Search results for "dimer"

showing 10 items of 558 documents

Effects of succinylation on thermal induced amyloid formation in Concanavalin A.

2007

We have recently shown that upon slight thermal destabilization the legume lectin Concanavalin A may undergo two different aggregation processes, leading, respectively, to amyloid fibrils at high pH and amorphous aggregates at low pH. Here we present an experimental study on the amyloid aggregation of Succinyl Concanavalin A, which is a dimeric active variant of Concanavalin. The results show that, as for the native protein, the fibrillation process appears to be favoured by alkaline pH, far from the isoelectric point of the protein. Moreover, it strongly depends on temperature and requires large conformational changes both at secondary and tertiary structure level. With respect to the nati…

Circular dichroismAmyloidProtein DenaturationAmyloidbiologyChemistryCircular DichroismBiophysicsLegume lectinGeneral MedicineProtein aggregationHydrogen-Ion ConcentrationProtein tertiary structureProtein Structure SecondaryProtein Structure Tertiaryprotein aggregationSuccinylationIsoelectric pointBiochemistryConcanavalin Abiology.proteinConcanavalin AThermodynamicsDimerizationHydrophobic and Hydrophilic Interactions
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Characterization of gramicidin A in an inverted micellar environment. A combined high-performance liquid chromatographic and spectroscopic study

1992

We have investigated the conformational adaptability of gramicidin A incorporated into reverse micelles of sodium bis(2-ethylhexyl)sulfosuccinate (AOT)/isooctane/water, a so far unexplored "host" membrane-mimetic model system for this peptide. A high-performance liquid chromatographic strategy previously developed for the study of gramicidin in phospholipid vesicles and normal micelles [Bañó et al. (1989) FEBS Lett. 250, 67; Bañó et al. (1991) Biochemistry 30, 886] has been successfully extended to this system. The method has permitted the separation of peptide conformational species, namely, double-stranded dimers and monomers, and an accurate quantitation of their proportion in the invert…

Circular dichroismChemical PhenomenaMacromolecular SubstancesProtein ConformationDimerMolecular Sequence DataSynthetic membraneFluorescence PolarizationPeptideBiochemistryMicelleDissociation (chemistry)chemistry.chemical_compoundAmino Acid SequenceChromatography High Pressure LiquidMicelleschemistry.chemical_classificationDioctyl Sulfosuccinic AcidChromatographyChemistry PhysicalCircular DichroismSpectrum AnalysisGramicidinSpectrometry FluorescenceMonomerchemistryGramicidinBiochemistry
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A semi-empirical approach for the simulation of circular dichroism spectra of gramicidin A in a model membrane

1992

In an extension of our previous work (Bañó, M. C., Braco, L., and Abad, C. 1991. Biochemistry. 30:886-94), the kinetics of dissociation of gramicidin A double-stranded dimers into beta 6.3-helical monomers in small unilamellar vesicles prepared following different protocols, were investigated using in combination circular dichroism (CD) and high-performance liquid chromatography (HPLC). The analysis of the data from both techniques according to a two-component model strongly supports that any given CD pattern of gramicidin incorporated in the phospholipid bilayer can be deconvoluted essentially as a linear combination of the reference subspectra calculated for the double-stranded dimer and …

Circular dichroismProtein ConformationChemistryCircular DichroismDimerLipid BilayersGramicidinSynthetic membraneBiophysicsMembranes ArtificialBiophysical PhenomenaDissociation (chemistry)KineticsCrystallographychemistry.chemical_compoundMembraneMonomerModels ChemicalGramicidinLipid bilayerResearch ArticleBiophysical Journal
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Environment- and sequence-dependent modulation of the double-stranded to single-stranded conformational transition of gramicidin A in membranes.

1998

The role of the membrane lipid composition and the individual Trp residues in the conformational rearrangement of gramicidin A along the folding pathway to its channel conformation has been examined in phospholipid bilayers by means of previously described size-exclusion high-performance liquid chromatography HPLC-based strategy (Bano et al. (1991) Biochemistry 30, 886). It has been demonstrated that the chemical composition of the membrane influences the transition rate of the peptide rearrangement from double-stranded dimers to beta-helical monomers. The chemical modification of Trp residues, or its substitution by the more hydrophobic residues phenylalanine or naphthylalanine, stabilized…

Circular dichroismStereochemistryProtein ConformationDimerPhenylalanineEnterococcus faeciumLipid BilayersMolecular Sequence DataPeptideMicrobial Sensitivity TestsBiochemistrychemistry.chemical_compoundProtein structureAmino Acid SequencePeptide sequenceChromatography High Pressure Liquidchemistry.chemical_classificationChemistryCholestenesCircular DichroismGramicidinTryptophanFolding (chemistry)MembraneSpectrometry FluorescenceAmino Acid SubstitutionGramicidinFatty Acids UnsaturatedPhosphatidylcholinesDimerizationBiochemistry
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Size-exclusion high-performance liquid chromatography in the study of the autoassociating antibiotic gramicidin A in micellar milieu.

2003

Gramicidin A (gA) is a polypeptide antibiotic which forms dimeric channels specific for monovalent cations in biological membranes. It is a polymorphic molecule that adopts several different conformations, double-stranded (ds) helical dimers (pore conformation) and single-stranded beta-helical dimers (channel conformation). This study investigated the conformational adaptability of gramicidin A when incorporated into micelles as membrane-mimetic model system. Taking advantage of our reported, versatile, size-exclusion high-performance liquid chromatography (SE-HPLC) strategy that allows the separation of double-stranded dimers and monomers, we have quantitatively characterized the conformat…

Circular dichroismStereochemistryProtein ConformationSize-exclusion chromatographyBiophysicsPeptideBiochemistryMicellechemistry.chemical_compoundMembrane LipidsSurface-Active AgentsProtein structureBiomimetic MaterialsColloidsChromatography High Pressure LiquidMicelleschemistry.chemical_classificationCircular DichroismGramicidinBiological membraneMembranes ArtificialCombinatorial chemistryAnti-Bacterial AgentsMembraneMonomerchemistryChromatography GelDimerizationJournal of biochemical and biophysical methods
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Fragmentation of gold clusters stored in a penning trap

1994

The collision-induced dissociation of positively charged gold clusters (2 to 23 atoms) stored in a Penning trap has been studied. After collisions with rare gases, excited clusters predominantly decay by emission of one or two atoms. The loss of two atoms occurs most likely through the emission of a dimer rather than a sequential evaporation. The minimum kinetic energies of clusters required to induce dissociation exhibit a pronounced odd-even effect. Clusters with an even number of delocalized electrons are more stable than the odd ones.

Condensed Matter::Quantum GasesGold clusterDimerOrganic ChemistryAnalytical chemistryPenning trapMolecular physicsBond-dissociation energyDissociation (chemistry)Analytical Chemistrychemistry.chemical_compoundDelocalized electronchemistryFragmentation (mass spectrometry)Excited statePhysics::Atomic and Molecular ClustersPhysics::Atomic PhysicsSpectroscopyRapid Communications in Mass Spectrometry
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Aryl hydrocarbon receptor activation by cAMP vs. dioxin: divergent signaling pathways.

2005

Even before the first vertebrates appeared on our planet, the aryl hydrocarbon receptor ( AHR ) gene was present to carry out one or more critical life functions. The vertebrate AHR then evolved to take on functions of detecting and responding to certain classes of environmental toxicants. These environmental pollutants include polycyclic aromatic hydrocarbons (e.g., benzo[ a ]pyrene), polyhalogenated hydrocarbons, dibenzofurans, and the most potent small-molecular-weight toxicant known, 2,3,7,8-tetrachlorodibenzo- p -dioxin (TCDD or dioxin). After binding of these ligands, the activated AHR translocates rapidly from the cytosol to the nucleus, where it forms a heterodimer with aryl hydroc…

Conservation of Natural ResourcesAryl hydrocarbon receptor nuclear translocatorPolychlorinated DibenzodioxinsTime FactorsTranscription GeneticGenetic VectorsGreen Fluorescent ProteinsImmunoblottingActive Transport Cell NucleusEnvironmentDioxinsLigandschemistry.chemical_compoundMiceCytosolGenes ReporterCell Line TumorCyclic AMPAnimalsImmunoprecipitationReceptorFluorescent Antibody Technique IndirectCell NucleusMultidisciplinarybiologyChemistryColforsinEndogenous mediatorrespiratory systemBiological SciencesAryl hydrocarbon receptorCyclic AMP-Dependent Protein KinasesCytosolProtein TransportBiochemistryBucladesineMicroscopy FluorescenceReceptors Aryl HydrocarbonSecond messenger systembiology.proteinProstaglandinsEnvironmental PollutantsSignal transductionDimerizationToxicantPlasmidsProtein BindingSignal TransductionProceedings of the National Academy of Sciences of the United States of America
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Coordination polymers based on bridging cyanocarbanions and bis-tridentate p-phenylenediamine ligands

2017

Two new Cu(II) coordination polymeric neutral chains of formula [Cu 2 (1,4-tpbd)(μ-A) 2 (H 2 O) 2 ](A) 2 with A = tcnoet − ( 1 ) and tcnopr − ( 2 ) (1,4-tpbd =  N,N,N′N′ -tetrakis(2-pyridylmethyl)benzene-1,4-diamine, tcnoet −  = 1,1,3,3-tetracyano-2-ethoxypropenide and tcnopr −  = 1,1,3,3-tetracyano-2-propoxypropenide) have been synthesized and characterized by infrared spectroscopy, X-ray diffraction and magnetic measurements. 1  and  2 show alternating chains where the 1,4-tpbd and the cyanocarbanion units (tcnoet − for 1 and tcnopr − for 2 ) alternate as bridging ligands. The molecular structure can be viewed as [Cu 2 (μ-tpbd)] 4+ dinuclear units (with Cu⋯Cu distances of 8.2233(3) for 1 …

Coordination polymerStereochemistryDimerInfrared spectroscopy010402 general chemistry01 natural sciencesInorganic Chemistrychemistry.chemical_compoundMagnetic interactionsMaterials ChemistryAntiferromagnetismMolecule[CHIM]Chemical Sciences[CHIM.COOR]Chemical Sciences/Coordination chemistryCoordination polymerPhysical and Theoretical ChemistryPolypyridyl ligand010405 organic chemistryLigandCopper complexp-PhenylenediaminePolypyridyl copper complexesMagnetic susceptibility3. Good health0104 chemical sciencesCrystallographychemistry
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Synthesis and characterization of vanadyl(IV) complexes of Schiff bases derived from anthranilic acid and salicylaldehyde (or its derivatives) or ace…

1997

Anhydrous, dimeric vanadyl(IV) complexes of Schiff bases derived from [1+1] condensation of salicylaldehyde (or its derivatives) and anthranilic acid, have been synthesized from CH3CN and were characterized by elemental analysis, FTIR, EPR, absorption, TGA, cyclic voltammetry and room temperature magnetic susceptibility measurements. These complexes were found to be oxidized by air in polar solvents like MeOH and DMF to V-V products. The E(1/2) values were found to be around 660 mV indicating that the carboxylate group favours vanadyl(IV) binding when compared to the alkoxo-bound vanadium complexes. Oxidative instability of these complexes are dependent on the substituent on the salicylalde…

Coordination sphereAcetylacetoneDimeric Vanadyl(Iv)Inorganic chemistryDecavanadateVanadiumchemistry.chemical_elementRedoxSingle Crystal X-RayInorganic Chemistrychemistry.chemical_compoundOxidationPyridinePolymer chemistryMaterials ChemistryAnthranilic acidPhysical and Theoretical ChemistrySchiff BasesSchiff baseReactivityVanadiumBindingMononuclear Octahedral Vo3+chemistrySalicylaldehydeDecavanadatesPyridiniumOxidative InstabilityOxovanadium(Iv)Polyhedron
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Three-dimensional structure of hepatitis B virus core particles determined by electron cryomicroscopy

1994

Human hepatitis B virus core protein expressed in E. coli assembles into two sizes of particle. We have determined their three-dimensional structures by electron cryomicroscopy and image processing. The large and small particles correspond to triangulation number T = 4 and T = 3 dimer clustered packings, containing 240 and 180 protein subunits, respectively. The local packing of subunits is very similar in the two sizes of particle and shows holes or channels through the shell. The native viral core particle packages RNA and is active in reverse transcription to DNA. The holes we observe may provide access for the necessary small molecules. Shells assembled from the intact core protein cont…

CryopreservationHepatitis B virusProtein ConformationCryo-electron microscopyProtein subunitDimerShell (structure)RNABiologyHepatitis B Core AntigensVirologyRecombinant ProteinsGeneral Biochemistry Genetics and Molecular BiologyMicroscopy Electronchemistry.chemical_compoundCrystallographyProtein structurechemistryEscherichia coliImage Processing Computer-AssistedHumansParticleDNACell
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