Search results for "Electron Spin Resonance Spectroscopy"

showing 10 items of 125 documents

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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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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Aß(25-35) and its C-and/or N-blocked derivatives: copper driven structural features and neurotoxicity

2006

The toxic properties of beta-amyloid protein, Abeta(1-42), the major component of senile plaques in Alzheimer's disease, depend on nucleation-dependent oligomerization and aggregation. In addition, Abeta(1-42) toxicity is favored by the presence of trace metals, which affect the secondary structure of the peptide. A peptide comprising 11 residues within Abeta(1-42) [Abeta(25-35)] aggregates and retains the neurotoxic activity of Abeta(1-42). We have used both Abeta(25-35) and its C-amidated or N-acetylated/C-amidated derivatives to investigate the role of copper(II) in modulating the conformation and aggregation state as well as the neurotoxic properties of amyloid peptides. Electrospray io…

Circular dichroismSpectrometry Mass Electrospray IonizationAmyloidProtein Conformationb-amyloidNeurotoxinsPeptideMicroscopy Atomic ForceCellular and Molecular NeuroscienceProtein structuremental disordersmedicineAnimalsSenile plaqueschemistry.chemical_classificationCerebral CortexNeuronsAmyloid beta-PeptidesCircular DichroismCopper toxicityNeurotoxicityP3 peptideElectron Spin Resonance SpectroscopyAlzheimer's diseasemedicine.diseasePeptide Fragmentsnervous system diseasesRatschemistryBiochemistrycopperModels AnimalBiophysicsAlzheimer’s disease
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Field-Induced Slow Magnetic Relaxation in a Mononuclear Manganese(III)-Porphyrin Complex

2015

We report on a novel manganese(III)-porphyrin complex with the formula [Mn(III) (TPP)(3,5-Me2 pyNO)2 ]ClO4 ⋅CH3 CN (2; 3,5-Me2 pyNO=3,5-dimethylpyridine N-oxide, H2 TPP=5,10,15,20-tetraphenylporphyrin), in which the Mn(III) ion is six-coordinate with two monodentate 3,5-Me2 pyNO molecules and a tetradentate TPP ligand to build a tetragonally elongated octahedral geometry. The environment in 2 is responsible for the large and negative axial zero-field splitting (D=-3.8 cm(-1) ), low rhombicity (E/|D|=0.04) of the high-spin Mn(III) ion, and, ultimately, for the observation of slow magnetic-relaxation effects (Ea =15.5 cm(-1) at H=1000 G) in this rare example of a manganese-based single-ion ma…

DenticityPorphyrinsMetalloporphyrinsPyridineschemistry.chemical_elementManganese010402 general chemistryCrystallography X-RayLigands01 natural sciencesCatalysisIonlaw.inventionchemistry.chemical_compoundlawOctahedral molecular geometryMoleculeElectron paramagnetic resonanceComputingMilieux_MISCELLANEOUS[PHYS]Physics [physics]Manganese010405 organic chemistryLigandOrganic ChemistryElectron Spin Resonance SpectroscopyTemperatureGeneral ChemistryPorphyrin0104 chemical sciencesCrystallographychemistryMagnets
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Pulsed EPR determination of water accessibility to spin-labeled amino acid residues in LHCIIb.

2009

Membrane proteins reside in a structured environment in which some of their residues are accessible to water, some are in contact with alkyl chains of lipid molecules, and some are buried in the protein. Water accessibility of residues may change during folding or function-related structural dynamics. Several techniques based on the combination of pulsed electron paramagnetic resonance (EPR) with site-directed spin labeling can be used to quantify such water accessibility. Accessibility parameters for different residues in major plant light-harvesting complex IIb are determined by electron spin echo envelope modulation spectroscopy in the presence of deuterated water, deuterium contrast in …

DetergentsBiophysicsLight-Harvesting Protein ComplexesSpectroscopy Imaging and Other TechniquesBuffersCrystallography X-RaySpectral linelaw.inventionlawMoleculeHumansAmino AcidsElectron paramagnetic resonanceProtein Structure QuaternaryHyperfine structureAlkylPlant Proteinschemistry.chemical_classificationPulsed EPRChemistryElectron Spin Resonance SpectroscopyPeasTemperatureWaterSite-directed spin labelingCrystallographyDeuteriumSolubilityMutationSolventsSpin LabelsProtein MultimerizationBiophysical journal
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ESR Spectra o f Normal Human Serum after Treatment with Complement Activating Agents*

1980

Abstract We describe the appearance of a free-radical signal in the ESR spectrum of normal human serum incubated with several complement activating agents. The intensity of this signal is dependent of dose of activating agents, time and temperature. Signals elicited by different complement activators differ in morphology and kinetics. Inhibition by treatment with EDTA and the presence of the signal in activated C 6-deficient rabbit serum suggest that the con-vertase forming steps of complement activation (C2 to 5) could be the source of free-radical containing molecules.

Elapid VenomsMaleFree RadicalsChemistryKineticsElectron Spin Resonance SpectroscopyZymosanBlood ProteinsComplement System ProteinsGeneral Biochemistry Genetics and Molecular BiologyComplement systemComplement (complexity)Esr spectraBiochemistryHumansFemaleComplement ActivationAfter treatmentZeitschrift für Naturforschung C
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Cryogenic 35GHz pulse ENDOR probehead accommodating large sample sizes: Performance and applications.

2009

The construction and performance of a cryogenic 35GHz pulse electron nuclear double resonance (ENDOR) probehead for large samples is presented. The resonator is based on a rectangular TE(102) cavity in which the radio frequency (rf) B(2)-field is generated by a two turn saddle ENDOR coil crossing the resonator along the sample axis with minimal distance to the sample tube. An rf power efficiency factor is used to define the B(2)-field strength per square-root of the transmitted rf power over the frequency range 2-180MHz. The distributions of the microwave B(1)- and E(1)-field, and the rf B(2)-field are investigated by electromagnetic field calculations. All dielectrics, the sample tube, and…

Electromagnetic fieldNuclear and High Energy PhysicsIndolesPorphyrinsLarge sample resonatorGlycineBiophysicsAnalytical chemistryIsoindolesPulse EPRHeliumBiochemistryResonatorElectromagnetic FieldsOpticsQ-band probeheadMetalloproteinsOrganometallic CompoundsComputer SimulationElectron nuclear double resonanceChemistryPulsed EPRbusiness.industryRF power amplifierElectron Spin Resonance SpectroscopyENDORCondensed Matter PhysicsSettore FIS/07 - Fisica Applicata(Beni Culturali Ambientali Biol.e Medicin)Cold TemperatureCoalENDOR resonatorElectromagnetic coilRadio frequencybusinessAlgorithmsMicrowaveJournal of magnetic resonance (San Diego, Calif. : 1997)
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Measurement of white wines resistance against oxidation by Electron Paramagnetic Resonance spectroscopy

2018

International audience; Free radical theory of aging hypothesizes that oxygen-derived radicals are responsible for the storage-related flavor instability in wine. In an optimal situation, a balanced-distribution exists between oxidants and antioxidants among wines intrinsic/extrinsic metabolites. Based on the kinetic study of POBN-1-hydroxyethyl spin adduct (POBN-1-HER) formation in wines initiated via the Fenton reaction, a novel tool based on EPR spin trapping methodology was developed to quantify wines resistance against oxidation. Antioxidant capacities of wines were evaluated according to POBN-1-HER maximum signal intensity (Imax POBN-1-HER) and rate formation (r(POBN-1-HER)) kinetic p…

Electron paramagnetic resonance spectroscopyAntioxidantFree Radicalssulfur-dioxidemedicine.medical_treatmentRadicalWinePhotochemistry01 natural sciencesAnalytical ChemistryAdductlaw.invention0404 agricultural biotechnologylaw[SDV.IDA]Life Sciences [q-bio]/Food engineeringmedicineAging potentialElectron paramagnetic resonanceFlavorFree-radical theory of agingdegradationWineparametersChemistryfree-radical generation010401 analytical chemistryRadical chemistryElectron Spin Resonance Spectroscopyfood and beveragesPolyphenolstemperature04 agricultural and veterinary sciencesGeneral Medicine040401 food science0104 chemical sciencescolorElectron Paramagnetic ResonancearomaSulfur dioxideidentificationSpin Labelsepr spectroscopyOxidation-ReductionFood Science
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Ligand-Binding Cooperativity Effects in Polymer-Protein Conjugation.

2019

We present an electron paramagnetic resonance (EPR) spectroscopic characterization of structural and dynamic effects that stem from post-translational modifications of bovine serum albumin (BSA), an established model system for polymer-protein conjugation. Beyond the typical drug delivery and biocompatibility aspect of such systems, we illustrate the causes that alter internal dynamics and therefore functionality in terms of ligand-binding to the BSA protein core. Uptake of the paramagnetic fatty acid derivative 16-doxyl stearic acid by several BSA-based squaric acid macroinitiators and polymer-protein conjugates was studied by EPR spectroscopy, aided by dynamic light scattering (DLS) and z…

Ethylene GlycolPolymers and PlasticsPolymersBioengineeringCooperativity02 engineering and technology010402 general chemistryLigands01 natural scienceslaw.inventionPolyethylene GlycolsBiomaterialsCyclic N-Oxideschemistry.chemical_compoundDrug Delivery SystemsDynamic light scatteringlawMaterials ChemistryZeta potentialBovine serum albuminElectron paramagnetic resonanceBinding SitesbiologyElectron Spin Resonance SpectroscopySerum Albumin Bovine021001 nanoscience & nanotechnologyLigand (biochemistry)Dynamic Light Scattering0104 chemical scienceschemistrybiology.proteinBiophysicsSurface modificationMethacrylates0210 nano-technologyEthylene glycolBiomacromolecules
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