Search results for "structural"

showing 10 items of 5047 documents

Estimation of the fatigue life of high strength steel under variable-amplitude tension with torsion: Use of the energy parameter in the critical plane

2003

Abstract The paper concerns application of the energy parameter, being a sum of the elastic and plastic strain energy density in the critical plane, for describing experimental data obtained in fatigue tests of 35NCD16 steel, subjected to constant amplitude tension-compression, torsion and variable amplitude tension-compression, torsion and combined proportional tension with torsion. It has been shown that the normal strain energy density in the critical plane is a suitable parameter for correlation of fatigue lives of 35NCD16 steel under considered kinds of loading. The critical plane is the plane where the normal strain energy density reaches its maximum value.

AmplitudeMaterials scienceEnergy parameterbusiness.industryEnergy densityHigh strength steelTorsion (mechanics)Strain energy density functionStructural engineeringMechanicsFracture planebusinessElastic and plastic strain
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Application of the Dang‐Van criterion for life determination under uniaxial random tension–compression with different mean values

2004

In this paper the experimental fatigue lives of specimens made of 10HNAP steel with the lives calculated with the Goodman and Gerber methods of cycle amplitude transformation and the Dang Van criterion for uniaxial loading are compared. Cycles were counted with the rain flow algorithm and damage was accumulated according to the Palmgren-Miner hypothesis. This paper includes comparison of the results for constant amplitude loading with a non-zero mean value and for random loading with zero or non-zero mean values. It has been shown that for 10HNAP steel the algorithm of fatigue life calculations using the Dang Van criterion gives satisfactory results.

AmplitudeMechanics of Materialsbusiness.industryTension compressionMechanical EngineeringMean valueLife timeGeneral Materials ScienceStructural engineeringUniaxial loadbusinessConstant (mathematics)MathematicsFatigue & Fracture of Engineering Materials & Structures
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Restoration of the Zisa Palace, Palermo

1993

The building of the Zisa, commissioned by William I, began in 1164-1165; it was completed by William II in the years immediately following. It was built as a splendid place for rest and amusement, ...

Amusementmedia_common.quotation_subject021105 building & construction0211 other engineering and technologies020101 civil engineering02 engineering and technologyBuilding and ConstructionArtAncient history0201 civil engineeringCivil and Structural Engineeringmedia_commonStructural Engineering International
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In vitro fibrillogenesis of the amyloid beta 1-42 peptide: cholesterol potentiation and aspirin inhibition.

2002

Understanding the formation of extracellular amyloid neurofibrillar bundles/senile plaques and their role in the development of Alzheimer's disease is of considerable interest to neuroscientists and clinicians. Major components of the extracellular neurofibrillar bundles are polymerized amyloid beta (Abeta) peptides (1-40), (1-42) and (1-43), derived in vivo from the soluble amyloid precursor protein (sAPP) by proteolytic (beta- and gamma-secretase) cleavage. The Abeta(1-42) peptide is widely considered to be of greatest significance in relation to the pathogenesis of Alzheimer's disease. A well-defined ultrastructural characteristic within Alzheimer dense plaques is the presence of helical…

AmyloidAmyloid betaGeneral Physics and AstronomyPeptideFibrilStructural BiologyAlzheimer DiseaseAmyloid precursor proteinAnimalsHumansGeneral Materials ScienceSenile plaqueschemistry.chemical_classificationAmyloid beta-PeptidesbiologyAspirinChemistryP3 peptideFibrillogenesisCell BiologyRatsSphingomyelinsMicroscopy ElectronCholesterolBiochemistrybiology.proteinlipids (amino acids peptides and proteins)PeptidesDimerizationCopperMicron (Oxford, England : 1993)
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Cholesterol binding to amyloid-β fibrils: A TEM study

2008

There is increasing interest in the role of brain cholesterol in Alzheimer's disease and the contribution of cholesterol to the formation of amyloid plaques. This paper presents a TEM study showing the binding of soluble approximately 10 nm diameter cholesterol-PEG 600 micelles to amyloid-beta(1-42) (Abeta(1-42)) fibrils formed either in the presence of this cholesterol derivative or to preformed fibrils generated under four different fibrillogenesis conditions. Specimens negatively stained with uranyl acetate revealed that during 24 h fibrillogenesis at 37 degrees C the cholesterol-PEG micelles bound periodically to Abeta(1-42) protofibrils and apparently also formed a thin smooth unbroken…

AmyloidAmyloid beta-PeptidesCholesterolCholesterol bindingGeneral Physics and AstronomyUranyl acetateFibrillogenesismacromolecular substancesCell BiologyFibrilNegative stainMicellePolyethylene GlycolsCrystallographychemistry.chemical_compoundCholesterolMicroscopy Electron TransmissionchemistryStructural BiologyHumanslipids (amino acids peptides and proteins)General Materials ScienceHydrogen peroxideMicellesMicron
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Kinetics of different processes in human insulin amyloid formation.

2007

Human insulin has long been known to form amyloid fibrils under given conditions. The molecular basis of insulin aggregation is relevant for modeling the amyloidogenesis process, which is involved in many pathologies, as well as for improving delivery systems, used for diabetes treatments. Insulin aggregation displays a wide variety of morphologies, from small oligomeric filaments to huge floccules, and therefore different specific processes are likely to be intertwined in the overall aggregation. In the present work, we studied the aggregation kinetics of human insulin at low pH and different temperatures and concentrations. The structure and the morphogenesis of aggregates on a wide range…

AmyloidAmyloidmedicine.medical_treatmentKineticsMicroscopy Atomic ForceFibrilModels BiologicalFluorescencechemistry.chemical_compoundlight-scatteringStructural Biologyamyloid fibrilMicroscopymedicineHumansInsulinScattering RadiationMicroscopy Phase-ContrastBenzothiazolesParticle SizeMolecular BiologyFluorescent Dyesatomic force microscopyInsulinaggregationTemperatureHydrogen-Ion ConcentrationKineticsThiazolesCrystallographyMonomerchemistryBiophysicsThioflavinElongation
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Design and synthesis of new trehalose-conjugated pentapeptides as inhibitors of Aβ(1-42) fibrillogenesis and toxicity

2009

Aggregation of the amyloid A? peptide and its accumulation into insoluble deposits (plaques) are believed to be the main cause of neuronal dysfunction associated with Alzheimer's disease (AD); small molecules that can interfere with the A? amyloid fibril formation are therefore of interest for a potential therapeutic strategy. Three new trehalose-conjugated peptides of the well known ?-sheet breaker peptide iA?5p,were synthesized. The disaccharide was covalently attached to different sites of the LPFFD peptide chain, i.e. at the N-terminus, C-terminus or at the Asp side chain. CD spectroscopy in different solvents was used to assess changes in the peptide conformation of these compounds. Th…

AmyloidCell SurvivalPeptideMicroscopy Atomic ForceBiochemistryMass Spectrometrychemistry.chemical_compoundbeta-sheet breaker peptideStructural BiologySFMmental disordersDrug DiscoveryAnimalsbeta-sheet breaker peptidesMolecular BiologyCells CulturedChromatography High Pressure LiquidtrehaloseCerebral CortexPharmacologychemistry.chemical_classificationthioflavin Tbeta-amyloidOrganic ChemistryP3 peptideFibrillogenesisGeneral MedicineTrehaloseSmall moleculeGlycopeptideNeuronal culturesRatsPeptide Conformationneuronal cultureBiochemistrychemistryMolecular MedicineAmyloid-betaPeptidesJournal of Peptide Science
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Polymorphism of amyloid-beta fibrils and its effects on human erythrocyte catalase binding.

2009

The Alzheimer's amyloid-beta (Abeta) peptide exists as a number of naturally occurring forms due to differential proteolytic processing of its precursor molecule. Many of the Abeta peptides of different lengths form fibrils in vitro, which often show polymorphisms in the fibril structure. This study presents a TEM based analysis of fibril formation by eighteen different Abeta peptides ranging in length from 5 to 43 amino acids. Spectrophotometric analysis of Congo red binding to the fibrillar material has been assessed and the binding of human erythrocyte catalase (HEC) to Abeta fibrils has also been investigated by TEM. The results show that a diverse range of Abeta peptides form fibrils a…

AmyloidErythrocytesGeneral Physics and AstronomyPeptidemacromolecular substancesPlasma protein bindingFibrilchemistry.chemical_compoundMicroscopy Electron TransmissionStructural BiologyHumansGeneral Materials Sciencechemistry.chemical_classificationbiologyStaining and LabelingCongo RedCell BiologyCatalaseIn vitroAmino acidCongo redPolymorphism (materials science)BiochemistrychemistryCatalaseSpectrophotometrybiology.proteinProtein BindingMicron (Oxford, England : 1993)
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Negative staining across holes: application to fibril and tubular structures.

2007

The negative staining technique, when used with holey carbon support films, presents superior imaging conditions than is the case when samples are adsorbed to continuous carbon films. A demonstration of this negative staining approach is presented, using ammonium molybdate in combination with trehalose, applied to several fibrillar and tubular samples. Fibrils formed from the amyloid-beta peptide and the protease inhibitor pepstain A spread very well unsupported across holes and the different polymorphic fibril forms can be readily assessed. However, tubular forms of amyloid-beta have a tendency to be flattened, due to surface tension forces prior to and during specimen drying. Sub-fibril a…

AmyloidMaterials scienceGeneral Physics and Astronomychemistry.chemical_elementFibrilNegative Stainingchemistry.chemical_compoundFerrihydriteMicroscopy Electron TransmissionStructural BiologyIron-Binding ProteinsPepstatinsAnimalsHumansNanotechnologyGeneral Materials ScienceAmmonium molybdateMolybdenumAmyloid beta-PeptidesProteinsTrehaloseCell BiologyDNATrehaloseNegative stainCarbonStainingRatsCrystallographyCarbon filmchemistryBiophysicsCollagenPeptidesCarbonMicron (Oxford, England : 1993)
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Cholesterol facilitates interactions between α‐synuclein oligomers and charge‐neutral membranes

2015

AbstractOligomeric species formed during α-synuclein fibrillation are suggested to be membrane-disrupting agents, and have been associated with cytotoxicity in Parkinson’s disease. The majority of studies, however, have revealed that the effect of α-synuclein oligomers is only noticeable on systems composed of anionic lipids, while the more physiologically relevant zwitterionic lipids remain intact. We present experimental evidence for significant morphological changes in zwitterionic membranes containing cholesterol, induced by α-synuclein oligomers. Depending on the lipid composition, model membranes are either unperturbed, disrupt, or undergo dramatic morphological changes and segregate …

AmyloidParkinson's diseaseFluorescent DyeBiophysicsPlasma protein bindingBiochemistryOligomerProtein Structure SecondaryMultiphoton microscopyMembrane phase separationCell membranechemistry.chemical_compoundGeneticStructural Biology2-NaphthylamineLaurdan fluorescenceGeneticsFluorescence microscopemedicineMolecular BiologyFluorescent DyesLaurateα-SynucleinMembranesChemistryMedicine (all)2-NaphthylamineCell MembraneMembraneCell BiologySettore FIS/07 - Fisica Applicata(Beni Culturali Ambientali Biol.e Medicin)CholesterolMembranemedicine.anatomical_structureBiophysicBiochemistryStructural biologyOligomeralpha-SynucleinParkinson’s diseaseProtein MultimerizationLaurdanLauratesProtein BindingFEBS Letters
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