.BC] Life Sciences [q-bio]/Cellular BiologyMolecular Biology030304 developmental biologyBinding SitesDose-Response Relationship DrugAlgal ProteinsCell MembraneElicitinCell BiologyAntigens PlantModels TheoreticalLipid MetabolismElicitinCarrier Proteins010606 plant biology & botanyFEBS Letters
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Discovery of benzimidazole-based Leishmania mexicana cysteine protease CPB2.8ΔCTE inhibitors as potential therapeutics for leishmaniasis

2018

Abstract: Chemotherapy is currently the only effective approach to treat all forms of leishmaniasis. However, its effectiveness is severely limited due to high toxicity, long treatment length, drug resistance, or inadequate mode of administration. As a consequence, there is a need to identify new molecular scaffolds and targets as potential therapeutics for the treatment of this disease. We report a small series of 1,2‐substituted‐1H‐benzo[d]imidazole derivatives (9ad) showing affinity in the submicromolar range (Ki = 0.150.69 μM) toward Leishmania mexicanaCPB2.8ΔCTE, one of the more promising targets for antileishmanial drug design. The compounds confirmed activity in vitro against intrace…

BenzimidazoleCell SurvivalIn silicoLeishmania mexicanaAntiprotozoal AgentsDrug Evaluation PreclinicalProtozoan ProteinsDrug resistanceCysteine Proteinase InhibitorsPharmacologyAntileishmanial agents Benzimidazole derivatives Docking studies In silico profiling Leishmania mexicanaCPB2.8 Biochemistry Molecular Medicine01 natural sciencesBiochemistryLeishmania mexicanaCell LineInhibitory Concentration 50chemistry.chemical_compoundCysteine ProteasesDrug DiscoverymedicineHumansAmastigoteLeishmaniasisBiologyEnzyme AssaysPharmacologyBinding Sitesbiology010405 organic chemistryChemistryPharmacology. TherapyOrganic ChemistryHydrogen BondingLeishmaniasisbiology.organism_classificationmedicine.diseaseLeishmaniaProtein Structure Tertiary0104 chemical sciencesMolecular Docking Simulation010404 medicinal & biomolecular chemistryChemistryMolecular MedicineBenzimidazolesHuman medicineLeishmania infantumChemical biology and drug design
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A rhamnose-binding lectin from sea bass (Dicentrarchus labrax) plasma agglutinates and opsonizes pathogenic bacteria

2014

Abstract The discovery of rhamnose-binding lectins (RBLs) in teleost fish eggs led to the identification of a novel lectin family characterized by a unique sequence motif and a structural fold, and initially proposed to modulate fertilization. Further studies of the RBL tissue localization and gene organization were also suggestive of role(s) in innate immunity. Here we describe the purification, and biochemical and functional characterization of a novel RBL (DlRBL) from sea bass (Dicentrarchus labrax) serum. The purified DlRBL had electrophoretic mobilities corresponding to 24 kDa and 100 kDa under reducing and non-reducing conditions, respectively, suggesting that in plasma the DlRBL is p…

AgglutinationGram-negative bacteriaErythrocytesRhamnoselectin; D. labraxImmunologyAmino Acid MotifsMolecular Sequence DataRhamnoseArticlechemistry.chemical_compoundPlasmaPhagocytosisLectinsEscherichia coliAnimalsAmino Acid SequenceSea bassPeptide sequencePhylogenybiologyD. labraxLectinRhamnose bindingBacterial Infectionsbiology.organism_classificationImmunity InnateProtein Structure TertiaryBiochemistrychemistrybiology.proteinMacrophages PeritoneallectinBassRabbitsProtein MultimerizationSequence motifDevelopmental BiologyHomotetramerProtein Binding
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Multiphoton Absorption of Myoglobin Nitric-Oxide complex: Relaxation by D-NEMD of a Stationary State

2012

ABSTRACT: The photodissociation and geminate recombination of nitric oxide in myoglobin, under continuous illumination, is modeled computationally. The relaxation of the photon energy into the protein matrix is also considered in a single simulation scheme that mimics a complete experimental setup. The dynamic approach to non-equilibrium molecular dynamics is used, starting from a steady state, to compute its relaxation to equilibrium. Simulations are conducted for the native form of sperm whale myoglobin and for two other mutants, V68W and L29F, illustrating a fair diversity of spatial and temporal geminate recombination processes. Energy flow to the heme and immediate protein environment …

myoglobin molecular dynamics simulations non equilibriumThermal fluctuationsMolecular Dynamics SimulationNitric OxideArticleAbsorptionchemistry.chemical_compoundMolecular dynamicsComputational chemistryMaterials ChemistryPhysical and Theoretical ChemistryHemePhotonsSteady stateChemistryMyoglobinPhotodissociationTemperatureSettore FIS/07 - Fisica Applicata(Beni Culturali Ambientali Biol.e Medicin)Recombinant ProteinsSurfaces Coatings and FilmsProtein Structure TertiaryMyoglobinChemical physicsMutationRelaxation (physics)Stationary stateProtein Binding
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The inner nuclear membrane protein Src1 associates with subtelomeric genes and alters their regulated gene expression

2008

Inner nuclear membrane proteins containing a LEM (LAP2, emerin, and MAN1) domain participate in different processes, including chromatin organization, gene expression, and nuclear envelope biogenesis. In this study, we identify a robust genetic interaction between transcription export (TREX) factors and yeast Src1, an integral inner nuclear membrane protein that is homologous to vertebrate LEM2. DNA macroarray analysis revealed that the expression of the phosphate-regulated genes PHO11, PHO12, and PHO84 is up-regulated in src1Δ cells. Notably, these PHO genes are located in subtelomeric regions of chromatin and exhibit a perinuclear location in vivo. Src1 spans the nuclear membrane twice an…

Chromatin ImmunoprecipitationSaccharomyces cerevisiae ProteinsGenes FungalSaccharomyces cerevisiaeProtein Sorting SignalsBiologyArticleGenètica molecularProton-Phosphate SymportersGene Expression Regulation FungalGene expressionmedicineExpressió genèticaInner membraneNuclear proteinNuclear poreNuclear membraneResearch ArticlesNucleoplasmMembrane ProteinsNuclear ProteinsCell BiologyTelomereMolecular biologyChromatinProtein Structure TertiaryChromatinAlternative SplicingGenòmicamedicine.anatomical_structureMultiprotein ComplexesNuclear lamina
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Quality assessment of protein NMR structures.

2013

Biomolecular NMR structures are now routinely used in biology, chemistry, and bioinformatics. Methods and metrics for assessing the accuracy and precision of protein NMR structures are beginning to be standardized across the biological NMR community. These include both knowledge-based assessment metrics, parameterized from the database of protein structures, and model versus data assessment metrics. On line servers are available that provide comprehensive protein structure quality assessment reports, and efforts are in progress by the world-wide Protein Data Bank (wwPDB) to develop a biomolecular NMR structure quality assessment pipeline as part of the structure deposition process. These qu…

Models MolecularProtein structure; NMR spectroscopyMagnetic Resonance SpectroscopyProtein ConformationAnalytical chemistryBiology010402 general chemistrycomputer.software_genre01 natural sciencesArticle03 medical and health sciencesStructural BiologyServerDatabases ProteinMolecular BiologyNuclear Magnetic Resonance Biomolecular030304 developmental biology0303 health sciencesExtramuralQuality assessmentData assessmentResearchProteinsReproducibility of ResultsNuclear magnetic resonance spectroscopycomputer.file_formatProtein Data Bank0104 chemical sciencesData miningcomputerDeposition processCurrent opinion in structural biology
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