Search results for "circular"

showing 10 items of 856 documents

Neighbor-Distinguishing k-tuple Edge-Colorings of Graphs

2009

AbstractThis paper studies proper k-tuple edge-colorings of graphs that distinguish neighboring vertices by their sets of colors. Minimum numbers of colors for such colorings are determined for cycles, complete graphs and complete bipartite graphs. A variation in which the color sets assigned to edges have to form cyclic intervals is also studied and similar results are given.

Circular coloringComputingMethodologies_IMAGEPROCESSINGANDCOMPUTERVISION0102 computer and information sciences[INFO.INFO-DM]Computer Science [cs]/Discrete Mathematics [cs.DM]01 natural sciencesGraphTheoretical Computer ScienceCombinatoricsGreedy coloringIndifference graphChordal graphDiscrete Mathematics and Combinatorics0101 mathematicsFractional coloringComputingMilieux_MISCELLANEOUSComputingMethodologies_COMPUTERGRAPHICSMathematicsDiscrete mathematicsk-tuple edge-coloringClique-sum010102 general mathematics[ INFO.INFO-DM ] Computer Science [cs]/Discrete Mathematics [cs.DM]1-planar graphMetric dimension010201 computation theory & mathematicsIndependent setMaximal independent setNeighbor-distinguishingMathematicsofComputing_DISCRETEMATHEMATICSAdjacent vertex-distinguishing
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How copper ions and membrane environment influence the structure of the human and chicken tandem repeats domain?

2019

Abstract Prion proteins (PrPs) from different species have the enormous ability to anchor copper ions. The N-terminal domain of human prion protein (hPrP) contains four tandem repeats of the –PHGGGWGQ– octapeptide sequence. This octarepeat domain can bind up to four Cu2+ ions. Similarly to hPrP, chicken prion protein (chPrP) is able to interact with Cu2+ through the tandem hexapeptide -HNPGYP- region (residues 53–94). In this work, we focused on the human octapeptide repeat (human Octa4, hPrP60–91) (Ac-PHGGGWGQPHGGGWGQPHGGGWGQPHGGGWGQ-NH2) and chicken hexapeptide repeat (chicken Hexa4, chPrP54–77) (Ac-HNPGYPHNPGYPHNPGYPHNPGYP-NH2) prion protein fragments. Due to the fact that PrP is a membr…

Circular dichroism010402 general chemistry01 natural sciencesBiochemistryMicelleInorganic Chemistrychemistry.chemical_compoundMembrane LipidsTandem repeatPeptide bondAnimalsHumansAmino Acid SequenceSodium dodecyl sulfateLipid bilayerMembrane mimicking environmentMicelleschemistry.chemical_classification010405 organic chemistryChemistryCopper ionsSodium Dodecyl SulfateHistidine residues0104 chemical sciencesPrion proteinsMembraneTandem Repeat SequencesBiophysicsPotentiometryThermodynamicsGlycoproteinChickensCopper
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Fluorescence and circular dichroism spectroscopy to understand the interactions between cyclodextrins and α-galactosidase from green coffee beans

2017

Abstract The potential of fluorescence measurement and circular dichroism spectroscopy (CDSP) to evaluate the interaction between cyclodextrins (CDs) (CD cavity size, concentration, pH, reaction time, and temperature as well as different side chain groups) and α-galactosidase was evaluated. A strong relationship was observed between α-galactosidase fluorescence intensity and CD cavity size, concentration, pH, reaction time, and temperature as well as different side chain groups. Therefore, it can be concluded that fluorescence intensity measurement can be a promising tool to ascertain β-CD-α-galactosidase interactions. CDSP is also an interesting tool to understand β-CD-α-galactosidase inte…

Circular dichroism010405 organic chemistryChemistryAnalytical chemistry010402 general chemistryPhotochemistry01 natural sciencesBiochemistryFluorescence0104 chemical sciencesFluorescence intensityα galactosidaseSide chainGreen coffeeProtein secondary structureInhibitory effectFood ScienceFood Bioscience
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Secondary metabolites from the aerial parts of Cytisus villosus Pourr

2017

Phytochemical investigation of the aerial parts of Cytisus villosus Pourr. resulted in the isolation and characterization of a new isoflavan, (3S, 4S)-2′,4′-dihydroxy-3′-methoxy-6,7-methylenedioxyisoflavan- 4-ol (1), and a new monoterpene, (4R,6S)-4-hydroxy-2,2,6-trimethyl-9-oxabicyclo [4.2.1] non-1(8)-en-7-one (2), together with four known flavonoids: geinstein (3), chrysin (4), chrysin -7-O-β-D-glucopyranoside (5) and 2″-O-α-L-rhamnosylorientin (6). The structures of the new compounds were elucidated on the basis of extensive spectroscopic analysis, including 1D, 2D NMR ((1)H, (13)C, COSY, TOCSY, HMBC and HSQC) and HRESIMS. The absolute configurations of 1 and 2 were established by the co…

Circular dichroism010405 organic chemistryStereochemistryMonoterpeneCytisus villosusPlant Science010402 general chemistryCytisus villosus01 natural sciencesBiochemistryisoflavonoidsArticle0104 chemical scienceschemistry.chemical_compoundchemistryPhytochemicalECDChrysinmonoterpenoidsAgronomy and Crop ScienceTwo-dimensional nuclear magnetic resonance spectroscopyBiotechnologyPhytochemistry Letters
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Unveiling Electronic Transitions in Three Novel Chiral Azo-Compounds Using Linear and Nonlinear Circular Dichroism: A Theoretical−Experimental Study

2011

Herein, we report on the experimental and theoretically study of the linear absorption, electronic circular dichroism (ECD) spectra, as well as the two-photon absorption circular-linear dichroism measurements of three different chiral azo derivatives in dimethylsulfoxide solution. Using potential energy surfaces and frontier orbital analysis, we established the most stable conformation for each molecule and elucidated their different electronic transitions. Our theoretical calculations allowed us to unambiguously identify the spectral position of such transitions and correlate them with the spectral profiles observed in the two-photon absorption spectra. To further elucidate the characteris…

Circular dichroismAbsorption spectroscopyChemistryAnalytical chemistryPhysics::OpticsDichroismLinear dichroismMolecular physicsSpectral lineAtomic electron transitionMoleculePhysical and Theoretical ChemistryAbsorption (electromagnetic radiation)ta116The Journal of Physical Chemistry A
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Circular dichroism of magnetically induced transitions for D 2 lines of alkali atoms

2018

In this letter we study magnetic circular dichroism in alkali atoms exhibiting asymmetric behaviour of magnetically induced transitions. The magnetic field induces transitions between hyperfine levels of alkali atoms and in the range of magnetic field, the intensities of these transitions experience significant enhancement. We have inferred a general rule applicable for the D 2 lines of all alkali atoms, that is the transition intensity enhancement is around four times larger for the case of than for excitation for , whereas it is several hundreds of thousand times larger in the case of than that for polarization for . This asymmetric behaviour results in circular dichroism. For experimenta…

Circular dichroismAlkali atomsMaterials scienceMagnetic circular dichroismGeneral Physics and AstronomyParity (physics)01 natural sciencesMolecular physicsMagnetic field010309 opticsLaser linewidth0103 physical sciencesPhysics::Atomic Physics010306 general physicsHyperfine structureExcitationEPL (Europhysics Letters)
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Entrapment of A Beta 1-40 peptide in unstructured aggregates

2012

Recognizing the complexity of the fibrillogenesis process provides a solid ground for the development of therapeutic strategies aimed at preventing or inhibiting protein-protein aggregation. Under this perspective, it is meaningful to identify the possible aggregation pathways and their relative products. We found that Aβ-peptide dissolved in a pH 7.4 solution at small peptide concentration and low ionic strength forms globular aggregates without typical amyloid β-conformation. ThT binding kinetics was used to monitor aggregate formation. Circular dichroism spectroscopy, AFM imaging, static and dynamic light scattering were used for structural and morphological characterization of the aggre…

Circular dichroismAmyloidKineticsPeptideProtein Structure SecondaryFIBRIL FORMATIONDynamic light scatteringMEMBRANE DISRUPTIONGeneral Materials ScienceFiberATOMIC-FORCE MICROSCOPYchemistry.chemical_classificationAmyloid beta-PeptidesChemistryProtein StabilityOsmolar ConcentrationTemperatureFibrillogenesisCondensed Matter PhysicsReceptor–ligand kineticsPeptide FragmentsAMYLOID-BETA-PROTEINALZHEIMERS-DISEASECrystallographyKineticsSpectrometry FluorescenceBiophysicsProtein Multimerization
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Amyloid fibrils formation and amorphous aggregation in Concanavalin A

2007

We here report an experimental study on the thermal aggregation process of concanavalin A, a protein belonging to the legume lectins family. The aggregation process and the involved conformational changes of the protein molecules were followed by means of fluorescence techniques, light scattering, circular dichroism, zeta potential measurements and atomic force microscopy. Our results show that the aggregation process of concanavalin A may evolve through two distinct pathways leading, respectively, to the formation of amyloids or amorphous aggregates. The relative extent of the two pathways is determined by pH, as amyloid aggregation is favored at high pH values ( approximately 9), while th…

Circular dichroismAmyloidLightBiophysicsProtein aggregationCircular dichroismMicroscopy Atomic ForceBiochemistryFluorescenceAtomic force microscopyZeta potentialConcanavalin AScattering RadiationBenzothiazolesProtein Structure QuaternaryFluorescent DyesbiologyChemistryAtomic force microscopyOrganic ChemistryThioflavin T fluorescenceHydrogen-Ion ConcentrationAmyloid fibrilFluorescenceAmorphous solidKineticsThiazolesCrystallographyConcanavalin Abiology.proteinProtein aggregation
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Irreversible formation of intermediate BSA oligomers requires and induces conformational changes.

2004

Understanding the relation between protein conformational changes and aggregation, and the physical mechanisms leading to such processes, is of primary importance, due to its direct relation to a vast class of severe pathologies. Growing evidence also suggests that oligomeric intermediates, which may occur early in the aggregation pathway, can be themselves pathogenic. The possible cytotoxicity of oligomers of non-disease-associated proteins adds generality to such suggestion and to the interest of studies of oligomer formation. Here we study the early stages of aggregation of Bovine Serum Albumin (BSA), a non pathogenic protein which has proved to be a useful model system. Dynamic light sc…

Circular dichroismAmyloidLightStereochemistryProtein ConformationProtein aggregationProcess interactionFibrilBiochemistryOligomerProtein Structure Secondarychemistry.chemical_compoundDynamic light scatteringStructural BiologyAnimalsScattering RadiationBovine serum albuminMolecular BiologybiologyCircular DichroismTemperatureSerum Albumin BovineKineticschemistrybiology.proteinCattleProteins
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Protein/lipid coaggregates are formed during α-synuclein-induced disruption of lipid bilayers.

2014

Amyloid formation is associated with neurodegenerative diseases such as Parkinson's disease (PD). Significant α-synuclein (αSN) deposition in lipid-rich Lewy bodies is a hallmark of PD. Nonetheless, an unraveling of the connection between neurodegeneration and amyloid fibrils, including the molecular mechanisms behind potential amyloid-mediated toxic effects, is still missing. Interaction between amyloid aggregates and the lipid cell membrane is expected to play a key role in the disease progress. Here, we present experimental data based on hybrid analysis of two-photon-microscopy, solution small-angle X-ray scattering and circular dichroism data. Data show in real time changes in liposome …

Circular dichroismAmyloidPolymers and PlasticsAmyloidLipid BilayersBioengineeringProtein Structure SecondaryBiomaterialsCell membraneMaterials ChemistrymedicineScattering RadiationLipid bilayerSpectroscopyLiposomeLaurdanAdvanced MicroscopyChemistryCircular DichroismX-RaysNeurodegenerationCell MembraneLipid bilayer fusionProteinsmedicine.diseaseamyloid-membrane interactionco-aggregatemedicine.anatomical_structureMembraneBiophysicsalpha-SynucleinLewy BodiesBiomacromolecules
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