Search results for "conformation"

showing 10 items of 1414 documents

Novel atrazine-binding biomimetics inspired to the D1 protein from the photosystem II of Chlamydomonas reinhardtii.

2020

Biomimetic design represents an emerging field for improving knowledge of natural molecules, as well as to project novel artificial tools with specific functions for biosensing. Effective strategies have been exploited to design artificial bioreceptors, taking inspiration from complex supramolecular assemblies. Among them, size-minimization strategy sounds promising to provide bioreceptors with tuned sensitivity, stability, and selectivity, through the ad hoc manipulation of chemical species at the molecular scale. Herein, a novel biomimetic peptide enabling herbicide binding was designed bioinspired to the D1 protein of the Photosystem II of the green alga Chlamydomonas reinhardtii. The D1…

Circular dichroismPhotosystem IIProtein ConformationSupramolecular chemistryPlastoquinoneChlamydomonas reinhardtiiPeptide02 engineering and technologyMolecular Dynamics SimulationBiochemistryFluorescence spectroscopy03 medical and health scienceschemistry.chemical_compoundStructural BiologyBiomimeticsAmino Acid SequencePhotosynthesisMolecular Biology030304 developmental biologychemistry.chemical_classification0303 health sciencesbiologyRational designphotosystem IIPhotosystem II Protein ComplexGeneral Medicine021001 nanoscience & nanotechnologybiology.organism_classificationSpectrometry FluorescencechemistryArtificial peptides Atrazine sensing Rational designBiophysicsThermodynamicsAtrazine0210 nano-technologyPeptidesChlamydomonas reinhardtiiInternational journal of biological macromolecules
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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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Bovine Serum Albumin protofibril-like aggregates formation: Solo but not simple mechanism

2011

We report an experimental study on the model protein Bovine Serum Albumin (BSA), with the aim of elucidating the mechanisms by which a fully folded globular protein undergoes different aggregation pathways leading to the formation of amyloid fibrils or amorphous aggregates. We observe thermally induced formation of fibrillar structures at pH far from the protein isoelectric point. The increase of electrostatic repulsion results in protein destabilization and in modifications of inter and intra-molecular interactions leading to the growth of fibril-like aggregates stabilized by inter-molecular-β sheets. The aggregation kinetics is studied by means of fluorescence techniques, light scattering…

Circular dichroismProtein ConformationGlobular proteinStatic ElectricityBiophysicsProtein aggregationBiochemistryprotein aggregation amyloid fibril fluorescence conformational changeschemistry.chemical_compoundProtein structureAnimalsBenzothiazolesBovine serum albuminMolecular Biologychemistry.chemical_classificationbiologyTemperatureTryptophanSerum Albumin BovineHydrogen-Ion ConcentrationSettore FIS/07 - Fisica Applicata(Beni Culturali Ambientali Biol.e Medicin)KineticsThiazolesCrystallographyIsoelectric pointchemistryProtein destabilizationbiology.proteinThermodynamicsCattleThioflavinProtein Multimerization
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Structural characterisation of the natural membrane-bound state of melittin: a fluorescence study of a dansylated analogue

1997

Abstract The binding of a dansylated analogue of melittin (DNC–melittin) to natural membranes is described. The cytolytic peptide from honey bee venom melittin was enzymatically labelled in its glutamine-25 with the fluorescent probe monodansylcadaverine using guinea pig liver transglutaminase. The labelled peptide was characterised functionally in cytolytic assays, and spectroscopically by circular dichroism and fluorescence. The behaviour of DNC–melittin was, in all respects, indistinguishable from that of the naturally occurring peptide. We used resonance energy transfer to measure the state of aggregation of melittin on the membrane plane in synthetic and natural lipid bilayers. When bo…

Circular dichroismProtein ConformationGlutamineGuinea PigsLipid BilayersBiophysicsPeptideHemolysiscomplex mixturesBiochemistryMelittinchemistry.chemical_compoundCadaverinePhosphatidylcholineAnimalsHumansLipid bilayerFluorescent Dyeschemistry.chemical_classificationBinding SitesTransglutaminasesCircular DichroismDansyl labelingtechnology industry and agricultureMembrane structureMelittinFluorescence energy transferCell BiologyMelittenFluorescenceSpectrometry FluorescenceMembraneEnergy TransferLiverBiochemistrychemistryBiophysicslipids (amino acids peptides and proteins)Natural membraneLipid-protein interactionProtein BindingBiochimica et Biophysica Acta (BBA) - Biomembranes
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HPLC study on the ‘history’ dependence of gramicidin A conformation in phospholipid model membranes

1989

AbstractA novel HPLC methodology for the study of gramicidin A reconstituted in model membranes has been tested in comparison with circular dichroism data. It is shown that this chromatographic technique not only corroborates most of the recent spectroscopic results but allows one to explain them in terms of mass fractions of different actual conformational species of GA in the phospholipid assemblies. In particular, the dependence of the inserted peptide configuration on the organic solvent and other parameters involved in the ‘history’ of the sample preparation and handling has been analyzed by HPLC in two phospholipid model systems: small unilamellar vesicles and micelles. Moreover, a sl…

Circular dichroismProtein ConformationMolecular ConformationBiophysicsPhospholipidPeptideBiochemistryHigh-performance liquid chromatographyMicellechemistry.chemical_compoundStructural BiologyGramicidin A conformationGeneticsGramicidin ASample preparationMolecular BiologyChromatography High Pressure Liquidchemistry.chemical_classificationChromatographyChemistryCircular DichroismGramicidinMembranes ArtificialCell BiologyModels TheoreticalCDMembraneLiposomesPhospholipid vesiclePhosphatidylcholinesHPLCFEBS Letters
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Calorimetric and structural investigation of the interaction between bovine serum albumin and high molecular weight dextran in water.

2005

This work studies specific interactions between a small globular protein and a highly flexible, branched polysaccharide using differential scanning calorimetry (DSC), circular dichroism (CD), fluorescence, and turbidimetry measurements. It uses the system water/bovine serum albumin (BSA)/dextran (D 2000) as a model. Dextran molecules are able to form interpolymeric complexes with BSA in water at both low and high temperatures if the polysaccharide is in excess and if the protein exists in its associated state. It leads to a partial destabilization of the secondary and tertiary structures of the protein and an additional exposure of the hydrophobic tryptophan residues to the surface of globu…

Circular dichroismProtein DenaturationProtein FoldingPolymers and PlasticsGlobular proteinMacromolecular SubstancesPolymersProtein ConformationUltraviolet RaysSerum albuminBioengineeringBiocompatible MaterialsCalorimetryProtein Structure SecondaryBiomaterialschemistry.chemical_compoundProtein structureNephelometry and TurbidimetryPolysaccharidesMaterials TestingMaterials ChemistryAnimalsBovine serum albuminchemistry.chemical_classificationChromatographybiologyCalorimetry Differential ScanningChemistryCircular DichroismTemperatureWaterDextransSerum Albumin BovineProtein Structure TertiaryDextranSpectrometry FluorescenceCalibrationbiology.proteinThermodynamicsProtein foldingCattleTurbidimetryBiomacromolecules
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Ferricytochrome c encapsulated in silica nanoparticles: structural stability and functional properties.

2004

Using a modified sol-gel technique, we have succeeded in encapsulating ferric cytochrome c in silica nanoparticles obtained from hydrolysis and polycondensation of tetramethylorthosilicate. Particles dimensions have been determined with dynamic light scattering; this technique yields an hydrodynamic radius of about 100 nm, each nanoparticle containing about 10(2)-10(3) proteins. If stored in the cold at low ionic strength, nanoparticles are stable for more than one week, even if a slow radius increase with time is observed. CD measurements show that encapsulated proteins exhibit substantially increased stability against guanidinium hydrochloride induced denaturation. Reduction kinetics of e…

Circular dichroismSiliconHydrodynamic radiusTime FactorsLightProtein ConformationBiophysicsNanoparticleBiosensing TechniquesDithioniteLigandsBiochemistryBiomaterialsSodium dithionitechemistry.chemical_compoundDynamic light scatteringmedicineAnimalsScattering RadiationDenaturation (biochemistry)HorsesGuanidineIonsCarbon MonoxideChromatographyDose-Response Relationship DrugMyoglobinCircular DichroismHydrolysisSilicatesOrganic ChemistryCytochromes cWaterGeneral MedicineKineticschemistryChemical engineeringSol-gel process Sol-gels scanning electronFerricmedicine.drugBiopolymers
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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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Metal NHC Complexes with Naphthalimide Ligands as DNA-Interacting Antiproliferative Agents

2017

Naphthalimide-based N-heterocyclic carbene (NHC) complexes of the type [(1,5-cyclooctadiene)(NHC)RhCl)] (4 a-c), [(p-cymene)(NHC)RuCl2 )] (5 a-c), and [(NHC)CuBr] (6 a-c) were synthesized and investigated as antiproliferative agents that target DNA. The cytotoxic effects were largely driven by the naphthalimide structure, which is a DNA-intercalating moiety. Regarding the metal center, the highest activities were observed with the rhodium complexes, and cytotoxic activity was significantly lower for the ruthenium derivatives. The stable coordination of the NHC ligands of selected complexes 4 b and 5 b in solution was confirmed, and their DNA binding properties were studied by UV/Vis spectro…

Circular dichroismStereochemistryIntercalation (chemistry)Molecular Conformationchemistry.chemical_elementApoptosisCrystallography X-RayLigands010402 general chemistry01 natural sciencesBiochemistryRhodiumMetalchemistry.chemical_compoundDrug StabilityCoordination ComplexesDrug DiscoveryHumansMoietyGeneral Pharmacology Toxicology and PharmaceuticsrutheniumCell ProliferationPharmacology010405 organic chemistryChemistryCircular DichroismOrganic ChemistryDNAnaphthalimideIntercalating Agentsanticancer agent0104 chemical sciencesRutheniumcarbeneNaphthalimidesSettore CHIM/03 - Chimica Generale E Inorganicacoppervisual_artrhodiumMCF-7 CellsMonoterpenesvisual_art.visual_art_mediumCymenesMolecular MedicineSpectrophotometry UltravioletHT29 CellsMethaneCarbeneDNAChemMedChem
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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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