Search results for "OMOP"

showing 10 items of 624 documents

Site-by-site tracking of signal transduction in an azidophenylalanine-labeled bacteriophytochrome with step-scan FTIR spectroscopy

2021

Signal propagation in photosensory proteins is a complex and multidimensional event. Unraveling such mechanisms site-specifically in real time is an eligible but a challenging goal. Here, we elucidate the site-specific events in a red-light sensing phytochrome using the unnatural amino acid azidophenylalanine, vibrationally distinguishable from all other protein signals. In canonical phytochromes, signal transduction starts with isomerization of an excited bilin chromophore, initiating a multitude of processes in the photosensory unit of the protein, which eventually control the biochemical activity of the output domain, nanometers away from the chromophore. By implementing the label in pri…

Models MolecularAzidesProtein ConformationPhenylalaninespektroskopiaTongue regionGeneral Physics and Astronomyfotobiologia010402 general chemistryTracking (particle physics)01 natural sciences03 medical and health scienceschemistry.chemical_compoundBacterial ProteinsSpectroscopy Fourier Transform InfraredAmino Acid SequenceAmino AcidsPhysical and Theoretical ChemistryFourier transform infrared spectroscopyBilin030304 developmental biology0303 health sciencesBinding SitesStaining and LabelingbiologyPhytochromeChemistryDeinococcus radioduransChromophorePhotochemical Processesbiology.organism_classification0104 chemical sciencesKineticsBiophysicsPhytochromeproteiinitvalokemiaSignal transductionProtein BindingSignal TransductionPhysical Chemistry Chemical Physics
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Synthesis, Crystal Structure, Magnetic Properties, and Theoretical Studies of [{Cu(mepirizole)Br}2(μ-OH)(μ-pz)] (Mepirizole = 4-Methoxy-2-(5-methoxy-…

2003

A novel mu-pyrazolato-mu-hydroxo-dibridged copper(II) complex has been synthesized and structurally characterized: [(Cu(mepirizole)Br)2(mu-OH)(mu-pz)] (mepirizole=4-methoxy-2-(5-methoxy-3-methyl-1H-pyrazol-1-yl)-6-methylpyrimidine; pz=pyrazolate). The title compound crystallizes in the monoclinic system, space group P2(1)/c, with a=15.618(2) A, b=15.369(3) A, c=16.071(3) A, and beta=112.250(1) degrees. The structure is built up of dinuclear [(Cu(mepirizole)Br)2(mu-OH)(mu-pz)] units with five-coordinated copper(II) ions (CuBrN3O chromophores) linked by mu2-OH and mu2-pyrazolato bridges that are well separated from each others. The intramolecular copper-copper distance is 3.378(3) A. Magnetic…

Models MolecularChemical PhenomenaChemistry PhysicalBand gapStereochemistryIronchemistry.chemical_elementCrystal structureChromophoreCrystallography X-RayLigandsCopperMagnetic susceptibilityIonInorganic ChemistryMagneticsCrystallographychemistryIntramolecular forceIndicators and ReagentsEpirizolePhysical and Theoretical ChemistryMonoclinic crystal systemInorganic Chemistry
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Metamorphosis of a butterfly: synthesis, structural, thermal, magnetic and DFT characterisation of a ferromagnetically coupled tetranuclear copper(ii…

2007

The reaction in water of Cu(OH)(2) with 2,2'-bipyridine (bipy) and (NH(4))(2)HPO(4) in a 4 : 4 : 2 molar ratio under an inert atmosphere leads to the formation of a tetranuclear copper(II) complex of formula {[(H(2)O)(2)Cu(4)(bipy)(4)(mu(4)-PO(4))(2)(mu(2)-OH)] x 0.5 HPO(4) x 15.5 H(2)O}, 1, with butterfly topology. The structure of the tetranuclear core in 1 consists of four crystallographically unique copper(II) ions in approximate square-pyramidal geometry with each coordinated to a bipy ligand and interacting through two mu(4)-O,O',O''-phosphate bridges. Additional bridging between Cu(3) and Cu(4) is provided by a hydroxide ligand, whereas two water molecules cap the Cu(1) and Cu(2) squ…

Models MolecularChemistryLigandInorganic chemistryTemperaturechemistry.chemical_elementChromophoreCrystallography X-RayCopperMagnetic susceptibilityIonInorganic ChemistryMagneticsCrystallographychemistry.chemical_compoundModels ChemicalIntramolecular forceOrganometallic CompoundsMoleculeHydroxideCopperDalton Transactions
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Thermal induced conformational changes involved in the aggregation pathways of beta-lactoglobulin.

2004

Aggregation of proteins appears to be associated most often with conformational and structural changes that lead to exposure of some apolar residues. Depending on the native structure of the protein in exam, aggregation is a process that involves different mechanisms, whose time of occurrence and interplay can depend upon temperature. To single out information about the multistages of the aggregation pathway, here we investigate the thermally induced conformational and structural changes of the beta-lactoglobulin (BLG). The experimental approach consists in studying steady-state fluorescence spectra of intrinsic chromophores, two tryptophans, and Anylino-Naphthalene-Sulfonate dye (ANS) mole…

Models MolecularCircular dichroismProtein DenaturationChemistryProtein ConformationSpectrum AnalysisOrganic ChemistryKineticsIntermolecular forceBiophysicsTemperatureLactoglobulinsProtein aggregationChromophoreCrystallography X-RayBiochemistryFluorescenceHydrophobic effectCrystallographyKineticsProtein structureBiophysicsDimerizationBiophysical chemistry
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Signal amplification and transduction in phytochrome photosensors

2014

[Introduction] Page 2 of 20 Sensory proteins must relay structural signals from the sensory site over large distances to regulatory output domains. Phytochromes are a major family of red-light sensing kinases that control diverse cell ular functions in plants, bacteria, and fungi. 1-9 Bacterial phytochro mes consist of a photosensory core and a C-te rminal regulatory domain. 10,11 Structures of photosensory cores are reported in the resting state 12-18 and conformational responses to light activat ion have been proposed in the vicinity of the chromophore. 19-23 However, the structure of the signalling state and the mechanism of downstream signal re lay through the photosensory core remain e…

Models MolecularLight Signal TransductionProtein ConformationCrystallography X-RayArticleProtein structureBacterial Proteinsmolecular biophysicsDeinococcusBinding siteCalcium signalingBinding SitesMultidisciplinarybiokemiabiologyPhytochrometa1182Deinococcus radioduransChromophorebiology.organism_classificationBiochemistryBiophysicsDeinococcusPhytochromeTransduction (physiology)röntgenkristallografiaNature
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Design of Triads for Probing the Direct Through Space Energy Transfers in Closely Spaced Assemblies

2013

Using a selective stepwise Suzuki cross-coupling reaction, two trimers built on three different chromophores were prepared. These trimers exhibit a D(^)A1-A2 structure where the donor D (octa-β-alkyl zinc(II)porphyrin either as diethylhexamethyl, 10a, or tetraethyltetramethyl, 10b, derivatives) through space transfers the S1 energy to two different acceptors, di(4-ethylbenzene) zinc(II)porphyrin (A1; acceptor 1) placed cofacial with D, and the corresponding free base (A2; acceptor 2), which is meso-meso-linked with A1. This structure design allows for the possibility of comparing two series of assemblies, 9a,b (D(^)A1) with 10a,b (D(^)Â1-A2), for the evaluation of the S1 energy transfer for…

Models MolecularMetalloporphyrinsChemistryEnergy transferMolecular Conformationchemistry.chemical_elementFree baseZincChromophoreSpace (mathematics)AcceptorPorphyrinFluorescenceInorganic ChemistryCrystallographychemistry.chemical_compoundEnergy TransferDrug DesignPhysical and Theoretical ChemistryAtomic physicsInorganic Chemistry
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Positional Isomers of Chromophore–Peptide Conjugates Self-Assemble into Different Morphologies

2018

Ordering π-systems into defined supramolecular structures is important for the development of organic functional materials. In recent years, peptides with defined secondary structures and/or self-assembly properties were introduced as powerful tools to order peptide-chromophore conjugates into different morphologies. This work explores whether or not the directionality of peptides can be used to control the self-assembly. The position of the π-system in conjugates between oligoprolines and perylene monoimide (PMI) chromophores was varied by attaching the PMI moiety to the second-to-last residue from the C- and N-termini, respectively. Microscopic and diffraction analysis revealed that the p…

Models MolecularNanostructurenanostructurepi interactionProtein ConformationNanofibersSupramolecular chemistry02 engineering and technologyImides010402 general chemistry01 natural sciencesCatalysissupramolecular chemistrychemistry.chemical_compoundIsomerismStructural isomerMoietyDirectionalityImidePeryleneChemistryOrganic ChemistryStereoisomerismGeneral Chemistryself-assemblyNanofiberChromophore021001 nanoscience & nanotechnology0104 chemical sciencesCrystallographyPeptideSelf-assemblyPeptides0210 nano-technologyPerylene
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Origins of fluorescence in evolved bacteriophytochromes

2014

Use of fluorescent proteins to study in vivo processes in mammals requires near-infrared (NIR) biomarkers that exploit the ability of light in this range to penetrate tissue. Bacteriophytochromes (BphPs) are photoreceptors that couple absorbance of NIR light to photoisomerization, protein conformational changes, and signal transduction. BphPs have been engineered to form NIR fluorophores, including IFP1.4, Wi-Phy, and the iRFP series, initially by replacement of Asp-207 by His. This position was suggestive because its main chain carbonyl is within hydrogen-bonding distance to pyrrole ring nitrogens of the biliverdin chromophore, thus potentially functioning as a crucial transient proton sin…

Models MolecularPhotoisomerizationNitrogenSurface PropertiesQuantum yieldCrystallography X-RayLigandsProtein EngineeringPhotochemistryBiochemistrychemistry.chemical_compoundparasitic diseasesSide chainAnimalsCloning MolecularneoplasmsMolecular BiologySpectroscopy Near-InfraredBiliverdinBacteriaPhytochromeChemistryBiliverdinetechnology industry and agricultureta1182WaterHydrogen BondingCell BiologyChromophoreequipment and suppliesFluorescenceProtein Structure Tertiarysurgical procedures operativeSpectrometry FluorescenceStructural biologySpectrophotometryProtein Structure and FoldingPhytochromeHydrophobic and Hydrophilic InteractionsBiomarkersProtein BindingJournal of Biological Chemistry
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Tips and turns of bacteriophytochrome photoactivation

2020

Phytochromes are ubiquitous photosensor proteins, which control the growth, reproduction and movement in plants, fungi and bacteria. Phytochromes switch between two photophysical states depending on the light conditions. In analogy to molecular machines, light absorption induces a series of structural changes that are transduced from the bilin chromophore, through the protein, and to the output domains. Recent progress towards understanding this structural mechanism of signal transduction has been manifold. We describe this progress with a focus on bacteriophytochromes. We describe the mechanism along three structural tiers, which are the chromophore-binding pocket, the photosensory module,…

Models MolecularProtein Conformation116 Chemical sciencesHISTIDINE KINASESSIGNAL-TRANSDUCTIONfotobiologiabacteriophytochrome photoactivation010402 general chemistry01 natural sciencesbakteeritPhytochrome B03 medical and health sciencesProtein structureBacterial ProteinsINDUCED PROTON RELEASEPHYTOCHROME-BCRYSTAL-STRUCTUREPhysical and Theoretical Chemistry030304 developmental biologyINDUCED CONFORMATIONAL-CHANGESPhysics0303 health sciencesRESONANCE RAMANMechanism (biology)AGROBACTERIUM-TUMEFACIENSPhotochemical ProcessesMolecular machine0104 chemical sciencesINFRARED FLUORESCENT PROTEINSCHROMOPHORE-BINDING DOMAINBiophysics1182 Biochemistry cell and molecular biologyvalokemiaproteiinitPhytochromeSignal TransductionPhotochemical & Photobiological Sciences
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The hairpin extension controls solvent access to the chromophore binding pocket in a bacterial phytochrome: a UV-vis absorption spectroscopy study.

2021

AbstractSolvent access to the protein interior plays an important role in the function of many proteins. Phytochromes contain a specific structural feature, a hairpin extension that appears to relay structural information from the chromophore to the rest of the protein. The extension interacts with amino acids near the chromophore, and hence shields the chromophore from the surrounding solvent. We envision that the detachment of the extension from the protein surface allows solvent exchange reactions in the vicinity of the chromophore. This can facilitate for example, proton transfer processes between solvent and the protein interior. To test this hypothesis, the kinetics of the protonation…

Models MolecularProtein ConformationProtonation010402 general chemistryPhotochemistry01 natural sciencespH jump03 medical and health scienceschemistry.chemical_compoundPhytochrome ADeprotonationBacterial ProteinsPhotostationary statePhysical and Theoretical Chemistrychromophore protein systems030304 developmental biology0303 health sciencesBiliverdinBinding SitesPhytochromeProtein dynamicsBiliverdineconformational substatesChromophoreHydrogen-Ion Concentrationsolvent gating0104 chemical sciencesKineticschemistryprotein dynamicsSolventsSpectrophotometry UltravioletproteiinitvalokemiaDeinococcusPhytochromeProtonsPhotochemicalphotobiological sciences : Official journal of the European Photochemistry Association and the European Society for Photobiology
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