Search results for "Denaturation"

showing 10 items of 107 documents

Erwinia piriflorinigrans sp. nov., a novel pathogen that causes necrosis of pear blossoms

2010

Eight Erwinia strains, isolated from necrotic pear blossoms in València, Spain, were compared with reference strains of Erwinia amylovora and Erwinia pyrifoliae, both of which are pathogenic to species of pear tree, and to other species of the family Enterobacteriaceae using a polyphasic approach. Phenotypic analyses clustered the novel isolates into one phenon, distinct from other species of the genus Erwinia, showing that the novel isolates constituted a homogeneous phenotypic group. Rep-PCR profiles, PCR products obtained with different pairs of primers and plasmid contents determined by restriction analysis showed differences between the novel strains and reference strains of E. amylovo…

AD-HOC-COMMITTEEBACTERIALFIRE BLIGHT PATHOGENErwiniaPolymerase Chain ReactionErwinia pyrifoliaePyrusRNA Ribosomal 16SCluster Analysis[SDV.BDD]Life Sciences [q-bio]/Development BiologyPhylogenyNESTED-PCRBase Composition0303 health sciencesPEARbiologyPhylogenetic treeNucleic Acid Hybridizationfood and beveragesGeneral MedicineEnterobacteriaceaeBacterial Typing TechniquesTHERMAL-DENATURATIONPlasmidsDNA BacterialGenotypeMolecular Sequence DataDNA RibosomalMicrobiologyMicrobiology03 medical and health sciencesBacterial ProteinsPhylogeneticsDEOXYRIBONUCLEIC-ACIDEcology Evolution Behavior and SystematicsPlant Diseases030304 developmental biologyIDENTIFICATIONSEQUENCES030306 microbiologyAMYLOVORASequence Analysis DNADNARibosomal RNAbiochemical phenomena metabolism and nutrition16S ribosomal RNAbiology.organism_classificationMolecular TypingSpainErwiniabacteria
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Mutation screening for the prothrombin variant G20210A by melting point analysis with the Light Cycler system: atypical results, detection of the var…

2005

In the differential diagnosis of thrombophilic disorders genotyping of prothrombin and factor V are nowadays performed as a routine analysis. In the following we describe the unusual results of the mutation screening using melting point analysis for two patients and the consecutive detection of the mutation C20209T by sequencing the corresponding gene fragments. The molecular result is discussed with special respect to the medical history, ethnic background and clinical findings of both patients.

AdultMaleHot TemperatureDNA Mutational AnalysisClinical BiochemistryBiologyNucleic Acid DenaturationThrombophiliaPolymerase Chain Reactionlaw.inventionlawmedicineHumansPoint MutationThrombophiliaMedical historyGenotypingPolymerase chain reactionGeneticsPoint mutationBiochemistry (medical)Factor VSequence Analysis DNAHematologyGeneral Medicinemedicine.diseaseMutation (genetic algorithm)biology.proteinFemaleProthrombinDifferential diagnosisClinical and Laboratory Haematology
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The kinetic behavior of insulin fibrillation is determined by heterogeneous nucleation pathways

2005

When subjected to acidic conditions and high temperature, insulin is known to produce fibrils that display the common properties of disease amyloids. Thus, clarifying the mechanisms of insulin fibrillation can help the general understanding of amyloidal aggregation. Insulin fibrillation exhibits a very sharp time dependence, with a pronounced lag phase and subsequent explosive growth of amyloidal aggregates. Here we show that the initial stages of this process can be well described by exponential growth of the fibrillated proteins. This indicates that the process is mainly controlled by a secondary nucleation pathway.

AmyloidProtein DenaturationTime FactorsAmyloidmedicine.medical_treatmentKineticsNucleationmacromolecular substancesProtein aggregationFibrilBiochemistryExponential growthmedicineAnimalsInsulinMolecular BiologyFibrillationChemistryInsulinTemperatureHydrogen-Ion ConcentrationKineticsBiochemistryFor the RecordBiophysicsCattlemedicine.symptomProtein Science
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Effect of pea proteins extraction and vicilin/legumin fractionation on the phase behavior in admixture with alginate

2012

Abstract Soluble and natural mixed pea proteins (PP) were extracted from defatted pea seeds according to acidic precipitation (PPP) or ultrafiltration/diafiltration (PPDF) procedures. The isolates contained proteins with a low level of denaturation. Mixed pea globulins isolates presented quite similar solubility and thermal profiles, also a similar polypeptide composition. Vicilin/convicilin 7S (Vic) and legumin 11S (Leg) fractions were obtained by batch chromatography using a salt gradient for the elution. Several incompatible systems were built by mixing the pea proteins with an anionic polysaccharide (sodium alginate, SA), when biopolymers were both negatively charged. Most of mixtures e…

BinodalChromatographyGlobulinbiologyChemistryGeneral Chemical EngineeringGeneral ChemistryFractionationDiafiltrationPhase (matter)Vicilinbiology.proteinLeguminDenaturation (biochemistry)Food ScienceFood Hydrocolloids
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Molecular Dynamics Simulations of the Initial Adsorption Stages of Fibrinogen on Mica and Graphite Surfaces.

2015

Fibrinogen, a blood glycoprotein of vertebrates, plays an essential role in blood clotting by polymerizing into fibrin when activated. Upon adsorption on material surfaces, it also contributes to determine their biocompatibility and has been implicated in the onset of thrombosis and inflammation at medical implants. Here we present the first fully atomistic simulations of the initial stages of the adsorption process of fibrinogen on mica and graphite surfaces. The simulations reveal a weak adsorption on mica that allows frequent desorption and reorientation events. This adsorption is driven by electrostatic interactions between the protein and the silicate surface as well as the counterion …

BiocompatibilityProtein ConformationSurface PropertiesStatic ElectricityNanotechnologyMolecular Dynamics SimulationAdsorptionDesorptionElectrochemistryGeneral Materials ScienceDenaturation (biochemistry)GraphiteSpectroscopychemistry.chemical_classificationFibrinogenSurfaces and InterfacesCondensed Matter PhysicschemistryChemical engineeringAluminum SilicatesGraphiteMicaAdsorptionCounterionHydrophobic and Hydrophilic InteractionsProtein adsorptionLangmuir : the ACS journal of surfaces and colloids
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The Internal Dynamics and Early Adsorption Stages of Fibrinogen Investigated by Molecular Dynamics Simulations

2016

Fibrinogen, a plasma glycoprotein of vertebrates, plays an essential role in blood clotting by polymerizing into fibrin upon activation. It also contributes, upon adsorption on material surfaces, to determine their biocompatibility and has been implicated as a cause of thrombosis and inflammation at medical implants. Here we present the first fully atomistic simulations of the initial stages of the adsorption process of fibrinogen on mica and graphite surfaces. The simulations reveal a weak adsorption on mica that allows frequent desorption and reorientation events. This adsorption is driven by electrostatic interactions between the protein and the silicate surface as well as the counter io…

BiocompatibilitybiologyChemistryFibrinogenFibrinMolecular dynamicsAdsorptionDesorptionmedicineBiophysicsbiology.proteinDenaturation (biochemistry)Micamedicine.drug
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Nanoparticle Assembly of Surface-Modified Proteins

2016

Nature's biomaterials such as peptides and proteins represent a valuable source of highly defined macromolecules. Herein we developed a nanoparticle drug delivery system based on the assembly of surface-modified proteins that can be transferred into organic solvents and represent the structural material of the carrier system. The particles are prepared by an oil-in-water nanoemulsion technique without the need of additional denaturation or cross-linking steps for stabilization. We achieve the necessary lipophilic solubility switch of the protein material by high surface PEGylation under conservation of the native three-dimensional protein structure. This study focuses on lysozyme as model e…

Carrier systemCell SurvivalSurface PropertiesNanoparticleNanotechnology02 engineering and technology010402 general chemistry01 natural sciencesBiochemistryCatalysisStructure-Activity RelationshipColloid and Surface ChemistryProtein structureHumansDenaturation (biochemistry)Particle SizeSolubilityDrug CarriersDose-Response Relationship DrugChemistryGeneral Chemistry021001 nanoscience & nanotechnology0104 chemical sciencesDoxorubicinDrug deliveryBiophysicsPEGylationNanoparticlesMuramidase0210 nano-technologyHeLa CellsMacromoleculeJournal of the American Chemical Society
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Toll-like receptor 3 mediates expression of clusterin/apolipoprotein J in vascular smooth muscle cells stimulated with RNA released from necrotic cel…

2010

Clusterin/Apolipoprotein J is a protein that is upregulated in a broad spectrum of diverse pathological processes. The predominant form is a secreted glycoprotein (sCLU) with cytoprotective and anti-inflammatory properties which shows enhanced expression in vascular smooth muscle cells (VSMC) following aortic injury and in atherosclerotic disease. Recent evidence indicates that during atherosclerosis, Toll-like receptors (TLRs) are activated in vascular cells by endogenous ligands. Here, we analyzed whether CLU expression in VSMC is controlled by TLRs, and stimulated by factors associated with or released by necrotic cells. Activation of TLR3 by the synthetic RNA analogue polyinosinic-polyc…

Cell ExtractsProtein DenaturationHot TemperatureMyocytes Smooth MuscleMedizinGene ExpressionBiologyTransfectionMuscle Smooth VascularCell LineMiceNecrosisDogsDownregulation and upregulationGene expressionAnimalsHumansChemokine CCL2Mice KnockoutMessenger RNAToll-like receptorClusterinToll-Like ReceptorsProteinsChloroquineCell BiologyMolecular biologyEndocytosisRatsToll-Like Receptor 3Mice Inbred C57BLTLR2Adaptor Proteins Vesicular TransportClusterinPoly I-CCulture Media ConditionedTLR3biology.proteinRNAEctopic expressionExperimental cell research
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Water-Soluble Chlorophyll Protein (WSCP) Stably Binds Two or Four Chlorophylls

2017

Water-soluble chlorophyll proteins (WSCPs) of class IIa from Brassicaceae form tetrameric complexes containing one chlorophyll (Chl) per apoprotein but no carotenoids. The complexes are remarkably stable toward dissociation and protein denaturation even at 100 °C and extreme pH values, and the Chls are partially protected against photooxidation. There are several hypotheses that explain the biological role of WSCPs, one of them proposing that they function as a scavenger of Chls set free upon plant senescence or pathogen attack. The biochemical properties of WSCP described in this paper are consistent with the protein acting as an efficient and flexible Chl scavenger. At limiting Chl concen…

ChlorophyllModels Molecular0106 biological sciences0301 basic medicineProtein DenaturationHot TemperatureLightLight-Harvesting Protein ComplexesGene ExpressionThylakoids01 natural sciencesBiochemistryProtein Structure SecondaryDissociation (chemistry)law.inventionchemistry.chemical_compoundlawpolycyclic compoundsDenaturation (biochemistry)CarotenoidPlant Proteinschemistry.chemical_classificationSinglet OxygenProtein Stabilityfood and beveragesHydrogen-Ion ConcentrationBiochemistryRecombinant DNAOxidation-ReductionProtein BindingRecombinant Fusion ProteinsBrassicamacromolecular substancesBiology03 medical and health sciencesProtein DomainsTetramerPlant senescenceChlorophyll APeasWaterOxygen030104 developmental biologyWater solubleSolubilitychemistryChlorophyllProtein MultimerizationApoproteins010606 plant biology & botanyBiochemistry
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The Folding State of the Lumenal Loop Determines the Thermal Stability of Light-Harvesting Chlorophyll a/b Protein

2004

The major light-harvesting protein of photosystem II (LHCIIb) is the most abundant chlorophyll-binding protein in the thylakoid membrane. It contains three membrane-spanning alpha helices; the first and third one closely interact with each other to form a super helix, and all three helices bind most of the pigment cofactors. The protein loop domains connecting the alpha helices also play an important role in stabilizing the LHCIIb structure. Single amino acid exchanges in either loop were found to be sufficient to significantly destabilize the complex assembled in vitro [Heinemann, B., and Paulsen, H. (1999) Biochemistry 38, 14088-14093. Mick, V., Eggert, K., Heinemann, B., Geister, S., and…

ChlorophyllProtein DenaturationProtein FoldingPhotosystem IILight-Harvesting Protein ComplexesBiochemistryProtein structureTrypsinPlant Proteinschemistry.chemical_classificationChemistryChlorophyll AHydrolysisPeasTemperaturePhotosystem II Protein ComplexSodium Dodecyl SulfateProtein Structure TertiaryAmino acidKineticsCrystallographyAmino Acid SubstitutionMembrane proteinThylakoidHelixBiophysicsElectrophoresis Polyacrylamide GelProtein foldingAlpha helixBiochemistry
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