Search results for " Spin"

showing 10 items of 1036 documents

The structure of pumice: An XPS and27Al MAS NMR study

1992

In order to investigate the surface structure of pumice, an amorphous aluminosilicate, samples of pumice and of standards of silica and alumina have been studied by x-ray photoelectron spectroscopy (XPS). The effect of a mild acid leaching was also considered. The analysis of the Si 2p, Al 2p and O 1s photoelectron peaks and the Si KLL and O KLL Auger peaks indicated that pumice is formed by tetrahedral silica with some units being replaced by aluminate, AlO2−. The acid treatment decreases the alkali and the aluminate ions. X-ray photoelectron spectra of the valence band of pumices and of standards of Al2O3 and SiO2 agree with the core-level results. To support the conclusions from the XPS …

ChemistryAluminateAnalytical chemistrychemistry.chemical_elementSurfaces and InterfacesGeneral ChemistryCondensed Matter PhysicsAlkali metalSurfaces Coatings and FilmsAmorphous solidchemistry.chemical_compoundNuclear magnetic resonanceX-ray photoelectron spectroscopyAluminiumAluminosilicatePumiceMaterials ChemistryMagic angle spinningSurface and Interface Analysis
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Experimental evidence of E’_gamma centers generation from oxygen vacancies in a-SiO2

2007

Abstract We report on the thermal treatment effects in a γ-ray irradiated oxygen deficient amorphous silicon dioxide (a-SiO2) containing Al impurities. We observed that by thermal treatments the intensity of the 7.6 eV optical absorption band, associated to an oxygen deficient center, and the EPR signal amplitude of irradiation induced [AlO4]0 centers gradually decrease. During these thermal treatments, the E γ ′ centers concentration is found to increase in a correlated way to the decrease of the 7.6 eV absorption amplitude. These results are interpreted assuming an hole-transfer process from the [AlO4]0 centers to the diamagnetic oxygen vacancies, resulting in the generation of E γ ′ cent…

ChemistryAnalytical chemistryOptical spectroscopychemistry.chemical_elementSilicaThermal treatmentCondensed Matter PhysicsOxygenElectronic Optical and Magnetic Materialslaw.inventionAbsorptionlawAbsorption bandImpurityElectron spin resonanceMaterials ChemistryCeramics and CompositesDiamagnetismDefectsIrradiationAtomic physicsElectron paramagnetic resonanceAbsorption (electromagnetic radiation)
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More insight into characterization of the waterlogged wooden part of Acqualadroni Roman Rostrum by solid-state NMR

2016

Abstract Solid-state NMR spectroscopy was applied to characterize the wooden part of a roman Rostrum recovered in the Tyrrhenian Sea in the Acqualadroni area (Messina, Italy). The Acqualadroni Rostrum has been, in the recent past, investigated to establish its provenance and conservation. In this paper, solid-state NMR was used to obtain information on the conservation state of the wood as a preliminary step for the conservation process. A wooden sample of this artifact, collected by coring, was divided in four parts in order to correlate the conservation state to the depth. Results were compared with those obtained for a modern wood of the same species. A structural study was performed by …

ChemistryNaval ramRostrum010401 analytical chemistryCondensationRostrumAnalytical chemistryMineralogy02 engineering and technologyNuclear magnetic resonance spectroscopy021001 nanoscience & nanotechnologySolid-state NMR01 natural sciencesCoring0104 chemical sciencesAnalytical ChemistryCharacterization (materials science)chemistry.chemical_compoundSolid-state nuclear magnetic resonanceMagic angle spinningLignin0210 nano-technologySpectroscopyWaterlogged woodSettore CHIM/02 - Chimica FisicaMicrochemical Journal
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Site-Specific Information on Membrane Protein Folding by Electron Spin Echo Envelope Modulation Spectroscopy

2010

Compared to folding of soluble proteins, folding of membrane proteins is complicated by the fact that it requires an amphiphilic environment. Few existing techniques can provide structurally resolved information on folding kinetics. For the major plant light harvesting complex LHCII, it is demonstrated that changes in water accessibility of a particular amino acid residue can be followed during folding by measuring the hyperfine interaction of spin labels with deuterium nuclei of heavy water. The incorporation of residue 196 into the hydrophobic core of a detergent micelle was investigated. The technique provides a time constant that is similar to the one found with fluorescence spectroscop…

ChemistryPhi value analysisSite-directed spin labelinglaw.inventionFolding (chemistry)CrystallographylawLattice proteinBiophysicsGeneral Materials ScienceProtein foldingDownhill foldingPhysical and Theoretical ChemistryElectron paramagnetic resonanceSpin labelThe Journal of Physical Chemistry Letters
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Accessibility of Protein-Bound Chlorophylls Probed by Dynamic Electron Polarization

2018

The possibility to probe the accessibility of sites of proteins represents an important point to explore their interactions with specific substrates in solution. The dynamic electron polarization of nitroxide radicals induced by excited triplet states of organic molecules is a phenomenon that is known to occur in aqueous solutions. The interaction within the radical-triplet pair causes a net emissive dynamic electron polarization of the nitroxide radical, that can be detected by means of time-resolved electron paramagnetic resonance (TR-EPR) spectroscopy. We have exploited this effect to prove the accessibility of chlorophylls bound to a protein, namely, the water-soluble chlorophyll protei…

Chlorophyll0301 basic medicineNitroxide mediated radical polymerizationFree RadicalsRadicalElectron010402 general chemistry01 natural scienceslaw.inventionElectron Transport03 medical and health scienceslawGeneral Materials SciencePhysical and Theoretical ChemistryPolarization (electrochemistry)Electron paramagnetic resonanceSpectroscopyChemistryElectron Spin Resonance SpectroscopyProteinsChlorophyll; Electron Spin Resonance Spectroscopy; Electron Transport; Free Radicals; Nitrogen Oxides; Protein Binding; Proteins0104 chemical sciences030104 developmental biologyChemical physicsExcited stateNitrogen OxidesProtein BindingMacromoleculeThe Journal of Physical Chemistry Letters
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Early folding events during light harvesting complex II assembly in vitro monitored by pulsed electron paramagnetic resonance

2016

Efficient energy transfer in the major light harvesting complex II (LHCII) of green plants is facilitated by the precise alignment of pigments due to the protein matrix they are bound to. Much is known about the import of the LHCII apoprotein into the chloroplast via the TOC/TIC system and its targeting to the thylakoid membrane but information is sparse about when and where the pigments are bound and how this is coordinated with protein folding. In vitro, the LHCII apoprotein spontaneously folds and binds its pigments if the detergent-solubilized protein is combined with a mixture of chlorophylls a and b and carotenoids. In the present work, we employed this approach to study apoprotein fo…

ChlorophyllModels Molecular0301 basic medicineProtein FoldingPigment bindingLight-Harvesting Protein ComplexesBiophysicsBiochemistrylaw.invention03 medical and health scienceslawElectron paramagnetic resonancePlant ProteinsPulsed EPRChemistryElectron Spin Resonance SpectroscopyPeasPhotosystem II Protein ComplexCell BiologyProtein tertiary structureProtein Structure TertiaryChloroplastFolding (chemistry)KineticsCrystallography030104 developmental biologyEnergy TransferThylakoidProtein foldingApoproteinsProtein BindingBiochimica et Biophysica Acta (BBA) - Bioenergetics
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Localization of the N-terminal Domain in Light-harvesting Chlorophyll a/b Protein by EPR Measurements

2005

The conformational distribution of the N-terminal domain of the major light-harvesting chlorophyll a/b protein (LHCIIb) has been characterized by electron-electron double resonance yielding distances between spin labels placed in various domains of the protein. Distance distributions involving residue 3 near the N terminus turned out to be bimodal, revealing that this domain, which is involved in regulatory functions such as balancing the energy flow through photosystems (PS) I and II, exists in at least two conformational states. Models of the conformational sub-ensembles were generated on the basis of experimental distance restraints from measurements on LHCIIb monomers and then checked f…

ChlorophyllModels MolecularThreonineConformational changeTime FactorsLightMacromolecular SubstancesProtein ConformationPhotosynthetic Reaction Center Complex ProteinsLight-Harvesting Protein ComplexesElectronsTrimerCrystallography X-RayThylakoidsBiochemistryProtein Structure Secondarylaw.inventionResidue (chemistry)chemistry.chemical_compoundlawEscherichia coliAnimalsPhosphorylationAnnexin A4Electron paramagnetic resonanceMolecular BiologyPhotosystemPhotosystem I Protein ComplexChemistryChlorophyll AElectron Spin Resonance SpectroscopyPeasPhotosystem II Protein ComplexCell BiologyRecombinant ProteinsProtein Structure TertiaryOxygenN-terminusCrystallographyMonomerThylakoidMutationCattleSpin LabelsDimerizationJournal of Biological Chemistry
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Impact of acidic/hydrothermal treatment on pore structural and chromatographic properties of porous silicas

1991

Abstract A series of commercial silicas and a laboratory made product were subjected to acidic/hydrothermal treatment with solutions of HCI, HNO3, H2SO4 and HF. The concentration of acid and the temperature and duration of treatment were varied. The specific surface area, content of metal impurities, types and concentration of surface hydroxyl and siloxane groups and crystallinity were determined for native and treated silicas. Only changes in the structural order of the surface could be assessed by means of 19Si cross-polarization magic angle spinning NMR spectrometry and electron diffraction. The native and acid-treated silicas were surface modified to n-octyl derivatives and tested under…

ChromatographyChemistryOrganic ChemistryKineticsGeneral MedicineReversed-phase chromatographyBiochemistryAnalytical ChemistryCrystallinitychemistry.chemical_compoundElectron diffractionSiloxaneSpecific surface areaMagic angle spinningPorosityJournal of Chromatography A
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Characterisation of phenolic compounds in Algerian honeys by RP-HPLC coupled to electrospray time-of-flight mass spectrometry

2017

Abstract A total of 35 honey samples from different regions of Algeria were studied to determine their phenolic profiles. Phenolic compounds, products of the secondary metabolism of plants, were extracted with amberlite XAD-4 and analysed by liquid chromatography, with diode array detection and electrospray ionisation mass spectrometry in negative ion polarity. By using colorometric assays, Erica honeys showed the highest content of phenolic compounds and flavonoids (245 ± 54 mg GAE/100 g and 29 ± 6 mg QE/100 g, respectively). More than 30 compounds were identified in the honey samples studied including 14 phenolic acids and 16 flavonoids. In general, honey samples showed different chromato…

ChromatographyPinocembrinCapparis spinosa010401 analytical chemistry04 agricultural and veterinary sciencesCoumaric acidMass spectrometry040401 food science01 natural sciencesfood.food0104 chemical sciencesGalanginchemistry.chemical_compound0404 agricultural biotechnologyfoodchemistryMyricetinKaempferolIsorhamnetinFood ScienceLWT - Food Science and Technology
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Electron paramagnetic resonance (EPR) spin trapping of biological nitric oxide

2007

Nitric oxide (NO) is a free radical species with multiple physiological functions. Because of low concentrations and short half-life of NO, its direct measurement in living tissues remains a difficult task. Electron paramagnetic resonance (EPR) spin trapping is probably one of the best suitable platforms for development of new methods for quantification of biological NO. The most reliable EPR-based approaches developed so far are based on the reaction of NO with various iron complexes, both intrinsic and exogenously applied. This review is focused on the current state and perspectives of EPR spin trapping for experimental and clinical NO biology.

ChromatographySpin trappingIronClinical BiochemistryElectron Spin Resonance SpectroscopyCell BiologyGeneral MedicineNitric OxidePhotochemistryBiochemistryAnalytical ChemistryNitric oxidelaw.inventionchemistry.chemical_compoundEpr spin trappingNuclear magnetic resonancechemistryThiocarbamateslawAnimalsHumansElectron paramagnetic resonanceSpin TrappingVolume concentrationJournal of Chromatography B
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