Search results for "Photometry"

showing 10 items of 797 documents

The Role of Adenine Excimers in the Photophysics of Oligonucleotides

2009

Energies and structures of different arrangements of the stacked adenine homodimer have been computed at the ab initio CASPT2 level of theory in isolation and in an aqueous environment. Adenine dimers are shown to form excimer singlet states with different degrees of stacking and interaction. A model for a 2-fold decay dynamics of adenine oligomers can be supported in which, after initial excitation in the middle UV range, unstacked or slightly stacked pairs of nucleobases will relax by an ultrafast internal conversion to the ground state, localizing the excitation in the monomer and through the corresponding conical intersection with the ground state. On the other hand, long-lifetime intra…

Models MolecularPhotochemistryUltraviolet RaysMolecular ConformationOligonucleotidesAb initioPhotochemistryExcimerBiochemistryCatalysisNucleobaseColloid and Surface ChemistryUltrafast laser spectroscopySinglet stateQuantitative Biology::BiomoleculesChemistryAdenineDNAGeneral ChemistryConical intersectionInternal conversion (chemistry)Chemical physicsNucleic Acid ConformationSpectrophotometry UltravioletGround stateDimerizationHydrogenJournal of the American Chemical Society
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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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Singlet Excited-State Interactions in Naphthalene-Thymine Dyads

2004

Two thymidine-derived nucleosides 1 and 2 were prepared by attaching a chiral naphthalene to the positions 5′ and 3′ of the sugar. The resulting dyads, which contain key substructures present in drugs and nucleic acids, exhibit different spatial arrangements (transoid or cisoid) of the fluorophore relative to the thymine unit. Emission measurements on these compounds in the presence of ROH molecules revealed a remarkable intramolecular fluorescence quenching for dyad 1. The obtained results are consistent with quenching of the singlet excited state of 1 by hydrogen-bond donor solvents. Thus, a physical deactivation process (vibronically induced internal conversion) would be the pathway resp…

Models MolecularPhotolysisQuenching (fluorescence)ChemistryLasersMolecular ConformationNaphthalenesCrystallography X-RayInternal conversion (chemistry)PhotochemistryFluorescenceAtomic and Molecular Physics and OpticsThyminechemistry.chemical_compoundSpectrometry FluorescenceIntersystem crossingIntramolecular forceExcited stateSpectrophotometry UltravioletSinglet statePhysical and Theoretical ChemistryThymineChemPhysChem
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A Ser residue influences the structure and stability of a Pro-kinked transmembrane helix dimer

2012

AbstractWhen localized adjacent to a Pro-kink, Thr and Ser residues can form hydrogen bonds between their polar hydroxyl group and a backbone carbonyl oxygen and thereby modulate the actual bending angle of a distorted transmembrane α-helix. We have used the homo-dimeric transmembrane cytochrome b559′ to analyze the potential role of a highly conserved Ser residue for assembly and stabilization of transmembrane proteins. Mutation of the conserved Ser residue to Ala resulted in altered heme binding properties and in increased stability of the holo-protein, most likely by tolerating subtle structural rearrangements upon heme binding. The results suggest a crucial impact of an intrahelical Ser…

Models MolecularProlineHeme bindingStereochemistryDimerMolecular ConformationBiophysicsCofactor bindingHemeBiochemistryProtein Structure Secondarychemistry.chemical_compoundProtein structureProtein stabilitySerineProtein foldingCofactor bindingHydrogen bondCell MembranePhotosystem II Protein ComplexHydrogen BondingCell BiologyCytochrome b GroupTransmembrane proteinProtein Structure TertiaryOxygenTransmembrane domainHelix interactionchemistrySpectrophotometryMembrane proteinMutationTransmembrane helixProtein foldingDimerizationProtein BindingBiochimica et Biophysica Acta (BBA) - Biomembranes
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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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Evidence for Water-Tuned Structural Differences in Proteins: An Approach Emphasizing Variations in Local Hydrophilicity

2012

We present experimental evidence for the significant effect that water can have on the functional structure of proteins in solution. Human (HSA) and Bovine Serum Albumin (BSA) have an amino acid sequence identity of 75.52% and are chosen as model proteins. We employ EPR-based nanoscale distance measurements using double electron-electron resonance (DEER) spectroscopy and both albumins loaded with long chain fatty acids (FAs) in solution to globally (yet indirectly) characterize the tertiary protein structures from the bound ligands' points of view. The complete primary structures and crystal structures of HSA and as of recently also BSA are available. We complement the picture as we have re…

Models MolecularProtein StructureMedical PhysicsNon-Clinical MedicineProtein ConformationMaterials ScienceBiophysicsMolecular Conformationlcsh:MedicineElectronsLigandsBiochemistryPhysical ChemistryAnalytical ChemistryMacromolecular Structure AnalysisAnimalsHumanslcsh:ScienceBiologySerum AlbuminQuantum MechanicsPhysicslcsh:RFatty AcidsElectron Spin Resonance SpectroscopyProteinsComputational BiologyWaterSerum Albumin BovineProtein Structure Tertiarybody regionsChemistrySpectrophotometryInterdisciplinary PhysicsMedicinelcsh:QMaterials CharacterizationCattleMedicinal ChemistryHydrophobic and Hydrophilic InteractionsResearch ArticleProtein BindingPLoS ONE
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A quantum-chemical study of the structure, vibrations and SiH bond properties of disilylamine, NH(SiH3)2.

2002

Quantum-chemical calculations at HF, MP2 and B3LYP levels with 6-31G* and 6-311G** basis sets are reported for disilylamine, NH(SiH3)2. The equilibrium structure is found to vary with both level and basis set, all but one of the structures exhibiting a small lack of planarity of the HNSi2 system. The barrier to inversion, however, is found to be very low, at most 38 cm(-1). Vibration frequencies and intensities are calculated. The frequencies are scaled, where possible, either using updated infrared data or with the aid of factors transferred from N(CH3)(SiH3)2. Unobserved frequencies due to the v(s)NSi2, deltaNSi2 and delta(perpendicular)NH modes are predicted near 610, 210 and 360 cm(-1),…

Models MolecularSiliconSpectrophotometry InfraredChemistrySilicon CompoundsBiophysicsInfrared spectroscopyHydrogen atomHyperconjugationSpectrum Analysis RamanPotential energyAtomic and Molecular Physics and OpticsBiophysical PhenomenaAnalytical Chemistrysymbols.namesakesymbolsQuantum TheoryAtomic physicsInstrumentationMulliken population analysisSpectroscopyBasis setRaman scatteringNatural bond orbitalSpectrochimica acta. Part A, Molecular and biomolecular spectroscopy
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Multinuclear Cytotoxic Metallodrugs: Physicochemical Characterization and Biological Properties of Novel Heteronuclear Gold-Titanium Complexes

2011

An unprecedented series of titanocene-gold bi- and trimetallic complexes of the general formula [[(η(5)-C(5)H(5))(μ-η(5):κ(1)-C(5)H(4)(CH(2))(n)PPh(2))TiCl(2)](m)AuCl(x)](q+) (n = 0, 2, or 4; m = 1, x = 1, q = 0 or m = 2, x = 0, q = 1) have been prepared and characterized spectroscopically. The luminescence spectroscopy and photophysics of one of the compounds, [[(η(5)-C(5)H(5))(μ-η(5):κ(1)-C(5)H(4)PPh(2))TiCl(2)](2)Au]PF(6), have been investigated in 2MeTHF solution and in the solid state at 77 and 298 K. Evidence for interfragment interactions based on the comparison of electronic band positions and emission lifetimes, namely, triplet energy transfer (ET) from the Au- to the Ti-containing…

Models MolecularSpectrometry Mass Electrospray IonizationLuminescenceMagnetic Resonance SpectroscopyTransfer Excited-StatesCell SurvivalStereochemistryAntineoplastic AgentsCharge-TransferUnsaturated-HydrocarbonsCrystallography X-RayElectronic-StructuresInorganic ChemistryStructure-Activity Relationshipchemistry.chemical_compoundCell Line TumorOrganometallic CompoundsHumansPhysical and Theoretical ChemistrySpectroscopyGroup 2 organometallic chemistryTitaniumArene-Ruthenium ComplexesX-rayTitanocene dichlorideNuclear magnetic resonance spectroscopyChromophoreTitanocene DichlorideCrystallographychemistryHeteronuclear moleculeAnticancer AgentsSpectrophotometry UltravioletGoldLuminescenceGold(Iii) CompoundsPhotophysical Properties
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Oxidative DNA cleavage induced by an iron(III) flavonoid complex: synthesis, crystal structure and characterization of chlorobis(flavonolato)(methano…

2006

A flavonol iron(III) complex, [Fe(flavonolato)(2)Cl(MeOH)], has been prepared. The compound has been characterized by X-ray crystallography, spectroscopy, magnetism and electronic paramagnetic resonance (EPR) at X- and Q-band. The geometrical environment around the metal is best described as rhombic distorted octahedral. This distortion has also been inferred from the magnetic measurements and from the EPR spectra at different temperatures, E/D(rhombicity parameter) approximately 0.06. The DNA cleavage activity of the iron(III) complex with and without ascorbate/hydrogen peroxide is reported. Mechanisms of the oxidative cleavage have been proposed when DNA strand scission is performed both …

Models MolecularSpectrophotometry InfraredCrystal structurePhotochemistryCrystallography X-RayBiochemistryFerric Compoundslaw.inventionInorganic ChemistryMetalchemistry.chemical_compoundParamagnetismlawMoleculeElectron paramagnetic resonanceHydrogen peroxideBond cleavageMolecular StructureChemistryElectron Spin Resonance SpectroscopyDNAResonance (chemistry)CrystallographyOxidative Stressvisual_artvisual_art.visual_art_mediumSpectrophotometry UltravioletJournal of inorganic biochemistry
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Vibrational spectrum of the spin crossover complex [Fe(phen)(2)(NCS)(2)] studied by IR and Raman spectroscopy, nuclear inelastic scattering and DFT c…

2006

The vibrational modes of the low-spin and high-spin isomers of the spin crossover complex [Fe(phen)(2)(NCS)(2)] (phen = 1,10-phenanthroline) have been measured by IR and Raman spectroscopy and by nuclear inelastic scattering. The vibrational frequencies and normal modes and the IR and Raman intensities have been calculated by density functional methods. The vibrational entropy difference between the two isomers, DeltaS(vib), which is--together with the electronic entropy difference DeltaS(el)--the driving force for the spin-transition, has been determined from the measured and from the calculated frequencies. The calculated difference (DeltaS(vib) = 57-70 J mol(-1) K(-1), depending on the m…

Models MolecularSpectrophotometry InfraredNitrogenAnalytical chemistryGeneral Physics and AstronomyInfrared spectroscopyInelastic scatteringIron Chelating AgentsSpectrum Analysis RamanMolecular physicsHot bandsymbols.namesakeIsomerismNormal modeSpin crossoverFerrous CompoundsPhysics::Chemical PhysicsPhysical and Theoretical ChemistryElectronic entropyChemistryMolecular vibrationsymbolsThermodynamicsSpin LabelsRaman spectroscopyMathematicsPhenanthrolinesPhysical chemistry chemical physics : PCCP
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