Search results for "conformation"

showing 10 items of 1414 documents

Antibiotic as Ligand. Coordinating Behavior of the Cephalexin Towards Zn(II) and Cd(II) Ions

1987

The complex formation equilibria of Zn(II) and Cd(II) with cephalexin have been studied through potentiometric titrations. Experimental data were analyzed using the least squares computer program SUPERQUAD. The stability constants were 1g beta ZnCEX+ = 2.40, 1g beta Zn(CEX)(OH) = -4.54, 1g beta CdCEX+ = 2.18, and 1g beta Cd(CEX)(OH) = -5.18 (I = 0.1 M NaNO3), CEX complexes of formulae Zn(CEX)2(3)H2O and Cd(CEX)(OH)H2O have been synthesized and characterized by elemental analysis, IR spectra, conductivity measurements, and electronic and NMR spectra. The thermal behavior of the synthesized compounds were studied by TGA and DTA. We conclude that the metal ion interacts with the amido group of…

Models MolecularCephalexinBicyclic moleculeLigandChemistryPotentiometric titrationInorganic chemistryMolecular ConformationInfrared spectroscopyLigandsBiochemistryInorganic ChemistryNMR spectra databaseMetalZincStability constants of complexesvisual_artvisual_art.visual_art_mediumThermal stabilityCopperSoftwareNuclear chemistryJournal of Inorganic Biochemistry
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A New Heterogeneous Catalyst Obtained via Supramolecular Decoration of Graphene with a Pd2+ Azamacrocyclic Complex

2019

A new G-(H2L)-Pd heterogeneous catalyst has been prepared via a self-assembly process consisting in the spontaneous adsorption, in water at room temperature, of a macrocyclic H2L ligand on graphene (G) (G + H2L = G-(H2L)), followed by decoration of the macrocycle with Pd2+ ions (G-(H2L) + Pd2+ = G-(H2L)-Pd) under the same mild conditions. This supramolecular approach is a sustainable (green) procedure that preserves the special characteristics of graphene and furnishes an efficient catalyst for the Cu-free Sonogashira cross coupling reaction between iodobenzene and phenylacetylene. Indeed, G-(H2L)-Pd shows an excellent conversion (90%) of reactants into diphenylacetylene under mild conditio…

Models MolecularChemical PhenomenaIodobenzeneMolecular ConformationPharmaceutical ScienceSonogashira couplingLigands010402 general chemistryHeterogeneous catalysiscross coupling01 natural sciencesArticleCoupling reactionAnalytical Chemistrylaw.inventionCatalysislcsh:QD241-441chemistry.chemical_compoundlcsh:Organic chemistryCoordination ComplexeslawDrug DiscoveryPolymer chemistryPhysical and Theoretical ChemistryDiphenylacetyleneMolecular Structurecatalysis010405 organic chemistryGrapheneSpectrum AnalysisOrganic ChemistrySonogashirapalladium catalystHydrogen-Ion Concentrationsupramolecular interactions0104 chemical sciencesSolutionsazamacrocycleschemistryPhenylacetyleneChemistry (miscellaneous)surface adsorptionMolecular MedicineGraphitecatalysis palladium catalyst; Sonogashira graphenePalladiumMolecules
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Electron capture activation of the disulfide bond. The role of the asymmetry and electronegativity.

2010

The effects of electron capture on the structure of XSSX' disulfide derivatives in which the substituents attached to the sulfur atoms have different electronegativites have been investigated at different levels of theory, namely DFT, MP2, QCISD and CASSCF/CASPT2. Although it has been generally assumed that electron attachment to disulfide derivatives leads to a systematic and significant activation of the S-S bond, our results show that this is the case only when the substituents X or X' have low electronegativity. Otherwise, the S-S bond in the anion remains practically unperturbed and only the S-X bond is largely activated or even broken, because the extra electron occupies the sigma*(S-…

Models MolecularChemistryElectron captureBent molecular geometryMolecular ConformationGeneral Physics and Astronomychemistry.chemical_elementElectronsElectronAntibonding molecular orbitalSulfurElectron transport chainIonElectronegativityElectron TransportCrystallographyComputational chemistryQuantum TheoryDisulfidesPhysical and Theoretical ChemistryPhysical chemistry chemical physics : PCCP
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Protein NMR Structures Refined with Rosetta Have Higher Accuracy Relative to Corresponding X-ray Crystal Structures

2014

We have found that refinement of protein NMR structures using Rosetta with experimental NMR restraints yields more accurate protein NMR structures than those that have been deposited in the PDB using standard refinement protocols. Using 40 pairs of NMR and X-ray crystal structures determined by the Northeast Structural Genomics Consortium, for proteins ranging in size from 5-22 kDa, restrained Rosetta refined structures fit better to the raw experimental data, are in better agreement with their X-ray counterparts, and have better phasing power compared to conventionally determined NMR structures. For 37 proteins for which NMR ensembles were available and which had similar structures in solu…

Models MolecularChemistryProtein ConformationProtein Data Bank (RCSB PDB)X-rayProteinsGeneral ChemistryNuclear magnetic resonance crystallographyCrystal structureCrystallography X-RayBiochemistryCatalysisArticleStructural genomicsCrystalCrystallographyColloid and Surface ChemistryMolecular replacementComputer SimulationNuclear Magnetic Resonance BiomolecularSoftwareJournal of the American Chemical Society
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Crystal structure of lactitol (4-O-beta-D-galactopyranosyl-D-glucitol) dihydrate.

1992

Abstract Lactitol dihydrate, C 12 H 24 O 11 ·2H 2 O, is tetragonal, space group P 4 3 2 1 2 with cell dimensions a and b = 8.762(1), c = 45.500(3) A, and V = 3493.2(3) A 3 ; Z = 8, D x = 1.45 Mg.m −3 , λ(Cu- K α ) = 1.54056 A, μ = 1.108 mm −1 , F (000) = 1632, and T = 23°. The structure was solved by direct methods and refined by least-squares calculations to R = 0.054 for 2037 unique observed reflections. There are three intra- and twelve inter-molecular hydrogen bonds in the structure. Bond lengths and angles accord quite well with the mean values of related structures. The galactopyranosyl ring has a chair of conformation.

Models MolecularChemistryStereochemistryHydrogen bondOrganic ChemistryMolecular Sequence DataHydrogen BondingGeneral MedicineCrystal structureBiochemistryAnalytical ChemistryBond lengthTetragonal crystal systemCrystallographyMolecular geometrySugar AlcoholsCarbohydrate SequenceX-Ray DiffractionX-ray crystallographyCarbohydrate ConformationMoleculeHydrateSoftwareCarbohydrate research
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Ferromagnetic Cu(II)4, Co(II)4, and Ni(II)6 azido complexes derived from metal-assisted methanolysis of di-2,6-(2-pyridylcarbonyl)pyridine.

2009

Reaction of copper(II) perchlorate with di-2,6-(2-pyridylcarbonyl)pyridine (pyCOpyCOpy, dpcp) in the presence of sodium azide yields complex [Cu(4)(N(3))(2){pyC(OMe)(O)pyC(OMe)(O)py}(2)(MeOH)(2)](ClO(4)) x 2 MeOH (1 x 2 MeOH), which crystallizes in the monoclinic P2(1)/c space group. Similar reaction of cobalt(II) nitrate yields complex [Co(4)(N(3))(2)(NO(3))(2){pyC(OMe)(O)pyC(OMe)(O)py}(2)] x 0.5 MeOH (2 x 0.5 MeOH) which crystallizes in the monoclinic I2/m space group. Reaction of nickel(II) perchlorate yields complex [Ni(6)(CO(3))(N(3))(6){pyCOpyC(O)(OMe)py}(3)(MeOH)(2)(H(2)O)][Ni(6)(CO(3))(N(3))(6){pyCOpyC(O)(OMe)py}(3) (MeOH)(3)](ClO(4))(2) x 1.8 MeOH (3 x 1.8 MeOH), which crystallizes…

Models MolecularChemistryStereochemistryPyridinesCyclohexane conformationTemperaturechemistry.chemical_elementCobaltCrystallography X-RayMagnetic susceptibilityInorganic ChemistryPerchloratechemistry.chemical_compoundNickelCrystallographyMagneticsDeprotonationCubaneNickelPyridineOrganometallic CompoundsPhysical and Theoretical ChemistryCopperMonoclinic crystal systemInorganic chemistry
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Energy Transfer between Surface-Immobilized Light-Harvesting Chlorophyll a/b Complex (LHCII) Studied by Surface Plasmon Field-Enhanced Fluorescence S…

2010

The major light-harvesting chlorophyll a/b complex (LHCII) of the photosynthetic apparatus in green plants can be viewed as a protein scaffold binding and positioning a large number of pigment molecules that combines rapid and efficient excitation energy transfer with effective protection of its pigments from photobleaching. These properties make LHCII potentially interesting as a light harvester (or a model thereof) in photoelectronic applications. Most of such applications would require the LHCII to be immobilized on a solid surface. In a previous study we showed the immobilization of recombinant LHCII on functionalized gold surfaces via a 6-histidine tag (His tag) in the protein moiety. …

Models MolecularChlorophyll aProtein ConformationSurface PropertiesLight-Harvesting Protein ComplexesPhotochemistryFluorescence spectroscopyAbsorptionchemistry.chemical_compoundFluorescence Resonance Energy TransferElectrochemistryMoleculeGeneral Materials ScienceSpectroscopyFluorescent DyesSurface plasmonPeasSurfaces and InterfacesEnzymes ImmobilizedCondensed Matter PhysicsPhotobleachingFluorescenceAcceptorKineticsB vitaminschemistryLangmuir
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Triggering dissymmetry in achiral dye molecules by chiral solvents: Circular dichroism experiments and DFT calculations

2011

The electronic circular dichroism spectra of achiral product “Lumogen F Red” (ROT-300) in four different chiral solvents are recorded at different temperatures. DFT calculations allow to identify two enantiomeric conformers for ROT-300. In vacuo they are equally populated; in chiral solvents one enantiomer prevails. Thermodynamic quantities involved in the chiral preference are derived. Chirality, 2011. © 2011 Wiley-Liss, Inc.

Models MolecularCircular dichroismMolecular ConformationPhotochemistryCatalysisAnalytical ChemistryProchiralityComputational chemistryDrug Discoverycircular dichroism (CD)time-dependent density functional theory (TDDFT)MoleculeColoring AgentsConformational isomerismSpectroscopySettore CHIM/02 - Chimica FisicaPharmacologyChemistryCircular DichroismOrganic ChemistryStereoisomerismCircular dichroism spectradye molecules solvent effectSolventsQuantum TheoryEnantiomerChirality (chemistry)Chirality
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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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Combined effect of the DeltaPhe or DeltaAla residue and the p-nitroanilide group on a didehydropeptides conformation.

2007

Two series of dehydropeptides of the general formulae Boc-Gly-X-Phe-p-NA, Boc-Gly-Gly-X-Phe-p-NA, Gly-X-Gly-Phe-p-NA·TFA, and Boc-Gly-X-Gly-Phe-p-NA, with X = ΔZPhe and ΔAla, were studied with NMR in DMSO and CDCl3-DMSO, and with CD in MeOH, MeCN, and TFE. The NMR spectra measured in DMSO suggest that peptides with the ΔPhe residue next to Phe are folded whereas peptides with Gly between ΔPhe and Phe are less ordered. NMR spectra of ΔAla-containing peptides indicate that these peptides are flexible and their conformational equilibria are populated by many different conformations. The CD spectra show that conformational properties of the peptides studied are distinctly influenced by a mutual…

Models MolecularCircular dichroismanimal structuresMagnetic Resonance SpectroscopyStereochemistryProtein ConformationPhenylalanineBiophysicsBiochemistryBiomaterialsResidue (chemistry)Spectroscopy Fourier Transform InfraredAlanineCrystallographyintegumentary systemChemistryMutual positionCircular DichroismOrganic ChemistryGeneral MedicineDipeptidesAmidesNMR spectra databaseSolventCrystallographyModels Chemicalembryonic structuresX-ray crystallographyBiopolymers
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